DMBT1_HUMAN
ID DMBT1_HUMAN Reviewed; 2413 AA.
AC Q9UGM3; A6NDG4; A6NDJ5; A8E4R5; B1ARE7; B1ARE8; B1ARE9; B1ARF0; B7Z8Y2;
AC F8WEF7; Q59EX0; Q5JR26; Q6MZN4; Q96DU4; Q9UGM2; Q9UJ57; Q9UKJ4; Q9Y211;
AC Q9Y4V9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Deleted in malignant brain tumors 1 protein;
DE AltName: Full=Glycoprotein 340;
DE Short=Gp-340;
DE AltName: Full=Hensin;
DE AltName: Full=Salivary agglutinin;
DE Short=SAG;
DE AltName: Full=Surfactant pulmonary-associated D-binding protein;
DE Flags: Precursor;
GN Name=DMBT1 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:2926};
GN Synonyms=GP340;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION AS A TUMOR SUPPRESSOR,
RP TISSUE SPECIFICITY, AND VARIANTS THR-42 AND ALA-60.
RC TISSUE=Lung;
RX PubMed=9288095; DOI=10.1038/ng0997-32;
RA Mollenhauer J., Wiemann S., Scheurlen W., Korn B., Hayashi Y.,
RA Wilgenbus K.K., von Deimling A., Poustka A.;
RT "DMBT1, a new member of the SRCR superfamily on chromosome 10q25.3-q26.1 is
RT deleted in malignant brain tumours.";
RL Nat. Genet. 17:32-39(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN MUCOSAL AND CELLULAR
RP IMMUNE DEFENSE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND VARIANTS THR-42; LEU-54; ALA-60; MET-649; MET-780 AND SER-856.
RC TISSUE=Trachea;
RX PubMed=10485905; DOI=10.1073/pnas.96.19.10794;
RA Holmskov U., Mollenhauer J., Madsen J., Vitved L., Gronlund J., Tornoe I.,
RA Kliem A., Reid K.B.M., Poustka A., Skjodt K.;
RT "Cloning of gp-340, a putative opsonin receptor for lung surfactant protein
RT D.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10794-10799(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), ALTERNATIVE SPLICING,
RP AND VARIANTS THR-42; LEU-54; ALA-60; LEU-337 AND SER-856.
RC TISSUE=Lung;
RX PubMed=10597221; DOI=10.1038/sj.onc.1203071;
RA Mollenhauer J., Holmskov U., Wiemann S., Krebs I., Herbertz S., Madsen J.,
RA Kioschis P., Coy J.F., Poustka A.;
RT "The genomic structure of the DMBT1 gene: evidence for a region with
RT susceptibility to genomic instability.";
RL Oncogene 18:6233-6240(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN LUNG CARCINOGENESIS, AND
RP VARIANTS THR-42; LEU-54 AND SER-856.
RX PubMed=10551316; DOI=10.1111/j.1349-7006.1999.tb00833.x;
RA Takeshita H., Sato M., Shiwaku H.O., Semba S., Sakurada A., Hoshi M.,
RA Hayashi Y., Tagawa Y., Ayabe H., Horii A.;
RT "Expression of the DMBT1 gene is frequently suppressed in human lung
RT cancer.";
RL Jpn. J. Cancer Res. 90:903-908(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN EPITHELIAL DIFFERENTIATION, TISSUE
RP SPECIFICITY, ALTERNATIVE SPLICING, INVOLVEMENT IN ESOPHAGEAL CARCINOMAS,
RP AND VARIANT SER-856.
RC TISSUE=Small intestine;
RX PubMed=11751412;
RA Mollenhauer J., Herbertz S., Helmke B., Kollender G., Krebs I., Madsen J.,
RA Holmskov U., Sorger K., Schmitt L., Wiemann S., Otto H.F., Grone H.-J.,
RA Poustka A.;
RT "Deleted in malignant brain tumors 1 is a versatile mucin-like molecule
RT likely to play a differential role in digestive tract cancer.";
RL Cancer Res. 61:8880-8886(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), AND VARIANT LEU-54.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-1480 (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1689-2413 (ISOFORM 5).
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [11]
RP PROTEIN SEQUENCE OF 2385-2413, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Tear;
RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
RA Suarez T., Elortza F.;
RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed
RT by in silico and in vitro analyses for antimicrobial peptide
RT identification.";
RL J. Proteome Res. 14:2649-2658(2015).
RN [12]
RP INTERACTION WITH SFTPD.
RX PubMed=9153228; DOI=10.1074/jbc.272.21.13743;
RA Holmskov U., Lawson P., Teisner B., Tornoe I., Willis A.C., Morgan C.,
RA Koch C., Reid K.B.;
RT "Isolation and characterization of a new member of the scavenger receptor
RT superfamily, glycoprotein-340 (gp-340), as a lung surfactant protein-D
RT binding molecule.";
RL J. Biol. Chem. 272:13743-13749(1997).
RN [13]
RP INTERACTION WITH SPAR.
RX PubMed=10101009; DOI=10.1165/ajrcmb.20.4.3439;
RA Tino M.J., Wright J.R.;
RT "Glycoprotein-340 binds surfactant protein-A (SP-A) and stimulates alveolar
RT macrophage migration in an SP-A-independent manner.";
RL Am. J. Respir. Cell Mol. Biol. 20:759-768(1999).
RN [14]
RP INVOLVEMENT IN ESOPHAGEAL; GASTRIC AND COLON CANCERS.
RX PubMed=9888459; DOI=10.1038/sj.bjc.6690035;
RA Mori M., Shiraishi T., Tanaka S., Yamagata M., Mafune K., Tanaka Y.,
RA Ueo H., Barnard G.F., Sugimachi K.;
RT "Lack of DMBT1 expression in oesophageal, gastric and colon cancers.";
RL Br. J. Cancer 79:211-213(1999).
RN [15]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=10749143;
RA Mollenhauer J., Herbertz S., Holmskov U., Tolnay M., Krebs I., Merlo A.,
RA Schroder H.D., Maier D., Breitling F., Wiemann S., Groene H.-J.,
RA Poustka A.;
RT "DMBT1 encodes a protein involved in the immune defense and in epithelial
RT differentiation and is highly unstable in cancer.";
RL Cancer Res. 60:1704-1710(2000).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RC TISSUE=Saliva;
RX PubMed=11007786; DOI=10.1074/jbc.m006928200;
RA Prakobphol A., Xu F., Hoang V.M., Larsson T., Bergstrom J., Johansson I.,
RA Fraengsmyr L., Holmskov U., Leffler H., Nilsson C., Boren T., Wright J.R.,
RA Stroemberg N., Fisher S.J.;
RT "Salivary agglutinin, which binds Streptococcus mutans and Helicobacter
RT pylori, is the lung scavenger receptor cysteine-rich protein gp-340.";
RL J. Biol. Chem. 275:39860-39866(2000).
RN [17]
RP BACTERIAL-BINDING DOMAIN.
RX PubMed=15355985; DOI=10.1074/jbc.m406095200;
RA Bikker F.J., Ligtenberg A.J.M., End C., Renner M., Blaich S., Lyer S.,
RA Wittig R., van't Hof W., Veerman E.C.I., Nazmi K.,
RA de Blieck-Hogervorst J.M.A., Kioschis P., Nieuw Amerongen A.V., Poustka A.,
RA Mollenhauer J.;
RT "Bacteria binding by DMBT1/SAG/gp-340 is confined to the VEVLXXXXW motif in
RT its scavenger receptor cysteine-rich domains.";
RL J. Biol. Chem. 279:47699-47703(2004).
RN [18]
RP FUNCTION, INTERACTION WITH HIV-1 GP120 (MICROBIAL INFECTION), AND TISSUE
RP SPECIFICITY.
RX PubMed=16796526; DOI=10.1089/aid.2006.22.508;
RA Wu Z., Lee S., Abrams W., Weissman D., Malamud D.;
RT "The N-terminal SRCR-SID domain of gp-340 interacts with HIV type 1 gp120
RT sequences and inhibits viral infection.";
RL AIDS Res. Hum. Retroviruses 22:508-515(2006).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1712; ASN-1889 AND ASN-2188.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [20]
RP TISSUE SPECIFICITY.
RX PubMed=17983803; DOI=10.1053/j.gastro.2007.08.007;
RA Renner M., Bergmann G., Krebs I., End C., Lyer S., Hilberg F., Helmke B.,
RA Gassler N., Autschbach F., Bikker F., Strobel-Freidekind O.,
RA Gronert-Sum S., Benner A., Blaich S., Wittig R., Hudler M.,
RA Ligtenberg A.J., Madsen J., Holmskov U., Annese V., Latiano A.,
RA Schirmacher P., Amerongen A.V.N., D'Amato M., Kioschis P., Hafner M.,
RA Poustka A., Mollenhauer J.;
RT "DMBT1 confers mucosal protection in vivo and a deletion variant is
RT associated with Crohn's disease.";
RL Gastroenterology 133:1499-1509(2007).
RN [21]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17548659; DOI=10.4049/jimmunol.178.12.8203;
RA Rosenstiel P., Sina C., End C., Renner M., Lyer S., Till A., Hellmig S.,
RA Nikolaus S., Foelsch U.R., Helmke B., Autschbach F., Schirmacher P.,
RA Kioschis P., Hafner M., Poustka A., Mollenhauer J., Schreiber S.;
RT "Regulation of DMBT1 via NOD2 and TLR4 in intestinal epithelial cells
RT modulates bacterial recognition and invasion.";
RL J. Immunol. 178:8203-8211(2007).
RN [22]
RP FUNCTION.
RX PubMed=17709527; DOI=10.4049/jimmunol.179.5.3126;
RA Stoddard E., Cannon G., Ni H., Kariko K., Capodici J., Malamud D.,
RA Weissman D.;
RT "gp340 expressed on human genital epithelia binds HIV-1 envelope protein
RT and facilitates viral transmission.";
RL J. Immunol. 179:3126-3132(2007).
RN [23]
RP BACTERIAL-BINDING DOMAIN.
RX PubMed=18713006; DOI=10.1515/bc.2008.135;
RA Leito J.T.D., Ligtenberg A.J.M., Nazmi K., de Blieck-Hogervorst J.M.A.,
RA Veerman E.C.I., Nieuw Amerongen A.V.;
RT "A common binding motif for various bacteria of the bacteria-binding
RT peptide SRCRP2 of DMBT1/gp-340/salivary agglutinin.";
RL Biol. Chem. 389:1193-1200(2008).
RN [24]
RP FUNCTION.
RX PubMed=19189310; DOI=10.1002/eji.200838689;
RA End C., Bikker F., Renner M., Bergmann G., Lyer S., Blaich S., Hudler M.,
RA Helmke B., Gassler N., Autschbach F., Ligtenberg A.J.M., Benner A.,
RA Holmskov U., Schirmacher P., Nieuw Amerongen A.V., Rosenstiel P., Sina C.,
RA Franke A., Hafner M., Kioschis P., Schreiber S., Poustka A.,
RA Mollenhauer J.;
RT "DMBT1 functions as pattern-recognition molecule for poly-sulfated and
RT poly-phosphorylated ligands.";
RL Eur. J. Immunol. 39:833-842(2009).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP INTERACTION WITH S.AUREUS SRAP (MICROBIAL INFECTION).
RX PubMed=23439307; DOI=10.1128/iai.00011-13;
RA Kukita K., Kawada-Matsuo M., Oho T., Nagatomo M., Oogai Y., Hashimoto M.,
RA Suda Y., Tanaka T., Komatsuzawa H.;
RT "Staphylococcus aureus SasA is responsible for binding to the salivary
RT agglutinin gp340, derived from human saliva.";
RL Infect. Immun. 81:1870-1879(2013).
RN [27]
RP VARIANTS THR-42; TRP-52; LEU-54; GLU-162; ASP-322; SER-357; SER-546;
RP PRO-1095; THR-1102; TRP-1434; SER-1732 AND MET-2255.
RX PubMed=12353266; DOI=10.1002/gcc.10115;
RA Mollenhauer J., Mueller H., Kollender G., Lyer S., Diedrichs L., Helmke B.,
RA Holmskov U., Ligtenberg T., Herbertz S., Krebs I., Madsen J., Bikker F.,
RA Schmitt L., Wiemann S., Scheurlen W., Otto H.F., von Deimling A.,
RA Poustka A.;
RT "The SRCR/SID region of DMBT1 defines a complex multi-allele system
RT representing the major basis for its variability in cancer.";
RL Genes Chromosomes Cancer 35:242-255(2002).
RN [28]
RP VARIANTS THR-42; TRP-52; LEU-54; ALA-60; LEU-65; LEU-337; SER-357; GLY-364;
RP MET-649; MET-780; TYR-1084; THR-1169; TRP-1176; MET-1545; SER-1732 AND
RP PRO-1961.
RX PubMed=12185598; DOI=10.1038/sj.onc.1205733;
RA Mueller W., Mollenhauer J., Stockhammer F., Poustka A., von Deimling A.;
RT "Rare mutations of the DMBT1 gene in human astrocytic gliomas.";
RL Oncogene 21:5956-5959(2002).
RN [29]
RP VARIANT ARG-969.
RX PubMed=28397838; DOI=10.1038/mp.2017.60;
RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M.,
RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M.,
RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R.,
RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M.,
RA Vincent J.B.;
RT "Mapping autosomal recessive intellectual disability: combined microarray
RT and exome sequencing identifies 26 novel candidate genes in 192
RT consanguineous families.";
RL Mol. Psychiatry 23:973-984(2018).
CC -!- FUNCTION: May be considered as a candidate tumor suppressor gene for
CC brain, lung, esophageal, gastric, and colorectal cancers. May play
CC roles in mucosal defense system, cellular immune defense and epithelial
CC differentiation. May play a role as an opsonin receptor for SFTPD and
CC SPAR in macrophage tissues throughout the body, including epithelial
CC cells lining the gastrointestinal tract. May play a role in liver
CC regeneration. May be an important factor in fate decision and
CC differentiation of transit-amplifying ductular (oval) cells within the
CC hepatic lineage. Required for terminal differentiation of columnar
CC epithelial cells during early embryogenesis. May function as a binding
CC protein in saliva for the regulation of taste sensation. Binds to HIV-1
CC envelope protein and has been shown to both inhibit and facilitate
CC viral transmission. Displays a broad calcium-dependent binding spectrum
CC against both Gram-positive and Gram-negative bacteria, suggesting a
CC role in defense against bacterial pathogens. Binds to a range of poly-
CC sulfated and poly-phosphorylated ligands which may explain its broad
CC bacterial-binding specificity. Inhibits cytoinvasion of S.enterica.
CC Associates with the actin cytoskeleton and is involved in its
CC remodeling during regulated exocytosis. Interacts with pancreatic
CC zymogens in a pH-dependent manner and may act as a Golgi cargo receptor
CC in the regulated secretory pathway of the pancreatic acinar cell.
CC {ECO:0000269|PubMed:10485905, ECO:0000269|PubMed:11007786,
CC ECO:0000269|PubMed:11751412, ECO:0000269|PubMed:16796526,
CC ECO:0000269|PubMed:17548659, ECO:0000269|PubMed:17709527,
CC ECO:0000269|PubMed:19189310, ECO:0000269|PubMed:9288095}.
CC -!- SUBUNIT: Interacts with LGALS3 (By similarity). Binds SFTPD and SPAR in
CC a calcium-dependent manner. {ECO:0000250, ECO:0000269|PubMed:10101009,
CC ECO:0000269|PubMed:9153228}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 glycoprotein 120.
CC {ECO:0000269|PubMed:16796526}.
CC -!- SUBUNIT: (Microbial infection) Interacts with S.aureus SraP; the
CC interaction is inhibited by N-acetylneuraminic acid (PubMed:23439307).
CC {ECO:0000269|PubMed:23439307}.
CC -!- INTERACTION:
CC Q9UGM3; P11226: MBL2; NbExp=2; IntAct=EBI-1044970, EBI-5325353;
CC Q9UGM3; Q8IWL2: SFTPA1; NbExp=2; IntAct=EBI-1044970, EBI-11316418;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Some isoforms may be
CC membrane-bound. Localized to the lumenal aspect of crypt cells in the
CC small intestine. In the colon, seen in the lumenal aspect of surface
CC epithelial cells. Formed in the ducts of von Ebner gland, and released
CC into the fluid bathing the taste buds contained in the taste papillae
CC (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Comment=More isoforms may exist.;
CC Name=1; Synonyms=DMBT1/8kb.2;
CC IsoId=Q9UGM3-1; Sequence=Displayed;
CC Name=2; Synonyms=DMBT1/6kb.1;
CC IsoId=Q9UGM3-2; Sequence=VSP_016846, VSP_016849;
CC Name=3; Synonyms=DMBT1/8kb.1;
CC IsoId=Q9UGM3-3; Sequence=VSP_016847;
CC Name=4;
CC IsoId=Q9UGM3-4; Sequence=VSP_016848;
CC Name=6;
CC IsoId=Q9UGM3-6; Sequence=VSP_034656;
CC Name=7;
CC IsoId=Q9UGM3-7; Sequence=VSP_016847, VSP_034656;
CC Name=8;
CC IsoId=Q9UGM3-8; Sequence=VSP_034653, VSP_034654, VSP_034655;
CC Name=5;
CC IsoId=Q9UGM3-5; Sequence=VSP_016850;
CC Name=9;
CC IsoId=Q9UGM3-9; Sequence=VSP_053979, VSP_053980, VSP_053981;
CC -!- TISSUE SPECIFICITY: Highly expressed in alveolar and macrophage
CC tissues. In some macrophages, expression is seen on the membrane, and
CC in other macrophages, strongly expressed in the phagosome/phagolysosome
CC compartments. Expressed in lung, trachea, salivary gland, small
CC intestine and stomach. In pancreas, expressed in certain cells of the
CC islets of Langerhans. In digestive tract, confined to tissues with
CC large epithelial surfaces. In intestinal tissue, moderately expressed
CC in epithelial cells of the midcrypts and the crypt base. Expression is
CC significantly elevated in intestinal tissue from patients with
CC inflammatory bowel disease (IBD), particularly in surface epithelial
CC and Paneth cells, but not in IBD patients with mutant NOD2. Present in
CC crypt bases of the duodenum, in crypt tops of the colon, and in
CC collecting ducts of the cortical kidney. Expressed in stratified
CC squamous epithelium of vagina and in outer luminar surface and basilar
CC region of columnar epithelial cells in cervix (at protein level).
CC Isoform 1 is secreted to the lumen of the respiratory tract.
CC {ECO:0000269|PubMed:10485905, ECO:0000269|PubMed:10749143,
CC ECO:0000269|PubMed:11751412, ECO:0000269|PubMed:16796526,
CC ECO:0000269|PubMed:17548659, ECO:0000269|PubMed:17983803,
CC ECO:0000269|PubMed:9288095}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal lung, intestine and skin.
CC Secreted to the extracellular matrix (ECM) in certain fetal epithelia.
CC {ECO:0000269|PubMed:10485905, ECO:0000269|PubMed:10749143}.
CC -!- INDUCTION: Up-regulated in intestinal epithelial cells in response to
CC pro-inflammatory stimuli including TNF and bacterial
CC lipopolysaccharides (LPS). {ECO:0000269|PubMed:17548659}.
CC -!- DOMAIN: The SRCR domains mediate binding to bacteria. The minimal
CC bacterial-binding site is an 11-residue repeat of GRVEVLYRGSW where
CC VEVL and W are critical residues.
CC -!- PTM: Highly N- and O-glycosylated. The O-glycans are heavily sulfated
CC (By similarity). {ECO:0000250}.
CC -!- POLYMORPHISM: The number of SRCR and SRCR-interspersed domains is
CC polymorphic in a variety of tumors and may represent the major site of
CC alterations in cancer.
CC -!- DISEASE: Glioma (GLM) [MIM:137800]: Gliomas are benign or malignant
CC central nervous system neoplasms derived from glial cells. They
CC comprise astrocytomas and glioblastoma multiforme that are derived from
CC astrocytes, oligodendrogliomas derived from oligodendrocytes and
CC ependymomas derived from ependymocytes. Note=The gene represented in
CC this entry is involved in disease pathogenesis. Homozygous deletions
CC may be the predominant mechanism of DMBT1 inactivation playing a role
CC in carcinogenesis. DMBT1 is deleted in medulloblastoma and glioblastoma
CC cell lines; point mutations have also been reported in patients with
CC glioma. A loss or reduction of DMBT1 expression has been seen in
CC esophageal, gastric, lung and colorectal carcinomas as well.
CC -!- SIMILARITY: Belongs to the DMBT1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DMBT1ID309ch10q26.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ000342; CAA04019.1; -; mRNA.
DR EMBL; AF159456; AAD49696.1; -; mRNA.
DR EMBL; AJ243212; CAB56155.1; -; mRNA.
DR EMBL; AJ243211; CAB63941.1; -; Genomic_DNA.
DR EMBL; AJ243224; CAB63942.1; -; mRNA.
DR EMBL; AB020851; BAA78577.1; -; Genomic_DNA.
DR EMBL; AJ297935; CAC44122.1; -; mRNA.
DR EMBL; AK304149; BAH14118.1; -; mRNA.
DR EMBL; AL603764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC153299; AAI53300.1; -; mRNA.
DR EMBL; AB209691; BAD92928.1; -; mRNA.
DR EMBL; BX640988; CAE45995.1; -; mRNA.
DR CCDS; CCDS44490.1; -. [Q9UGM3-1]
DR CCDS; CCDS44491.1; -. [Q9UGM3-2]
DR CCDS; CCDS44492.1; -. [Q9UGM3-3]
DR PIR; A59386; A59386.
DR RefSeq; NP_001307573.1; NM_001320644.1.
DR RefSeq; NP_004397.2; NM_004406.2. [Q9UGM3-2]
DR RefSeq; NP_015568.2; NM_007329.2. [Q9UGM3-1]
DR RefSeq; NP_060049.2; NM_017579.2. [Q9UGM3-3]
DR RefSeq; XP_011537690.1; XM_011539388.2.
DR RefSeq; XP_011537693.1; XM_011539391.2. [Q9UGM3-7]
DR RefSeq; XP_011537707.1; XM_011539405.2. [Q9UGM3-1]
DR PDB; 6SA4; X-ray; 1.77 A; A=95-203.
DR PDB; 6SA5; X-ray; 1.29 A; A=986-1094.
DR PDB; 6SAN; X-ray; 1.36 A; A/B=986-1094.
DR PDBsum; 6SA4; -.
DR PDBsum; 6SA5; -.
DR PDBsum; 6SAN; -.
DR AlphaFoldDB; Q9UGM3; -.
DR SMR; Q9UGM3; -.
DR BioGRID; 108095; 65.
DR DIP; DIP-50763N; -.
DR IntAct; Q9UGM3; 26.
DR MINT; Q9UGM3; -.
DR STRING; 9606.ENSP00000357905; -.
DR GlyGen; Q9UGM3; 14 sites.
DR iPTMnet; Q9UGM3; -.
DR PhosphoSitePlus; Q9UGM3; -.
DR BioMuta; DMBT1; -.
DR DMDM; 85687556; -.
DR jPOST; Q9UGM3; -.
DR MassIVE; Q9UGM3; -.
DR MaxQB; Q9UGM3; -.
DR PaxDb; Q9UGM3; -.
DR PeptideAtlas; Q9UGM3; -.
DR PRIDE; Q9UGM3; -.
DR ProteomicsDB; 31825; -.
DR ProteomicsDB; 84235; -. [Q9UGM3-1]
DR ProteomicsDB; 84236; -. [Q9UGM3-2]
DR ProteomicsDB; 84237; -. [Q9UGM3-3]
DR ProteomicsDB; 84238; -. [Q9UGM3-4]
DR ProteomicsDB; 84239; -. [Q9UGM3-5]
DR ProteomicsDB; 84240; -. [Q9UGM3-6]
DR ProteomicsDB; 84241; -. [Q9UGM3-7]
DR ProteomicsDB; 84242; -. [Q9UGM3-8]
DR Antibodypedia; 32275; 199 antibodies from 28 providers.
DR DNASU; 1755; -.
DR Ensembl; ENST00000330163.8; ENSP00000327747.4; ENSG00000187908.20. [Q9UGM3-2]
DR Ensembl; ENST00000338354.10; ENSP00000342210.4; ENSG00000187908.20. [Q9UGM3-6]
DR Ensembl; ENST00000344338.7; ENSP00000343175.3; ENSG00000187908.20. [Q9UGM3-3]
DR Ensembl; ENST00000368909.7; ENSP00000357905.3; ENSG00000187908.20. [Q9UGM3-1]
DR Ensembl; ENST00000368955.7; ENSP00000357951.3; ENSG00000187908.20. [Q9UGM3-3]
DR Ensembl; ENST00000368956.6; ENSP00000357952.2; ENSG00000187908.20. [Q9UGM3-2]
DR Ensembl; ENST00000619379.1; ENSP00000484603.1; ENSG00000187908.20. [Q9UGM3-1]
DR Ensembl; ENST00000652446.2; ENSP00000498825.1; ENSG00000187908.20. [Q9UGM3-1]
DR Ensembl; ENST00000653442.1; ENSP00000499436.1; ENSG00000187908.20. [Q9UGM3-5]
DR Ensembl; ENST00000657942.1; ENSP00000499391.1; ENSG00000187908.20. [Q9UGM3-9]
DR Ensembl; ENST00000664692.1; ENSP00000499397.1; ENSG00000187908.20. [Q9UGM3-7]
DR GeneID; 1755; -.
DR KEGG; hsa:1755; -.
DR MANE-Select; ENST00000338354.10; ENSP00000342210.4; NM_001377530.1; NP_001364459.1. [Q9UGM3-6]
DR UCSC; uc001lgk.1; human. [Q9UGM3-1]
DR CTD; 1755; -.
DR DisGeNET; 1755; -.
DR GeneCards; DMBT1; -.
DR HGNC; HGNC:2926; DMBT1.
DR HPA; ENSG00000187908; Group enriched (intestine, salivary gland).
DR MIM; 137800; phenotype.
DR MIM; 601969; gene.
DR neXtProt; NX_Q9UGM3; -.
DR OpenTargets; ENSG00000187908; -.
DR PharmGKB; PA27376; -.
DR VEuPathDB; HostDB:ENSG00000187908; -.
DR eggNOG; ENOG502QQ5W; Eukaryota.
DR GeneTree; ENSGT00950000183145; -.
DR HOGENOM; CLU_230903_0_0_1; -.
DR InParanoid; Q9UGM3; -.
DR OMA; LSHNCNH; -.
DR OrthoDB; 1095487at2759; -.
DR PhylomeDB; Q9UGM3; -.
DR TreeFam; TF329295; -.
DR PathwayCommons; Q9UGM3; -.
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR SignaLink; Q9UGM3; -.
DR BioGRID-ORCS; 1755; 7 hits in 1070 CRISPR screens.
DR ChiTaRS; DMBT1; human.
DR GeneWiki; DMBT1; -.
DR GenomeRNAi; 1755; -.
DR Pharos; Q9UGM3; Tbio.
DR PRO; PR:Q9UGM3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9UGM3; protein.
DR Bgee; ENSG00000187908; Expressed in parotid gland and 142 other tissues.
DR ExpressionAtlas; Q9UGM3; baseline and differential.
DR Genevisible; Q9UGM3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; TAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:1904399; F:heparan sulfate binding; IDA:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0070891; F:lipoteichoic acid binding; IDA:UniProtKB.
DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IDA:UniProtKB.
DR GO; GO:0035375; F:zymogen binding; ISS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0042494; P:detection of bacterial lipoprotein; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; TAS:UniProtKB.
DR GO; GO:0043152; P:induction of bacterial agglutination; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR CDD; cd00041; CUB; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 2.60.40.4100; -; 1.
DR Gene3D; 3.10.250.10; -; 14.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00530; SRCR; 14.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00202; SR; 14.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF56487; SSF56487; 14.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00420; SRCR_1; 13.
DR PROSITE; PS50287; SRCR_2; 14.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Host-virus interaction; Protein transport;
KW Reference proteome; Repeat; Secreted; Signal; Transport; Tumor suppressor.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2413
FT /note="Deleted in malignant brain tumors 1 protein"
FT /id="PRO_0000045387"
FT DOMAIN 102..202
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 234..334
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 363..463
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 494..594
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 602..702
FT /note="SRCR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 733..833
FT /note="SRCR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 862..962
FT /note="SRCR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 993..1093
FT /note="SRCR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 1122..1222
FT /note="SRCR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 1251..1351
FT /note="SRCR 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 1380..1480
FT /note="SRCR 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 1509..1609
FT /note="SRCR 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 1640..1740
FT /note="SRCR 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 1766..1877
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1883..1986
FT /note="SRCR 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 2008..2117
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 2126..2381
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 335..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002"
FT CARBOHYD 1745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002"
FT CARBOHYD 1998
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002"
FT CARBOHYD 2233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127..191
FT /evidence="ECO:0000250"
FT DISULFID 140..201
FT /evidence="ECO:0000250"
FT DISULFID 171..181
FT /evidence="ECO:0000250"
FT DISULFID 259..323
FT /evidence="ECO:0000250"
FT DISULFID 272..333
FT /evidence="ECO:0000250"
FT DISULFID 303..313
FT /evidence="ECO:0000250"
FT DISULFID 388..452
FT /evidence="ECO:0000250"
FT DISULFID 401..462
FT /evidence="ECO:0000250"
FT DISULFID 432..442
FT /evidence="ECO:0000250"
FT DISULFID 519..583
FT /evidence="ECO:0000250"
FT DISULFID 532..593
FT /evidence="ECO:0000250"
FT DISULFID 563..573
FT /evidence="ECO:0000250"
FT DISULFID 627..691
FT /evidence="ECO:0000250"
FT DISULFID 640..701
FT /evidence="ECO:0000250"
FT DISULFID 671..681
FT /evidence="ECO:0000250"
FT DISULFID 758..822
FT /evidence="ECO:0000250"
FT DISULFID 771..832
FT /evidence="ECO:0000250"
FT DISULFID 802..812
FT /evidence="ECO:0000250"
FT DISULFID 887..951
FT /evidence="ECO:0000250"
FT DISULFID 900..961
FT /evidence="ECO:0000250"
FT DISULFID 931..941
FT /evidence="ECO:0000250"
FT DISULFID 1018..1082
FT /evidence="ECO:0000250"
FT DISULFID 1031..1092
FT /evidence="ECO:0000250"
FT DISULFID 1062..1072
FT /evidence="ECO:0000250"
FT DISULFID 1147..1211
FT /evidence="ECO:0000250"
FT DISULFID 1160..1221
FT /evidence="ECO:0000250"
FT DISULFID 1191..1201
FT /evidence="ECO:0000250"
FT DISULFID 1276..1340
FT /evidence="ECO:0000250"
FT DISULFID 1289..1350
FT /evidence="ECO:0000250"
FT DISULFID 1320..1330
FT /evidence="ECO:0000250"
FT DISULFID 1405..1469
FT /evidence="ECO:0000250"
FT DISULFID 1418..1479
FT /evidence="ECO:0000250"
FT DISULFID 1449..1459
FT /evidence="ECO:0000250"
FT DISULFID 1534..1598
FT /evidence="ECO:0000250"
FT DISULFID 1547..1608
FT /evidence="ECO:0000250"
FT DISULFID 1578..1588
FT /evidence="ECO:0000250"
FT DISULFID 1665..1729
FT /evidence="ECO:0000250"
FT DISULFID 1678..1739
FT /evidence="ECO:0000250"
FT DISULFID 1709..1719
FT /evidence="ECO:0000250"
FT DISULFID 1766..1792
FT /evidence="ECO:0000250"
FT DISULFID 1819..1841
FT /evidence="ECO:0000250"
FT DISULFID 1911..1975
FT /evidence="ECO:0000250"
FT DISULFID 1924..1985
FT /evidence="ECO:0000250"
FT DISULFID 1955..1965
FT /evidence="ECO:0000250"
FT DISULFID 2008..2034
FT /evidence="ECO:0000250"
FT DISULFID 2059..2081
FT /evidence="ECO:0000250"
FT DISULFID 2302..2360
FT /evidence="ECO:0000250"
FT VAR_SEQ 201..332
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053979"
FT VAR_SEQ 337..835
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9288095"
FT /id="VSP_016846"
FT VAR_SEQ 344..1360
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053980"
FT VAR_SEQ 464..473
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10597221"
FT /id="VSP_016847"
FT VAR_SEQ 472..478
FT /note="SPDTLPT -> RPGERPR (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034653"
FT VAR_SEQ 479..971
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034654"
FT VAR_SEQ 523..1408
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_016848"
FT VAR_SEQ 1099..1356
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034655"
FT VAR_SEQ 1169
FT /note="M -> MSAPGNARFGQGSGPIVLDDVRCSGHESYLWSCPHNGWLSHNCGHHE
FT DAGVICSASQSQPTPSPDTWPTSHASTAGSESSLALRLVNGGDRCQGRVEVLYRGSWGT
FT VCDDYWDTNDANVVCRQLGCGWAT (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_034656"
FT VAR_SEQ 1170..1298
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9288095"
FT /id="VSP_016849"
FT VAR_SEQ 1608..1738
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053981"
FT VAR_SEQ 1741..1761
FT /note="ATQINSTTTDWWHPTTTTTAR -> G (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016850"
FT VARIANT 42
FT /note="P -> T (in dbSNP:rs11523871)"
FT /evidence="ECO:0000269|PubMed:10485905,
FT ECO:0000269|PubMed:10551316, ECO:0000269|PubMed:10597221,
FT ECO:0000269|PubMed:12185598, ECO:0000269|PubMed:12353266,
FT ECO:0000269|PubMed:9288095"
FT /id="VAR_024788"
FT VARIANT 52
FT /note="S -> W (in dbSNP:rs75209396)"
FT /evidence="ECO:0000269|PubMed:12185598,
FT ECO:0000269|PubMed:12353266"
FT /id="VAR_024789"
FT VARIANT 54
FT /note="S -> L (in dbSNP:rs3013236)"
FT /evidence="ECO:0000269|PubMed:10485905,
FT ECO:0000269|PubMed:10551316, ECO:0000269|PubMed:10597221,
FT ECO:0000269|PubMed:12185598, ECO:0000269|PubMed:12353266,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_024790"
FT VARIANT 60
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:10485905,
FT ECO:0000269|PubMed:10597221, ECO:0000269|PubMed:12185598,
FT ECO:0000269|PubMed:9288095"
FT /id="VAR_024791"
FT VARIANT 65
FT /note="P -> L (in dbSNP:rs185045706)"
FT /evidence="ECO:0000269|PubMed:12185598"
FT /id="VAR_024792"
FT VARIANT 162
FT /note="G -> E (in a glioma cell line; dbSNP:rs200664624)"
FT /evidence="ECO:0000269|PubMed:12353266"
FT /id="VAR_057981"
FT VARIANT 322
FT /note="N -> D (in dbSNP:rs1969620)"
FT /evidence="ECO:0000269|PubMed:12353266"
FT /id="VAR_044417"
FT VARIANT 337
FT /note="Q -> L"
FT /evidence="ECO:0000269|PubMed:10597221,
FT ECO:0000269|PubMed:12185598"
FT /id="VAR_024793"
FT VARIANT 357
FT /note="P -> S (in dbSNP:rs141757453)"
FT /evidence="ECO:0000269|PubMed:12185598,
FT ECO:0000269|PubMed:12353266"
FT /id="VAR_024794"
FT VARIANT 364
FT /note="R -> G"
FT /evidence="ECO:0000269|PubMed:12185598"
FT /id="VAR_024795"
FT VARIANT 420
FT /note="Q -> H (in a glioma sample; glioblastoma multiforme;
FT somatic mutation; dbSNP:rs104894156)"
FT /id="VAR_024796"
FT VARIANT 546
FT /note="N -> S (in a glioma cell line; dbSNP:rs200713568)"
FT /evidence="ECO:0000269|PubMed:12353266"
FT /id="VAR_057982"
FT VARIANT 607
FT /note="G -> V (in a glioma sample; pilocytic astrocytoma)"
FT /id="VAR_024797"
FT VARIANT 649
FT /note="T -> M (in dbSNP:rs189478437)"
FT /evidence="ECO:0000269|PubMed:10485905,
FT ECO:0000269|PubMed:12185598"
FT /id="VAR_024798"
FT VARIANT 656
FT /note="R -> W (in dbSNP:rs989419742)"
FT /id="VAR_024799"
FT VARIANT 670
FT /note="R -> C (in dbSNP:rs2277237)"
FT /id="VAR_052994"
FT VARIANT 719
FT /note="T -> M (in dbSNP:rs2277238)"
FT /id="VAR_052995"
FT VARIANT 780
FT /note="T -> M (in dbSNP:rs199704744)"
FT /evidence="ECO:0000269|PubMed:10485905,
FT ECO:0000269|PubMed:12185598"
FT /id="VAR_024800"
FT VARIANT 856
FT /note="P -> S (in dbSNP:rs144450471)"
FT /evidence="ECO:0000269|PubMed:10485905,
FT ECO:0000269|PubMed:10551316, ECO:0000269|PubMed:10597221,
FT ECO:0000269|PubMed:11751412"
FT /id="VAR_024801"
FT VARIANT 969
FT /note="T -> R (found in a consanguineous family with
FT intellectual disability; unknown pathological significance;
FT dbSNP:rs1195952221)"
FT /evidence="ECO:0000269|PubMed:28397838"
FT /id="VAR_080764"
FT VARIANT 1084
FT /note="H -> Y (in dbSNP:rs2277244)"
FT /evidence="ECO:0000269|PubMed:12185598"
FT /id="VAR_024802"
FT VARIANT 1095
FT /note="S -> P (in dbSNP:rs200551848)"
FT /evidence="ECO:0000269|PubMed:12353266"
FT /id="VAR_057983"
FT VARIANT 1102
FT /note="S -> T (in dbSNP:rs566926424)"
FT /evidence="ECO:0000269|PubMed:12353266"
FT /id="VAR_057984"
FT VARIANT 1169
FT /note="M -> T (in dbSNP:rs149099696)"
FT /evidence="ECO:0000269|PubMed:12185598"
FT /id="VAR_024803"
FT VARIANT 1176
FT /note="R -> W (in dbSNP:rs761527369)"
FT /evidence="ECO:0000269|PubMed:12185598"
FT /id="VAR_024804"
FT VARIANT 1434
FT /note="R -> W"
FT /evidence="ECO:0000269|PubMed:12353266"
FT /id="VAR_057985"
FT VARIANT 1545
FT /note="V -> M (in dbSNP:rs189221852)"
FT /evidence="ECO:0000269|PubMed:12185598"
FT /id="VAR_024805"
FT VARIANT 1732
FT /note="H -> S (requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:12185598,
FT ECO:0000269|PubMed:12353266"
FT /id="VAR_024806"
FT VARIANT 1860
FT /note="R -> L (in dbSNP:rs7099177)"
FT /id="VAR_044418"
FT VARIANT 1961
FT /note="T -> P"
FT /evidence="ECO:0000269|PubMed:12185598"
FT /id="VAR_024807"
FT VARIANT 2255
FT /note="V -> M (in dbSNP:rs183135544)"
FT /evidence="ECO:0000269|PubMed:12353266"
FT /id="VAR_057986"
FT CONFLICT 10
FT /note="M -> V (in Ref. 5; CAC44122)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="L -> S (in Ref. 6; BAH14118)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="A -> T (in Ref. 8; AAI53300)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="P -> Q (in Ref. 2; AAD49696 and 8; AAI53300)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="S -> T (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="T -> A (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="S -> T (in Ref. 6; BAH14118)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="G -> S (in Ref. 6; BAH14118)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="W -> R (in Ref. 5; CAC44122)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="S -> SDTLPTTTLPASTV (in Ref. 3; CAB63941)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="R -> G (in Ref. 3; CAB63942)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="R -> G (in Ref. 5; CAC44122)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="Q -> R (in Ref. 3; CAB63942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="L -> P (in Ref. 1; CAA04019 and 2; AAD49696)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="V -> A (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 1069
FT /note="L -> P (in Ref. 1; CAA04019 and 2; AAD49696)"
FT /evidence="ECO:0000305"
FT CONFLICT 1159
FT /note="V -> A (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 1204
FT /note="N -> D (in Ref. 3; CAB63942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271
FT /note="S -> P (in Ref. 3; CAB63942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1295
FT /note="G -> S (in Ref. 5; CAC44122)"
FT /evidence="ECO:0000305"
FT CONFLICT 1336
FT /note="L -> F (in Ref. 5; CAC44122)"
FT /evidence="ECO:0000305"
FT CONFLICT 1411
FT /note="T -> I (in Ref. 8; AAI53300)"
FT /evidence="ECO:0000305"
FT CONFLICT 1432
FT /note="N -> S (in Ref. 3; CAB63942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1443
FT /note="V -> A (in Ref. 3; CAB63942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1448
FT /note="R -> H (in Ref. 8; AAI53300)"
FT /evidence="ECO:0000305"
FT CONFLICT 1482
FT /note="S -> F (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 1583
FT /note="S -> P (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 1591
FT /note="N -> K (in Ref. 6; BAH14118)"
FT /evidence="ECO:0000305"
FT CONFLICT 1595
FT /note="S -> T (in Ref. 6; BAH14118)"
FT /evidence="ECO:0000305"
FT CONFLICT 1705
FT /note="D -> G (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 1845
FT /note="R -> G (in Ref. 10)"
FT /evidence="ECO:0000305"
FT CONFLICT 1909
FT /note="T -> A (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 2004..2005
FT /note="TD -> N (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 2196
FT /note="F -> L (in Ref. 2; CAB56155)"
FT /evidence="ECO:0000305"
FT CONFLICT 2380
FT /note="L -> S (in Ref. 8; AAI53300)"
FT /evidence="ECO:0000305"
FT CONFLICT 2405
FT /note="P -> A (in Ref. 5; CAC44122)"
FT /evidence="ECO:0000305"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:6SA4"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:6SA4"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:6SA4"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:6SA4"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6SA4"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6SA4"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6SA4"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:6SA4"
FT STRAND 992..1000
FT /evidence="ECO:0007829|PDB:6SA5"
FT STRAND 1003..1010
FT /evidence="ECO:0007829|PDB:6SA5"
FT STRAND 1013..1019
FT /evidence="ECO:0007829|PDB:6SA5"
FT HELIX 1024..1033
FT /evidence="ECO:0007829|PDB:6SA5"
FT STRAND 1038..1041
FT /evidence="ECO:0007829|PDB:6SA5"
FT TURN 1045..1048
FT /evidence="ECO:0007829|PDB:6SA5"
FT STRAND 1055..1057
FT /evidence="ECO:0007829|PDB:6SA5"
FT HELIX 1069..1071
FT /evidence="ECO:0007829|PDB:6SA5"
FT HELIX 1084..1086
FT /evidence="ECO:0007829|PDB:6SA5"
FT STRAND 1089..1092
FT /evidence="ECO:0007829|PDB:6SA5"
SQ SEQUENCE 2413 AA; 260735 MW; 25363E6263234F15 CRC64;
MGISTVILEM CLLWGQVLST GGWIPRTTDY ASLIPSEVPL DPTVAEGSPF PSESTLESTV
AEGSPISLES TLESTVAEGS LIPSESTLES TVAEGSDSGL ALRLVNGDGR CQGRVEILYR
GSWGTVCDDS WDTNDANVVC RQLGCGWAMS APGNAWFGQG SGPIALDDVR CSGHESYLWS
CPHNGWLSHN CGHGEDAGVI CSAAQPQSTL RPESWPVRIS PPVPTEGSES SLALRLVNGG
DRCRGRVEVL YRGSWGTVCD DYWDTNDANV VCRQLGCGWA MSAPGNAQFG QGSGPIVLDD
VRCSGHESYL WSCPHNGWLT HNCGHSEDAG VICSAPQSRP TPSPDTWPTS HASTAGPESS
LALRLVNGGD RCQGRVEVLY RGSWGTVCDD SWDTSDANVV CRQLGCGWAT SAPGNARFGQ
GSGPIVLDDV RCSGYESYLW SCPHNGWLSH NCQHSEDAGV ICSAAHSWST PSPDTLPTIT
LPASTVGSES SLALRLVNGG DRCQGRVEVL YRGSWGTVCD DSWDTNDANV VCRQLGCGWA
MLAPGNARFG QGSGPIVLDD VRCSGNESYL WSCPHNGWLS HNCGHSEDAG VICSGPESSL
ALRLVNGGDR CQGRVEVLYR GSWGTVCDDS WDTNDANVVC RQLGCGWATS APGNARFGQG
SGPIVLDDVR CSGHESYLWS CPNNGWLSHN CGHHEDAGVI CSAAQSRSTP RPDTLSTITL
PPSTVGSESS LTLRLVNGSD RCQGRVEVLY RGSWGTVCDD SWDTNDANVV CRQLGCGWAT
SAPGNARFGQ GSGPIVLDDV RCSGHESYLW SCPHNGWLSH NCGHHEDAGV ICSVSQSRPT
PSPDTWPTSH ASTAGPESSL ALRLVNGGDR CQGRVEVLYR GSWGTVCDDS WDTSDANVVC
RQLGCGWATS APGNARFGQG SGPIVLDDVR CSGYESYLWS CPHNGWLSHN CQHSEDAGVI
CSAAHSWSTP SPDTLPTITL PASTVGSESS LALRLVNGGD RCQGRVEVLY QGSWGTVCDD
SWDTNDANVV CRQLGCGWAM SAPGNARFGQ GSGPIVLDDV RCSGHESYLW SCPHNGWLSH
NCGHSEDAGV ICSASQSRPT PSPDTWPTSH ASTAGSESSL ALRLVNGGDR CQGRVEVLYR
GSWGTVCDDY WDTNDANVVC RQLGCGWAMS APGNARFGQG SGPIVLDDVR CSGHESYLWS
CPHNGWLSHN CGHHEDAGVI CSASQSQPTP SPDTWPTSHA STAGSESSLA LRLVNGGDRC
QGRVEVLYRG SWGTVCDDYW DTNDANVVCR QLGCGWATSA PGNARFGQGS GPIVLDDVRC
SGHESYLWSC PHNGWLSHNC GHHEDAGVIC SASQSQPTPS PDTWPTSHAS TAGSESSLAL
RLVNGGDRCQ GRVEVLYRGS WGTVCDDYWD TNDANVVCRQ LGCGWATSAP GNARFGQGSG
PIVLDDVRCS GHESYLWSCP HNGWLSHNCG HHEDAGVICS ASQSQPTPSP DTWPTSRAST
AGSESTLALR LVNGGDRCRG RVEVLYQGSW GTVCDDYWDT NDANVVCRQL GCGWAMSAPG
NAQFGQGSGP IVLDDVRCSG HESYLWSCPH NGWLSHNCGH HEDAGVICSA AQSQSTPRPD
TWLTTNLPAL TVGSESSLAL RLVNGGDRCR GRVEVLYRGS WGTVCDDSWD TNDANVVCRQ
LGCGWAMSAP GNARFGQGSG PIVLDDVRCS GNESYLWSCP HKGWLTHNCG HHEDAGVICS
ATQINSTTTD WWHPTTTTTA RPSSNCGGFL FYASGTFSSP SYPAYYPNNA KCVWEIEVNS
GYRINLGFSN LKLEAHHNCS FDYVEIFDGS LNSSLLLGKI CNDTRQIFTS SYNRMTIHFR
SDISFQNTGF LAWYNSFPSD ATLRLVNLNS SYGLCAGRVE IYHGGTWGTV CDDSWTIQEA
EVVCRQLGCG RAVSALGNAY FGSGSGPITL DDVECSGTES TLWQCRNRGW FSHNCNHRED
AGVICSGNHL STPAPFLNIT RPNTDYSCGG FLSQPSGDFS SPFYPGNYPN NAKCVWDIEV
QNNYRVTVIF RDVQLEGGCN YDYIEVFDGP YRSSPLIARV CDGARGSFTS SSNFMSIRFI
SDHSITRRGF RAEYYSSPSN DSTNLLCLPN HMQASVSRSY LQSLGFSASD LVISTWNGYY
ECRPQITPNL VIFTIPYSGC GTFKQADNDT IDYSNFLTAA VSGGIIKRRT DLRIHVSCRM
LQNTWVDTMY IANDTIHVAN NTIQVEEVQY GNFDVNISFY TSSSFLYPVT SRPYYVDLNQ
DLYVQAEILH SDAVLTLFVD TCVASPYSND FTSLTYDLIR SGCVRDDTYG PYSSPSLRIA
RFRFRAFHFL NRFPSVYLRC KMVVCRAYDP SSRCYRGCVL RSKRDVGSYQ EKVDVVLGPI
QLQTPPRREE EPR
