DMBT1_MOUSE
ID DMBT1_MOUSE Reviewed; 2085 AA.
AC Q60997; Q80YC6; Q9JMJ9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Deleted in malignant brain tumors 1 protein;
DE AltName: Full=Apactin;
DE AltName: Full=CRP-ductin;
DE AltName: Full=Glycoprotein 300;
DE Short=gp300;
DE AltName: Full=Hensin;
DE AltName: Full=Mucin-like glycoprotein;
DE Short=Muclin;
DE AltName: Full=Vomeroglandin;
DE AltName: Full=p80;
DE Flags: Precursor;
GN Name=Dmbt1; Synonyms=Crpd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION IN EPITHELIAL
RP DIFFERENTIATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Jejunal epithelium;
RX PubMed=8742698;
RX DOI=10.1002/(sici)1097-0185(199603)244:3<327::aid-ar5>3.0.co;2-v;
RA Cheng H., Bjerknes M., Chen H.;
RT "CRP-ductin: a gene expressed in intestinal crypts and in pancreatic and
RT hepatic ducts.";
RL Anat. Rec. 244:327-343(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PROTEIN SEQUENCE OF 22-40 AND
RP 1942-1957, AND TISSUE SPECIFICITY.
RC STRAIN=ddY;
RX PubMed=10679193; DOI=10.1006/bbrc.2000.2104;
RA Matsushita F., Miyawaki A., Mikoshiba K.;
RT "Vomeroglandin/CRP-ductin is strongly expressed in the glands associated
RT with the mouse vomeronasal organ: identification and characterization of
RT mouse vomeroglandin.";
RL Biochem. Biophys. Res. Commun. 268:275-281(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=7876332; DOI=10.1002/jcb.240560315;
RA De Lisle R.C.;
RT "Characterization of the major sulfated protein of mouse pancreatic acinar
RT cells: a high molecular weight peripheral membrane glycoprotein of zymogen
RT granules.";
RL J. Cell. Biochem. 56:385-396(1994).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=7537458; DOI=10.1152/ajpgi.1995.268.4.g717;
RA De Lisle R.C.;
RT "Increased expression of sulfated gp300 and acinar tissue pathology in
RT pancreas of CFTR(-/-) mice.";
RL Am. J. Physiol. 268:G717-G723(1995).
RN [6]
RP DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=8543783; DOI=10.1177/44.1.8543783;
RA De Lisle R.C., Isom K.S.;
RT "Expression of sulfated gp300 and changes in glycosylation during
RT pancreatic development.";
RL J. Histochem. Cytochem. 44:57-66(1996).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9247472; DOI=10.1053/gast.1997.v113.pm9247472;
RA De Lisle R.C., Petitt M., Huff J., Isom K.S., Agbas A.;
RT "Muclin expression in the cystic fibrosis transmembrane conductance
RT regulator knockout mouse.";
RL Gastroenterology 113:521-532(1997).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=9688648; DOI=10.1152/ajpgi.1998.275.2.g219;
RA De Lisle R.C., Petitt M., Isom K.S., Ziemer D.;
RT "Developmental expression of a mucinlike glycoprotein (MUCLIN) in pancreas
RT and small intestine of CF mice.";
RL Am. J. Physiol. 275:G219-G227(1998).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11152281; DOI=10.1078/0171-9335-00121;
RA De Lisle R.C., Ziemer D.;
RT "Processing of pro-muclin and divergent trafficking of its products to
RT zymogen granules and the apical plasma membrane of pancreatic acinar
RT cells.";
RL Eur. J. Cell Biol. 79:892-904(2000).
RN [10]
RP FUNCTION.
RX PubMed=12082154; DOI=10.1242/jcs.115.14.2941;
RA De Lisle R.C.;
RT "Role of sulfated O-linked glycoproteins in zymogen granule formation.";
RL J. Cell Sci. 115:2941-2952(2002).
RN [11]
RP FUNCTION, INTERACTION WITH SFTPD, AND TISSUE SPECIFICITY.
RX PubMed=12884308; DOI=10.1002/eji.200323972;
RA Madsen J., Tornoee I., Nielsen O., Lausen M., Krebs I., Mollenhauer J.,
RA Kollender G., Poustka A., Skjodt K., Holmskov U.;
RT "CRP-ductin, the mouse homologue of gp-340/deleted in malignant brain
RT tumors 1 (DMBT1), binds gram-positive and gram-negative bacteria and
RT interacts with lung surfactant protein D.";
RL Eur. J. Immunol. 33:2327-2336(2003).
RN [12]
RP FUNCTION, PHOSPHORYLATION AT THR-2073 AND SER-2082, AND MUTAGENESIS OF
RP THR-2073 AND SER-2082.
RX PubMed=15146979; DOI=10.1078/0171-9335-00361;
RA Tandon C., De Lisle R.C.;
RT "Apactin is involved in remodeling of the actin cytoskeleton during
RT regulated exocytosis.";
RL Eur. J. Cell Biol. 83:79-89(2004).
RN [13]
RP FUNCTION.
RX PubMed=15292166; DOI=10.1074/jbc.m406213200;
RA Boulatnikov I., De Lisle R.C.;
RT "Binding of the Golgi sorting receptor muclin to pancreatic zymogens
RT through sulfated O-linked oligosaccharides.";
RL J. Biol. Chem. 279:40918-40926(2004).
RN [14]
RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15452149; DOI=10.1083/jcb.200405159;
RA Takito J., Al-Awqati Q.;
RT "Conversion of ES cells to columnar epithelia by hensin and to squamous
RT epithelia by laminin.";
RL J. Cell Biol. 166:1093-1102(2004).
RN [15]
RP FUNCTION.
RX PubMed=15987769; DOI=10.1152/ajpcell.00099.2005;
RA De Lisle R.C., Norkina O., Roach E., Ziemer D.;
RT "Expression of pro-muclin in pancreatic AR42J cells induces functional
RT regulated secretory granules.";
RL Am. J. Physiol. 289:C1169-C1178(2005).
RN [16]
RP DISRUPTION PHENOTYPE.
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 [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=18202109; DOI=10.1152/ajpgi.00525.2007;
RA De Lisle R.C., Xu W., Roe B.A., Ziemer D.;
RT "Effects of muclin (Dmbt1) deficiency on the gastrointestinal system.";
RL Am. J. Physiol. 294:G717-G727(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Required for terminal
CC differentiation of columnar epithelial cells during early
CC embryogenesis. 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:0000250, ECO:0000269|PubMed:11152281, ECO:0000269|PubMed:12082154,
CC ECO:0000269|PubMed:12884308, ECO:0000269|PubMed:15146979,
CC ECO:0000269|PubMed:15292166, ECO:0000269|PubMed:15452149,
CC ECO:0000269|PubMed:15987769, ECO:0000269|PubMed:8742698}.
CC -!- SUBUNIT: Interacts with LGALS3. Binds SPAR in a calcium-dependent
CC manner (By similarity). Binds SFTPD in a calcium-dependent manner.
CC {ECO:0000250, ECO:0000269|PubMed:12884308}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle
CC membrane; Single-pass membrane protein; Lumenal side. Note=Localized to
CC the lumenal aspect of crypt cells in the small intestine. In the colon,
CC seen in the lumenal aspect of surface epithelial cells. Formed in the
CC ducts of von Ebner gland and released into the fluid bathing the taste
CC buds contained in the taste papillae. In the CFTR knockout mouse,
CC enhanced on the acinar luminar surface.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=CPR-ductin alpha;
CC IsoId=Q60997-1; Sequence=Displayed;
CC Name=2; Synonyms=CPR-ductin beta;
CC IsoId=Q60997-2; Sequence=VSP_016853;
CC Name=3;
CC IsoId=Q60997-3; Sequence=VSP_016851, VSP_016852;
CC Name=4;
CC IsoId=Q60997-4; Sequence=VSP_016852;
CC -!- TISSUE SPECIFICITY: Strongly expressed in acini and duct epithelial
CC cells of the exocrine pancreas but not in the islets of Langerhans.
CC Expressed in gall bladder, salivary glands and in the epithelium lining
CC larger hepatic ducts, but not in the liver parenchyma, stomach or lung.
CC Expressed along the intestinal tract including duodenum, jejunum, ileum
CC and colon (at protein level). Expressed in glands associated with
CC vomeronasal tissues. Expressed in the vomeronasal gland and posterior
CC gland of nasal septum. Weakly expressed in lateral nasal gland. CFTR
CC knockout mice show increased expression in pancreas, duodenum and small
CC intestine but not in gall bladder. In pancreas and small intestine,
CC increased expression occurs after the appearance of dilated lumina.
CC {ECO:0000269|PubMed:10679193, ECO:0000269|PubMed:12884308,
CC ECO:0000269|PubMed:7537458, ECO:0000269|PubMed:8742698,
CC ECO:0000269|PubMed:9247472, ECO:0000269|PubMed:9688648}.
CC -!- DEVELOPMENTAL STAGE: Present in the 3.5 dpc blastocyst. Levels increase
CC to a maximum between 18.5 dpc and birth and decrease gradually between
CC birth and adulthood with the greatest decreases occurring between
CC neonate and P1 and between P9 and P16 (at protein level). Expressed in
CC the primitive endoderm at 4.5 dpc. At 9.5 dpc, expressed in midbrain,
CC notochord, liver primordium, midgut and hindgut.
CC {ECO:0000269|PubMed:15452149, ECO:0000269|PubMed:8543783}.
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 O-glycosylation and sulfation in pancreatic acinar cells are required
CC for zymogen granule maturation. Glycoconjugate composition changes
CC during development with fucose only acquired post-natally during
CC weaning. {ECO:0000269|PubMed:7876332, ECO:0000269|PubMed:8543783}.
CC -!- DISRUPTION PHENOTYPE: Variable phenotypes have been reported. In some
CC studies mice display normal development and viability with impaired
CC exocrine pancreatic function and no development of gastrointestinal
CC tumors (PubMed:17983803 and PubMed:18202109). In other studies mice die
CC between 4.5 dpc and 5.5 dpc due to defects in the differentiation of
CC the primitive endoderm layer (PubMed:15452149).
CC {ECO:0000269|PubMed:15452149, ECO:0000269|PubMed:17983803,
CC ECO:0000269|PubMed:18202109}.
CC -!- SIMILARITY: Belongs to the DMBT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52505.1; Type=Frameshift; Evidence={ECO:0000305};
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; U37438; AAC52505.1; ALT_FRAME; mRNA.
DR EMBL; AB005909; BAA92266.1; -; mRNA.
DR EMBL; BC049835; AAH49835.1; -; mRNA.
DR PIR; T42721; T42721.
DR RefSeq; NP_001334561.1; NM_001347632.1.
DR RefSeq; NP_031795.2; NM_007769.2.
DR AlphaFoldDB; Q60997; -.
DR SMR; Q60997; -.
DR BioGRID; 198900; 4.
DR IntAct; Q60997; 1.
DR MINT; Q60997; -.
DR STRING; 10090.ENSMUSP00000081556; -.
DR GlyGen; Q60997; 21 sites.
DR iPTMnet; Q60997; -.
DR PhosphoSitePlus; Q60997; -.
DR MaxQB; Q60997; -.
DR PaxDb; Q60997; -.
DR PRIDE; Q60997; -.
DR ProteomicsDB; 277340; -. [Q60997-1]
DR ProteomicsDB; 277341; -. [Q60997-2]
DR ProteomicsDB; 277342; -. [Q60997-3]
DR ProteomicsDB; 277343; -. [Q60997-4]
DR DNASU; 12945; -.
DR GeneID; 12945; -.
DR KEGG; mmu:12945; -.
DR CTD; 1755; -.
DR MGI; MGI:106210; Dmbt1.
DR eggNOG; ENOG502RSDM; Eukaryota.
DR InParanoid; Q60997; -.
DR OrthoDB; 1095487at2759; -.
DR PhylomeDB; Q60997; -.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR BioGRID-ORCS; 12945; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Dmbt1; mouse.
DR PRO; PR:Q60997; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60997; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030670; C:phagocytic vesicle membrane; ISO:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042589; C:zymogen granule membrane; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:1904399; F:heparan sulfate binding; ISO:MGI.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
DR GO; GO:0070891; F:lipoteichoic acid binding; ISO:MGI.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISO:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
DR GO; GO:0035375; F:zymogen binding; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR GO; GO:0002065; P:columnar/cuboidal epithelial cell differentiation; IDA:MGI.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0042494; P:detection of bacterial lipoprotein; IBA:GO_Central.
DR GO; GO:0043152; P:induction of bacterial agglutination; ISO:MGI.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IDA:MGI.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR CDD; cd00041; CUB; 5.
DR Gene3D; 2.60.120.290; -; 5.
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; 5.
DR Pfam; PF00530; SRCR; 8.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00042; CUB; 5.
DR SMART; SM00202; SR; 8.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49854; SSF49854; 5.
DR SUPFAM; SSF56487; SSF56487; 8.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS00420; SRCR_1; 8.
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; Cytoplasmic vesicle; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2085
FT /note="Deleted in malignant brain tumors 1 protein"
FT /id="PRO_0000045388"
FT TRANSMEM 2050..2070
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 37..137
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 186..286
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 324..424
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 463..563
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 741..841
FT /note="SRCR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 880..980
FT /note="SRCR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 1023..1132
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1139..1248
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1265..1374
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1381..1490
FT /note="CUB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1510..1610
FT /note="SRCR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 1633..1742
FT /note="CUB 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1751..1999
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT MOD_RES 2073
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15146979"
FT MOD_RES 2082
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15146979"
FT CARBOHYD 1088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..126
FT /evidence="ECO:0000250"
FT DISULFID 75..136
FT /evidence="ECO:0000250"
FT DISULFID 106..116
FT /evidence="ECO:0000250"
FT DISULFID 211..275
FT /evidence="ECO:0000250"
FT DISULFID 224..285
FT /evidence="ECO:0000250"
FT DISULFID 255..265
FT /evidence="ECO:0000250"
FT DISULFID 349..413
FT /evidence="ECO:0000250"
FT DISULFID 362..423
FT /evidence="ECO:0000250"
FT DISULFID 393..403
FT /evidence="ECO:0000250"
FT DISULFID 488..552
FT /evidence="ECO:0000250"
FT DISULFID 501..562
FT /evidence="ECO:0000250"
FT DISULFID 532..542
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 766..830
FT /evidence="ECO:0000250"
FT DISULFID 779..840
FT /evidence="ECO:0000250"
FT DISULFID 810..820
FT /evidence="ECO:0000250"
FT DISULFID 905..969
FT /evidence="ECO:0000250"
FT DISULFID 918..979
FT /evidence="ECO:0000250"
FT DISULFID 949..959
FT /evidence="ECO:0000250"
FT DISULFID 1023..1049
FT /evidence="ECO:0000250"
FT DISULFID 1074..1096
FT /evidence="ECO:0000250"
FT DISULFID 1139..1165
FT /evidence="ECO:0000250"
FT DISULFID 1190..1212
FT /evidence="ECO:0000250"
FT DISULFID 1265..1291
FT /evidence="ECO:0000250"
FT DISULFID 1316..1338
FT /evidence="ECO:0000250"
FT DISULFID 1381..1407
FT /evidence="ECO:0000250"
FT DISULFID 1432..1454
FT /evidence="ECO:0000250"
FT DISULFID 1535..1599
FT /evidence="ECO:0000250"
FT DISULFID 1548..1609
FT /evidence="ECO:0000250"
FT DISULFID 1579..1589
FT /evidence="ECO:0000250"
FT DISULFID 1633..1659
FT /evidence="ECO:0000250"
FT DISULFID 1684..1706
FT /evidence="ECO:0000250"
FT DISULFID 1920..1978
FT /evidence="ECO:0000250"
FT VAR_SEQ 29
FT /note="D -> DEVSYTAEQSTE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10679193"
FT /id="VSP_016851"
FT VAR_SEQ 397..534
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10679193,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016852"
FT VAR_SEQ 2032..2085
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8742698"
FT /id="VSP_016853"
FT MUTAGEN 2073
FT /note="T->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:15146979"
FT MUTAGEN 2082
FT /note="S->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:15146979"
FT CONFLICT 247..248
FT /note="PI -> L (in Ref. 1; AAC52505)"
FT /evidence="ECO:0000305"
FT CONFLICT 1494..1497
FT /note="PPSF -> SLH (in Ref. 1; AAC52505)"
FT /evidence="ECO:0000305"
FT CONFLICT 2061
FT /note="V -> G (in Ref. 2; BAA92266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2085 AA; 226815 MW; 8BE4E77D299B32ED CRC64;
MGISTVIFEI CLLWGQILST ASQTAVPTDG TDSGLAVRLV NGGDRCQGRV EILYQGSWGT
VCDDSWDLND ANVVCRQLGC GLAVSAPGNA RFGQGSGPIV MDDVACGGYE DYLWRCSHRG
WLSHNCGHQE DAGVICSDSQ TSSPTPGWWN PGGTNNDVFY PTEQTTAEQT TIPDYTPIGT
DSGLAVRLVN GGDRCQGRVE ILYQGSWGTV CDDSWDVSDA NVVCRQLGCG WAVSAPGNAY
FGQGQGPIVL DDVACGGYEN YLWSCSHQGW LSHNCGHQED AGVICSASQS SSPTPGWWNP
GGTNNDVFYP TEQTTAGTDS GLAVRLVNGG DRCQGRVEIL YQGSWGTVCD DSWDTNDANV
VCRQLGCGWA VSAPGNAYFG PGSGSIVLDD VACTGHEDYL WRCSHRGWLS HNCGHHEDAG
VICSASQSSS PTPDVFYPTD QTTAEQTTVP DYTPIGTDSG LAVRLVNGGD RCQGRVEILY
QGSWGTVCDD SWDLNDANVV CRQLGCGLAV SAPGSARFGQ GTGPIVMDDV ACGGYEDYLW
RCSHRGWLSH NCGHHEDAGV ICSASQSSSP TPDVFYPTDQ TTAEQTTVPD YTPIGTDSGL
AVRLVNGGDR CQGRVEILYQ GSWGTVCDDS WDLNDANVVC RQLGCGLAVS APGSARFGQG
TGPIVMDDVA CGGYEDYLWR CSHRGWLSHN CGHHEDAGVI CSASQSSSPT PDVFYPTDQT
TAEQTTVPDY TTIGTENSLA VRLENGGDRC QGRVEILYQG SWGTVCDDSW DLNDANVVCR
QLGCGLAVSA PGSARFGQGT GPIVMDDVAC GGYEDYLWRC SHRGWLSHNC GHHEDAGVIC
SASQSSSPTP DVFYPTDQTT VEQTTVPDYT PIGTENSLAV RLENGGDRCQ GRVEILYQGS
WGTVCDDSWD TKDANVVCRQ LGCGWAVSAP GNAYFGPGSG SIVLDDVACT GHEDYLWSCS
HRGWLSHNCG HHEDAGVICS DAQIQSTTRP DLWPTTTTPE TTTELLTTTP YFDWWTTTSD
YSCGGLLTQP SGQFSSPYYP SNYPNNARCS WKIVLPNMNR VTVVFTDVQL EGGCNYDYIL
VYDGPEYNSS LIARVCDGSN GSFTSTGNFM SVVFITDGSV TRRGFQAHYY STVSTNYSCG
GLLTQPSGQF SSPYYPSNYP NNARCSWEIL VPNMNRVTVV FTDVQLEGGC NYDYILVYDG
PQYNSSLIAR VCDGSNGSFT STGNFMSVVF ITDGSVTRRG FQAHYYSTVS TTPPVPIPTT
DDYSCGGLLT LPSGQFSSPH YPSNYPNNAR CSWEILVPNM NRVTVAFTDV QLEGGCNYDY
ILVYDGPEYN SSLIARVCDG SNGSFTSTGN FMSVVFITDG SVTRRGFQAH YYSTVSTNYS
CGGLLTQPSG QFSSPHYPSN YPNNVRCSWE ILVPSMNRVT VAFTDVQLEG GCSFDYILVY
DGPEYNSSLI APVCDGFNGS FTSTGNFMSV VFITDGSVTR RGFQAYYYST VSTPPSFHPN
ITGNDSSLAL RLVNGSNRCE GRVEILYRGS WGTVCDDSWG ISDANVVCRQ LGCGSALSAP
GNAWFGQGSG LIVLDDVSCS GYESHLWNCH HPGWLVHNCR HSEDAGVICA LPEVTSPSPG
WWTTSPSYVN YTCGGFLTQP SGQFSSPFYP GNYPNNARCL WNIEVPNNYR VTVVFRDLQL
ERGCSYDYIE IFDGPHHSSP LIARVCDGSL GSFTSTSNFM SIRFITDHSI TARGFQAHYY
SDFDNNTTNL LCQSNHMQAS VSRSYLQSMG YSARDLVIPG WNSSYHCQPQ ITQREVIFTI
PYTGCGTIKQ ADNETINYSN FLRAVVSNGI IKRRKDLNIH VSCKMLQNTW VNTMYITNNT
VEIQEVQYGN FDVNISFYTS SSFLFPVTSS PYYVDLDQNL YLQAEILHSD ASLALFVDTC
VASPHPNDFS SLTYDLIRSG CVRDDTYQSY SSPSPRVSRF KFSSFHFLNR FPSVYLQCKL
VVCRAYDTSS RCYRGCVVRS KRDVGSYQEK VDVVLGPIQL QSPSKEKRSL DLAVEDVKKP
ASSQAVYPTA AIFGGVFLAM VLAVAAFTLG RRTHIDRGQP PSTKL
