DMBT1_RABIT
ID DMBT1_RABIT Reviewed; 1594 AA.
AC Q95218; Q95219; Q9TV20; Q9TV21; Q9TV22;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Deleted in malignant brain tumors 1 protein;
DE AltName: Full=Hensin;
DE Flags: Precursor;
GN Name=Dmbt1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 93-129; 732-751
RP AND 1083-1090, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8941650; DOI=10.1172/jci119044;
RA Takito J., Hikita C., Al-Awqati Q.;
RT "Hensin, a new collecting duct protein involved in the in vitro plasticity
RT of intercalated cell polarity.";
RL J. Clin. Invest. 98:2324-2331(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), GLYCOSYLATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=10444583; DOI=10.1152/ajprenal.1999.277.2.f277;
RA Takito J., Yan L., Ma J., Hikita C., Vijayakumar S., Warburton D.,
RA Al-Awqati Q.;
RT "Hensin, the polarity reversal protein, is encoded by DMBT1, a gene
RT frequently deleted in malignant gliomas.";
RL Am. J. Physiol. 277:F277-F289(1999).
CC -!- FUNCTION: May play roles in mucosal defense system and cellular immune
CC defense. May play a role in liver regeneration. May be an important
CC factor in fate decision and differentiation of transit-amplifying
CC ductular (oval) cells within the hepatic lineage. May function as a
CC binding protein in saliva for the regulation of taste sensation. May
CC play a role as an opsonin receptor for SFTPD and SPAR in macrophage
CC tissues throughout the body, including epithelial cells lining the
CC gastrointestinal tract. Required for terminal differentiation of
CC columnar epithelial cells during early embryogenesis. Displays a broad
CC calcium-dependent binding spectrum against both Gram-positive and Gram-
CC negative bacteria, suggesting a role in defense against bacterial
CC pathogens. Binds to a range of poly-sulfated and poly-phosphorylated
CC ligands which may explain its broad bacterial-binding specificity.
CC Inhibits cytoinvasion of S.enterica. Associates with the actin
CC cytoskeleton and is involved in its remodeling during regulated
CC exocytosis. Interacts with pancreatic zymogens in a pH-dependent manner
CC and may act as a Golgi cargo receptor in the regulated secretory
CC pathway of the pancreatic acinar cell (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LGALS3. Binds SFTPD and SPAR in a calcium-
CC dependent manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8941650}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q95218-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95218-2; Sequence=VSP_034658, VSP_034659;
CC -!- TISSUE SPECIFICITY: Expressed in small intestine, liver, stomach and
CC kidney. Present in small intestine and in collecting tubules of kidney
CC cortex, medulla and papilla (at protein level).
CC {ECO:0000269|PubMed:10444583, ECO:0000269|PubMed:8941650}.
CC -!- DOMAIN: The SRCR domains mediate binding to bacteria. {ECO:0000250}.
CC -!- PTM: Highly N- and O-glycosylated. The O-glycans are heavily sulfated
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DMBT1 family. {ECO:0000305}.
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DR EMBL; AF043112; AAD02242.1; -; mRNA.
DR EMBL; AF078900; AAD50330.1; -; Genomic_DNA.
DR EMBL; AF078900; AAD50331.1; -; Genomic_DNA.
DR EMBL; AF078900; AAD50332.1; -; Genomic_DNA.
DR PIR; T30549; T30549.
DR RefSeq; NP_001075502.1; NM_001082033.1.
DR AlphaFoldDB; Q95218; -.
DR SMR; Q95218; -.
DR STRING; 9986.ENSOCUP00000011615; -.
DR PRIDE; Q95218; -.
DR GeneID; 100008679; -.
DR KEGG; ocu:100008679; -.
DR CTD; 1755; -.
DR InParanoid; Q95218; -.
DR OrthoDB; 1095487at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0035375; F:zymogen binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; -; 8.
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; 8.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00202; SR; 8.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF56487; SSF56487; 8.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00420; SRCR_1; 6.
DR PROSITE; PS50287; SRCR_2; 8.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Protein transport;
KW Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1594
FT /note="Deleted in malignant brain tumors 1 protein"
FT /id="PRO_0000343684"
FT DOMAIN 53..153
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 192..292
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 323..423
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 454..551
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 582..682
FT /note="SRCR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 713..813
FT /note="SRCR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 821..921
FT /note="SRCR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 951..1061
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1067..1170
FT /note="SRCR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 1192..1301
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1310..1558
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..142
FT /evidence="ECO:0000250"
FT DISULFID 91..152
FT /evidence="ECO:0000250"
FT DISULFID 122..132
FT /evidence="ECO:0000250"
FT DISULFID 217..281
FT /evidence="ECO:0000250"
FT DISULFID 230..291
FT /evidence="ECO:0000250"
FT DISULFID 261..271
FT /evidence="ECO:0000250"
FT DISULFID 348..412
FT /evidence="ECO:0000250"
FT DISULFID 361..422
FT /evidence="ECO:0000250"
FT DISULFID 392..402
FT /evidence="ECO:0000250"
FT DISULFID 476..540
FT /evidence="ECO:0000250"
FT DISULFID 489..550
FT /evidence="ECO:0000250"
FT DISULFID 520..530
FT /evidence="ECO:0000250"
FT DISULFID 607..671
FT /evidence="ECO:0000250"
FT DISULFID 620..681
FT /evidence="ECO:0000250"
FT DISULFID 651..661
FT /evidence="ECO:0000250"
FT DISULFID 738..802
FT /evidence="ECO:0000250"
FT DISULFID 751..812
FT /evidence="ECO:0000250"
FT DISULFID 782..792
FT /evidence="ECO:0000250"
FT DISULFID 846..910
FT /evidence="ECO:0000250"
FT DISULFID 859..920
FT /evidence="ECO:0000250"
FT DISULFID 890..900
FT /evidence="ECO:0000250"
FT DISULFID 951..977
FT /evidence="ECO:0000250"
FT DISULFID 1004..1025
FT /evidence="ECO:0000250"
FT DISULFID 1095..1159
FT /evidence="ECO:0000250"
FT DISULFID 1108..1169
FT /evidence="ECO:0000250"
FT DISULFID 1139..1149
FT /evidence="ECO:0000250"
FT DISULFID 1192..1218
FT /evidence="ECO:0000250"
FT DISULFID 1243..1265
FT /evidence="ECO:0000250"
FT DISULFID 1479..1537
FT /evidence="ECO:0000250"
FT VAR_SEQ 45..302
FT /note="EVFPSGLELRLANGGDRCQGRVEVLYQGSWGTVCDDGWDINDAQVVCRQLGC
FT GMAVSAPGSARFGQGPGQIVLDDVSCSGQEPYLWSCHHRGWLSHNCGHQEDAGVICSDA
FT MAMTSPPPDTWPTTVIYESTPHFPSGLELVFPSGLELRLANGSDRCQGRVEVLYQGSWG
FT TVCDDGWDINDAQVVCRQLGCGMAVSAPGSARFGQGPGQIVLDDVSCSGQEPYLWSCHH
FT RGWLSHNCGHQEDAGVICSDAVPTTTPPP -> TE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10444583"
FT /id="VSP_034658"
FT VAR_SEQ 361..488
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10444583"
FT /id="VSP_034659"
FT CONFLICT 40
FT /note="E -> EA (in Ref. 2; AAD50330)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="T -> A (in Ref. 2; AAD50332/AAD50331)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="S -> T (in Ref. 2; AAD50330)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..185
FT /note="HFPSGLELV -> L (in Ref. 2; AAD50330)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="S -> G (in Ref. 2; AAD50330)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="S -> T (in Ref. 2; AAD50332/AAD50331)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="S -> G (in Ref. 2; AAD50332/AAD50331)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="H -> L (in Ref. 2; AAD50332/AAD50331)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="S -> G (in Ref. 2; AAD50332/AAD50331)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="T -> M (in Ref. 2; AAD50332/AAD50331)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="L -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1594 AA; 172764 MW; 29D6BEFEAA987CC4 CRC64;
MGISTVLALS LLWGPALSQG QWIPYTTYHD SVSSPGAPVE TTTTEVFPSG LELRLANGGD
RCQGRVEVLY QGSWGTVCDD GWDINDAQVV CRQLGCGMAV SAPGSARFGQ GPGQIVLDDV
SCSGQEPYLW SCHHRGWLSH NCGHQEDAGV ICSDAMAMTS PPPDTWPTTV IYESTPHFPS
GLELVFPSGL ELRLANGSDR CQGRVEVLYQ GSWGTVCDDG WDINDAQVVC RQLGCGMAVS
APGSARFGQG PGQIVLDDVS CSGQEPYLWS CHHRGWLSHN CGHQEDAGVI CSDAVPTTTP
PPDTWPTTVI YESSPVFPSG LELRLANGSD RCQGRVEVLY QGSWGTVCDD GWDINDAQVV
CRQLGCGTAV SAPGSARFGQ GPGQIVLDDV SCSGQEPYLW SCHHRGWLSH NCGHQEDAGV
ICSDAMAMTT PLPDTWPTTV IHESTPVFPS GLELQLANGS DRCQGRVEVL YQGTVCDDGW
DINDAQVVCR QLGCGMAVSA PGSARFGQGP GQIVLDDVSC SGQEPYLWSC HHRGWLSHNC
GHQEDAGVIC SDAMAMTTPP PDTWPTTVIY ESTPHFPSGL ELRLANGSDR CQGRVEVLYQ
GSWGTVCDDG WDINDAQVVC RQLGCGTAVS APGSARFGQG PGQIVLDDVS CSGQEPYLWS
CHHRGWLSHN CGHQEDAGVI CSGAMDTTTP LPDTWPTTVI YESTPVHISG LQLRLVNGSD
RCEGRVEVLY QGSWGTVCDD SWDLNDASVV CRQLGCGTAL SAPASAQFGQ SSGSIVLDDV
SCSGSEPNLW SCSHRGWLSH NCGHHEDAGV VCSGPDSRLA VRLVNGSTRC QGRVEVLYRG
SWGTVCDDSW DINDASVVCR QLGCGWAVSA PGSARFGQGS GSIFLDEVSC SGQEPYLWNC
SHRGWLSHNC GHYEDAGVIC SDGWTTVTPP APTTDWWEPT VTTTVGPSSN CGGFLYNATG
SFSSPSYPGY YPNNALCVWE IAVPSGYLIN LGFSQLRLEQ HSYCNFDYVE IFDGSTDSSL
LGKICNDSGQ IFTTSSNRMT VLFRSDISVQ NTGFLAWYNS FPRDASLRLV SGNSSYGACA
GRVEIYHGGR WGTVCDDSWD TQDAQVVCRQ LQCGDAVSAP GGAYFGSGSG PITLDDVNCS
GTEATLWQCR SQSWFSHNCG HHEDASVICT GNYGTTTASV PNISTSNASY SCGGFLSQHS
GRFSSPFYPG NYPNNARCVW DIEVQNNYQV TVTFTDVQLE GGCQYDYIEV FDGPYHSSPL
IARVCDGARG SFTSSSNFLS VRFVSDGSIT RRGFQAEFYS LPSNDSTNLL CLMNHMQASV
SRAYLQSLGF SAWELVVSGW NGNYQCQRQI TPSQVIFTIP YSGCGTIKQV DNETITYSNF
LKAAVSSGVI KRKKDLHIHV SCRMLQDSWV HTMYIANDTI EVSEVQYSNF NVNVSFYTSS
SFSYPVTSSP YYVDLDQNLY LQAEILHSDA SLALFVDTCV ASPNPNDFTS VTYDLIRSGC
VRDETYRSYA QPSPRVVRFR FNSFHFLNRF PAVYLRCKMV VCRAYDYSSR CYRGCVVRSK
RDVGSYQERV DVVLGPIQLL DPPAGKKSPG KGSP
