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Mucin-4 (MUC-4) (Ascites sialoglycoprotein) (ASGP) (Pancreatic adenocarcinoma mucin) (Testis mucin) (Tracheobronchial mucin) [Cleaved into: Mucin-4 alpha chain (Ascites sialoglycoprotein 1) (ASGP-1); Mucin-4 beta chain (Ascites sialoglycoprotein 2) (ASGP-2)]

 MUC4_HUMAN              Reviewed;        2169 AA.
Q99102; O95938; Q9GZM2; Q9GZV6; Q9H481; Q9H482; Q9H483; Q9H484;
Q9H485; Q9H486; Q9H487; Q9H4D6; Q9H4D8; Q9NPJ0; Q9NY09; Q9NY75;
Q9NY76; Q9NY77; Q9NY78; Q9NY79; Q9NY80; Q9NY81;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 4.
25-OCT-2017, entry version 143.
RecName: Full=Mucin-4;
Short=MUC-4;
AltName: Full=Ascites sialoglycoprotein;
Short=ASGP;
AltName: Full=Pancreatic adenocarcinoma mucin;
AltName: Full=Testis mucin;
AltName: Full=Tracheobronchial mucin;
Contains:
RecName: Full=Mucin-4 alpha chain;
AltName: Full=Ascites sialoglycoprotein 1;
Short=ASGP-1;
Contains:
RecName: Full=Mucin-4 beta chain;
AltName: Full=Ascites sialoglycoprotein 2;
Short=ASGP-2;
Flags: Precursor;
Name=MUC4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12 AND 13), PARTIAL NUCLEOTIDE
SEQUENCE [MRNA] (ISOFORMS 2; 3; 11; 15; 16 AND 17), TISSUE
SPECIFICITY, AND VARIANT ASP-1081.
TISSUE=Lung, and Testis;
PubMed=10880978; DOI=10.1046/j.1432-1327.2000.01504.x;
Moniaux N., Escande F., Batra S.K., Porchet N., Laine A.,
Aubert J.-P.;
"Alternative splicing generates a family of putative secreted and
membrane-associated MUC4 mucins.";
Eur. J. Biochem. 267:4536-4544(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5; 7; 8; 9; 10 AND 11),
TISSUE SPECIFICITY, AND VARIANTS PRO-41 AND ASP-1081.
TISSUE=Pancreatic tumor;
PubMed=10920259; DOI=10.1093/oxfordjournals.jbchem.a022746;
Choudhury A., Moniaux N., Winpenny J.P., Hollingsworth M.A.,
Aubert J.-P., Batra S.K.;
"Human MUC4 mucin cDNA and its variants in pancreatic carcinoma.";
J. Biochem. 128:233-243(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-41; ASP-1081 AND
SER-1578.
PubMed=12084055; DOI=10.1046/j.1432-1033.2002.02988.x;
Desseyn J.-L., Clavereau I., Laine A.;
"Cloning, chromosomal localization and characterization of the murine
mucin gene orthologous to human MUC4.";
Eur. J. Biochem. 269:3150-3159(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1014-2169 (ISOFORM 1), TISSUE
SPECIFICITY, AND VARIANT ASP-1081.
TISSUE=Colon mucosa;
PubMed=10024507; DOI=10.1042/bj3380325;
Moniaux N., Nollet S., Porchet N., Degand P., Laine A., Aubert J.-P.;
"Complete sequence of the human mucin MUC4: a putative cell membrane-
associated mucin.";
Biochem. J. 338:325-333(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1014-2169, AND VARIANT ASP-1081.
PubMed=12153560; DOI=10.1046/j.1432-1033.2002.03032.x;
Escande F., Lemaitre L., Moniaux N., Batra S.K., Aubert J.-P.,
Buisine M.P.;
"Genomic organization of MUC4 mucin gene: towards the characterization
of splice variants.";
Eur. J. Biochem. 269:3637-3644(2002).
[6]
PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1673336; DOI=10.1016/0006-291X(91)91580-6;
Porchet N., van Cong N., Dufosse J., Audie J.P., Guyonnet-Duperat V.,
Gross M.S., Denis C., Degand P., Bernheim A., Aubert J.-P.;
"Molecular cloning and chromosomal localization of a novel human
tracheo-bronchial mucin cDNA containing tandemly repeated sequences of
48 base pairs.";
Biochem. Biophys. Res. Commun. 175:414-422(1991).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12102554; DOI=10.1016/S0079-6603(02)71043-X;
Carraway K.L., Perez A., Idris N., Jepson S., Arango M.E., Komatsu M.,
Haq B., Price-Schiavi S.A., Zhang J., Carraway C.A.;
"Muc4/sialomucin complex, the intramembrane ErbB2 ligand, in cancer
and epithelia: to protect and to survive.";
Prog. Nucleic Acid Res. Mol. Biol. 71:149-185(2002).
[9]
FUNCTION.
PubMed=16049287; DOI=10.1136/jcp.2004.023572;
Saitou M., Goto M., Horinouchi M., Tamada S., Nagata K., Hamada T.,
Osako M., Takao S., Batra S.K., Aikou T., Imai K., Yonezawa S.;
"MUC4 expression is a novel prognostic factor in patients with
invasive ductal carcinoma of the pancreas.";
J. Clin. Pathol. 58:845-852(2005).
[10]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=16814944; DOI=10.1016/j.prp.2006.04.002;
Karg A., Dinc Z.A., Basok O., Ucvet A.;
"MUC4 expression and its relation to ErbB2 expression, apoptosis,
proliferation, differentiation, and tumor stage in non-small cell lung
cancer (NSCLC).";
Pathol. Res. Pract. 202:577-583(2006).
[11]
DEVELOPMENTAL STAGE, AND FUNCTION.
PubMed=16914178; DOI=10.1016/j.tice.2006.06.004;
Zhang J., Yasin M., Carraway C.A., Carraway K.L.;
"MUC4 expression and localization in gastrointestinal tract and skin
of human embryos.";
Tissue Cell 38:271-275(2006).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1809.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
-!- FUNCTION: May play a role in tumor progression. Ability to promote
tumor growth may be mainly due to repression of apoptosis as
opposed to proliferation. Has anti-adhesive properties. Seems to
alter cellular behavior through both anti-adhesive effects on
cell-cell and cell-extracellular matrix interactions and in its
ability to act as an intramembrane ligand for ERBB2. Plays an
important role in cell proliferation and differentiation of
epithelial cells by inducing specific phosphorylation of ERBB2.
The MUC4-ERBB2 complex causes site-specific phosphorylation of the
ERBB2 'Tyr-1248'. In polarized epithelial cells segregates ERBB2
and other ERBB receptors and prevents ERBB2 from acting as a
coreceptor. The interaction with ERBB2 leads to enhanced
expression of CDKN1B. The formation of a MUC4-ERBB2-ERBB3-NRG1
complex leads to down-regulation of CDKN1B, resulting in
repression of apoptosis and stimulation of proliferation.
{ECO:0000269|PubMed:12102554, ECO:0000269|PubMed:16049287,
ECO:0000269|PubMed:16814944, ECO:0000269|PubMed:16914178}.
-!- SUBUNIT: A heterodimeric complex, composed of a mucin-4 alpha
chain and a cysteine-rich transmembrane mucin-4 beta chain. Mucin-
4 beta chain interacts with ERBB2 via the EGF-like domain 1. In
nonpolarized cells, associates with ERBB2 and ERBB3 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:12102554}.
Note=Isoforms lacking the Cys-rich region, EGF-like domains and
transmembrane region are secreted. Secretion occurs by splicing or
proteolytic processing.
-!- SUBCELLULAR LOCATION: Mucin-4 beta chain: Cell membrane; Single-
pass membrane protein.
-!- SUBCELLULAR LOCATION: Mucin-4 alpha chain: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane; Single-pass
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 11: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 15: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 17: Cell membrane; Single-pass
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=14;
Comment=Additional isoforms exist.;
Name=1;
IsoId=Q99102-1; Sequence=Displayed;
Name=2; Synonyms=Sv12, Sv13;
IsoId=Q99102-2; Sequence=VSP_022658, VSP_022659;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3; Synonyms=Sv20;
IsoId=Q99102-3; Sequence=VSP_022674, VSP_022675;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=5; Synonyms=Sv18, Sv19;
IsoId=Q99102-5; Sequence=VSP_022661, VSP_022669, VSP_022670;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=7; Synonyms=Sv16;
IsoId=Q99102-7; Sequence=VSP_022656, VSP_022665;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=8; Synonyms=Sv15;
IsoId=Q99102-8; Sequence=VSP_022657, VSP_022664;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=9; Synonyms=Sv11;
IsoId=Q99102-9; Sequence=VSP_022652, VSP_022655;
Note=Dubious isoform produced through aberrant splice sites.;
Name=10; Synonyms=Sv3, Sv17;
IsoId=Q99102-10; Sequence=VSP_022661;
Name=11; Synonyms=Sv2;
IsoId=Q99102-11; Sequence=VSP_022653, VSP_022663;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=12; Synonyms=SvX;
IsoId=Q99102-12; Sequence=VSP_022650;
Note=May be preferentially expressed in tumor tissues.;
Name=13; Synonyms=SvY;
IsoId=Q99102-13; Sequence=VSP_022651;
Note=May be preferentially expressed in tumor tissues.;
Name=15; Synonyms=Sv1;
IsoId=Q99102-15; Sequence=VSP_022654, VSP_022662;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=16; Synonyms=Sv6;
IsoId=Q99102-16; Sequence=VSP_022671, VSP_022673;
Note=Dubious isoform produced through aberrant splice sites.;
Name=17; Synonyms=Sv8;
IsoId=Q99102-17; Sequence=VSP_022672;
Note=Dubious isoform produced through aberrant splice sites.;
-!- TISSUE SPECIFICITY: Expressed in the thymus, thyroid, lung,
trachea, esophagus, stomach, small intestine, colon, testis,
prostate, ovary, uterus, placenta, and mammary and salivary
glands. Expressed in carcinomas arising from some of these
epithelia, such as lung cancers, squamous cell carcinomas of the
upper aerodigestive tract, mammary carcinomas, biliary tract,
colon, and cervix cancers. Minimally or not expressed in the
normal pancreas or chronic pancreatitis, but is highly expressed
in pancreatic tumors and pancreatic tumor cell lines.
{ECO:0000269|PubMed:10024507, ECO:0000269|PubMed:10880978,
ECO:0000269|PubMed:10920259, ECO:0000269|PubMed:16814944}.
-!- DEVELOPMENTAL STAGE: Expressed early in the primitive gut before
respiratory and digestive epithelial cells have acquired their
tissue and cell specificity. Expressed at the basal surface of the
epithelium from week 14 to 26 weeks and then predominantly
localized in only parietal cells. Immediately before birth, found
in the cytoplasm of the mucous columnar epithelial cells. In the
embryo expressed in skin, then disappears late in gestation.
{ECO:0000269|PubMed:16914178}.
-!- PTM: Proteolytically cleaved into 2 chains, mucin-4 alpha chain
and mucin-4 beta chain.
-!- PTM: mucrnin-4 alpha chain is highly O-glycosylated.
{ECO:0000269|PubMed:18780401}.
-!- PTM: mucin-4 beta chain is predominantly N-glycosylated.
{ECO:0000269|PubMed:18780401}.
-!- MISCELLANEOUS: Expression is a very useful predictor of poor
prognosis in patients with invasive ductal carcinoma and
intrahepatic cholangiocarcinoma, mass forming type (IDC,ICC-MF).
Patients with IDC or ICC-MF who have high MUC4 expression had a
worse survival rate than those with low MUC4 expression.
-!- SEQUENCE CAUTION:
Sequence=AAA63230.1; Type=Miscellaneous discrepancy; Note=May be derived from an intron translation.; Evidence={ECO:0000305};
Sequence=CAC14139.1; Type=Frameshift; Positions=1171; Evidence={ECO:0000305};
Sequence=CAC14141.1; Type=Frameshift; Positions=1256; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Mucin database;
URL="http://www.medkem.gu.se/mucinbiology/databases/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MUC4ID41459ch3q29.html";
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EMBL; AJ242541; CAB85597.1; -; mRNA.
EMBL; AJ242542; CAB85598.1; -; mRNA.
EMBL; AJ242543; CAB85599.1; -; mRNA.
EMBL; AJ242544; CAB85600.1; -; mRNA.
EMBL; AJ242545; CAB85601.1; -; mRNA.
EMBL; AJ242546; CAB85602.1; -; mRNA.
EMBL; AJ242547; CAB85603.1; -; mRNA.
EMBL; AJ242548; CAB85604.1; -; mRNA.
EMBL; AJ242549; CAB85605.1; -; mRNA.
EMBL; AJ242550; CAB85606.1; -; mRNA.
EMBL; AJ276359; CAB81773.1; -; mRNA.
EMBL; AJ277412; CAC10061.1; -; mRNA.
EMBL; AJ277505; CAC14585.1; -; mRNA.
EMBL; AJ400633; CAC10062.1; -; mRNA.
EMBL; AJ400849; CAC14134.1; -; mRNA.
EMBL; AJ400850; CAC14135.1; -; mRNA.
EMBL; AJ400851; CAC14136.1; -; mRNA.
EMBL; AJ400852; CAC14137.1; -; mRNA.
EMBL; AJ400855; CAC14140.1; -; mRNA.
EMBL; AJ400853; CAC14138.1; -; mRNA.
EMBL; AJ400854; CAC14139.1; ALT_FRAME; mRNA.
EMBL; AJ400856; CAC14141.1; ALT_FRAME; mRNA.
EMBL; AJ400857; CAC14142.1; -; mRNA.
EMBL; AJ400858; CAC14143.1; -; mRNA.
EMBL; AF522055; AAM66747.1; -; Genomic_DNA.
EMBL; AF522031; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522032; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522033; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522034; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522035; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522036; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522037; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522038; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522039; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522040; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522041; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522042; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522043; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522044; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522045; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522046; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522047; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522048; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522049; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522050; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522051; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522052; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522053; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AF522054; AAM66747.1; JOINED; Genomic_DNA.
EMBL; AJ010901; CAB38059.1; -; mRNA.
EMBL; AJ430032; CAD22550.1; -; Genomic_DNA.
EMBL; AJ430033; CAD22550.1; JOINED; Genomic_DNA.
EMBL; AJ430034; CAD22550.1; JOINED; Genomic_DNA.
EMBL; M64594; AAA63230.1; ALT_SEQ; mRNA.
EMBL; AC069513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC233280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS3310.1; -. [Q99102-13]
CCDS; CCDS3311.1; -. [Q99102-12]
PIR; PN0012; PN0012.
RefSeq; NP_004523.3; NM_004532.5. [Q99102-13]
RefSeq; NP_060876.5; NM_018406.6.
RefSeq; NP_612154.2; NM_138297.4. [Q99102-12]
UniGene; Hs.369646; -.
SMR; Q99102; -.
IntAct; Q99102; 1.
STRING; 9606.ENSP00000417498; -.
iPTMnet; Q99102; -.
PhosphoSitePlus; Q99102; -.
UniCarbKB; Q99102; -.
BioMuta; MUC4; -.
DMDM; 338817990; -.
MaxQB; Q99102; -.
PaxDb; Q99102; -.
PeptideAtlas; Q99102; -.
PRIDE; Q99102; -.
TopDownProteomics; Q99102-3; -. [Q99102-3]
Ensembl; ENST00000346145; ENSP00000304207; ENSG00000145113. [Q99102-13]
Ensembl; ENST00000349607; ENSP00000338109; ENSG00000145113. [Q99102-12]
GeneID; 4585; -.
KEGG; hsa:4585; -.
UCSC; uc003fvo.5; human. [Q99102-1]
CTD; 4585; -.
DisGeNET; 4585; -.
EuPathDB; HostDB:ENSG00000145113.21; -.
GeneCards; MUC4; -.
H-InvDB; HIX0003957; -.
H-InvDB; HIX0163449; -.
HGNC; HGNC:7514; MUC4.
HPA; CAB013536; -.
HPA; HPA005895; -.
MIM; 158372; gene.
neXtProt; NX_Q99102; -.
OpenTargets; ENSG00000145113; -.
PharmGKB; PA31319; -.
eggNOG; ENOG410IHUZ; Eukaryota.
eggNOG; ENOG4111F6U; LUCA.
GeneTree; ENSGT00730000110943; -.
HOVERGEN; HBG081997; -.
InParanoid; Q99102; -.
KO; K22017; -.
Reactome; R-HSA-5083625; Defective GALNT3 causes familial hyperphosphatemic tumoral calcinosis (HFTC).
Reactome; R-HSA-5083632; Defective C1GALT1C1 causes Tn polyagglutination syndrome (TNPS).
Reactome; R-HSA-5083636; Defective GALNT12 causes colorectal cancer 1 (CRCS1).
Reactome; R-HSA-5621480; Dectin-2 family.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
SIGNOR; Q99102; -.
ChiTaRS; MUC4; human.
GeneWiki; MUC4; -.
GenomeRNAi; 4585; -.
PRO; PR:Q99102; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000145113; -.
ExpressionAtlas; Q99102; baseline and differential.
Genevisible; Q99102; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; NAS:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0005176; F:ErbB-2 class receptor binding; TAS:ProtInc.
GO; GO:0030197; F:extracellular matrix constituent, lubricant activity; NAS:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:UniProtKB.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
InterPro; IPR005533; AMOP_dom.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR003886; NIDO_dom.
InterPro; IPR001846; VWF_type-D.
Pfam; PF06119; NIDO; 1.
Pfam; PF00094; VWD; 1.
SMART; SM00723; AMOP; 1.
SMART; SM00181; EGF; 3.
SMART; SM00539; NIDO; 1.
SMART; SM00216; VWD; 1.
PROSITE; PS50856; AMOP; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS51220; NIDO; 1.
PROSITE; PS51233; VWFD; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Polymorphism;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 2169 Mucin-4.
/FTId=PRO_0000158956.
CHAIN 29 1444 Mucin-4 alpha chain.
/FTId=PRO_0000274225.
CHAIN 1445 2169 Mucin-4 beta chain.
/FTId=PRO_0000274226.
TRANSMEM 2126 2146 Helical. {ECO:0000255}.
DOMAIN 1154 1309 NIDO. {ECO:0000255|PROSITE-
ProRule:PRU00570}.
DOMAIN 1310 1425 AMOP. {ECO:0000255|PROSITE-
ProRule:PRU00347}.
DOMAIN 1438 1673 VWFD. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 1875 1914 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2078 2117 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 1002 1038 Repeat.
COMPBIAS 793 1013 Ser-rich.
SITE 1444 1445 Cleavage.
CARBOHYD 161 161 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1472 1472 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1525 1525 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1544 1544 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1553 1553 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1588 1588 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1609 1609 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1632 1632 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1659 1659 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1685 1685 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1703 1703 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1739 1739 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1754 1754 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1802 1802 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1809 1809 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
CARBOHYD 1857 1857 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1876 1876 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1942 1942 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1949 1949 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2049 2049 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1879 1890 {ECO:0000250}.
DISULFID 1884 1902 {ECO:0000250}.
DISULFID 1904 1913 {ECO:0000250}.
DISULFID 2081 2092 {ECO:0000250}.
DISULFID 2086 2101 {ECO:0000250}.
DISULFID 2103 2116 {ECO:0000250}.
VAR_SEQ 29 1072 Missing (in isoform 12).
{ECO:0000303|PubMed:10880978}.
/FTId=VSP_022650.
VAR_SEQ 29 1021 Missing (in isoform 13).
{ECO:0000303|PubMed:10880978}.
/FTId=VSP_022651.
VAR_SEQ 1071 1107 RGVSLFPYGAGAGDLEFVRRTVDFTSPLFKPATGFPL ->
SPLWGRRRGPGVRQEDRGLHLPTLQAGDWLPP (in
isoform 9).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022652.
VAR_SEQ 1073 1187 VSLFPYGAGAGDLEFVRRTVDFTSPLFKPATGFPLGSSLRD
SLYFTDNGQIIFPESDYQIFSYPNPLPTGFTGRDPVALVAP
FWDDADFSTGRGTTFYQEYETFYGEHSLLVQQA -> EAIQ
EFPSSPMGQTPGTWSSSGGPWTSPPHSSSRRLASPLAPLSV
IPSTSQTMARSSSQSQTTRFSPTPTHSQQASQAGTLWPWWL
RSGTMLTSPLVGGPHFIRNTRRSMVNTAC (in isoform
11). {ECO:0000303|PubMed:10920259}.
/FTId=VSP_022653.
VAR_SEQ 1073 1177 VSLFPYGAGAGDLEFVRRTVDFTSPLFKPATGFPLGSSLRD
SLYFTDNGQIIFPESDYQIFSYPNPLPTGFTGRDPVALVAP
FWDDADFSTGRGTTFYQEYETFY -> AIQEFPSSPMGQTP
GTWSSSGGPWTSPPHSSSRRLASPLAPLSVIPSTSQTMARS
SSQSQTTRFSPTPTHSQQASQAGTLWPWWLRSGTMLTSPLV
GGPHFIRL (in isoform 15). {ECO:0000305}.
/FTId=VSP_022654.
VAR_SEQ 1108 2169 Missing (in isoform 9).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022655.
VAR_SEQ 1117 1201 FTDNGQIIFPESDYQIFSYPNPLPTGFTGRDPVALVAPFWD
DADFSTGRGTTFYQEYETFYGEHSLLVQQAESWIRKMTNNG
GYK -> ASQAGTLWPWWLRSGTMLTSPLVGGPHFIRATPT
KPSSPRTGAGPMPCFSTRAVGCSGTWPSAQWRWLFRKQPTD
VPASVGEVSP (in isoform 7).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022656.
VAR_SEQ 1117 1199 FTDNGQIIFPESDYQIFSYPNPLPTGFTGRDPVALVAPFWD
DADFSTGRGTTFYQEYETFYGEHSLLVQQAESWIRKMTNNG
G -> ASQAGTLWPWWLRSGTMLTSPLVGGPHFIRATPTKP
SSPRTGAGPMPCFSTRAVGCSGTWPSAQASRCSWASLVEMA
FSKTAH (in isoform 8).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022657.
VAR_SEQ 1117 1157 FTDNGQIIFPESDYQIFSYPNPLPTGFTGRDPVALVAPFWD
-> ASQAGTLWPWWLRSGTMLTSPLVGGPHFIRNTRRSMVN
TAC (in isoform 2).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022658.
VAR_SEQ 1158 2169 Missing (in isoform 2).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022659.
VAR_SEQ 1172 1223 Missing (in isoform 5 and isoform 10).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022661.
VAR_SEQ 1178 2169 Missing (in isoform 15). {ECO:0000305}.
/FTId=VSP_022662.
VAR_SEQ 1188 2169 Missing (in isoform 11).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022663.
VAR_SEQ 1200 2169 Missing (in isoform 8).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022664.
VAR_SEQ 1202 2169 Missing (in isoform 7).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022665.
VAR_SEQ 1258 1267 GNPVLMGFSS -> VEMAFSKTAH (in isoform 5).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022669.
VAR_SEQ 1268 2169 Missing (in isoform 5).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022670.
VAR_SEQ 1336 1384 VSCPCSWQQGRRDLRFQPVSIGRWGLGSRQLCSFTSWRGGV
CCSYGPWG -> AAPPRLAQPRPPTSSPLRLSTAPAAWAPS
RSNGSLSLTTQSVSCWITRL (in isoform 16).
{ECO:0000305}.
/FTId=VSP_022671.
VAR_SEQ 1354 1579 Missing (in isoform 17). {ECO:0000305}.
/FTId=VSP_022672.
VAR_SEQ 1385 2169 Missing (in isoform 16). {ECO:0000305}.
/FTId=VSP_022673.
VAR_SEQ 1814 1827 VAGCKCDGGTFGRY -> LWGALSCVRTSPAL (in
isoform 3).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022674.
VAR_SEQ 1828 2169 Missing (in isoform 3).
{ECO:0000303|PubMed:10920259}.
/FTId=VSP_022675.
VARIANT 37 37 G -> D (in dbSNP:rs2259292).
/FTId=VAR_030211.
VARIANT 41 41 A -> P (in dbSNP:rs3107764).
{ECO:0000269|PubMed:10920259,
ECO:0000269|PubMed:12084055}.
/FTId=VAR_065261.
VARIANT 161 161 T -> A (in dbSNP:rs2293232).
/FTId=VAR_030212.
VARIANT 585 585 S -> A (in dbSNP:rs2246901).
/FTId=VAR_030213.
VARIANT 721 721 A -> T (in dbSNP:rs3749331).
/FTId=VAR_056585.
VARIANT 1081 1081 G -> D (in dbSNP:rs2259292).
{ECO:0000269|PubMed:10024507,
ECO:0000269|PubMed:10880978,
ECO:0000269|PubMed:10920259,
ECO:0000269|PubMed:12084055,
ECO:0000269|PubMed:12153560}.
/FTId=VAR_065262.
VARIANT 1205 1205 A -> T (in dbSNP:rs2293232).
/FTId=VAR_056586.
VARIANT 1578 1578 A -> S (in dbSNP:rs2246901).
{ECO:0000269|PubMed:12084055}.
/FTId=VAR_056587.
CONFLICT 1194 1194 M -> I (in Ref. 1; CAB85602/CAB85603/
CAB85604/CAB85605/CAB85606, 2; CAB81773/
CAC14141/CAC14142/CAC14143, 3; AAM66747,
4; CAD22550 and 5; CAB38059).
{ECO:0000305}.
CONFLICT 1259 1259 N -> K (in Ref. 2; CAB81773/CAC14143/
CAC10061 and 3; AAM66747). {ECO:0000305}.
CONFLICT 1271 1271 Y -> F (in Ref. 2; CAB81773/CAC14143/
CAC10061 and 3; AAM66747). {ECO:0000305}.
CONFLICT 1305 1305 R -> G (in Ref. 2; CAB81773/CAC14143/
CAC10061 and 3; AAM66747). {ECO:0000305}.
CONFLICT 1557 1557 V -> A (in Ref. 2; CAB81773/CAC14143/
CAC10061 and 3; AAM66747). {ECO:0000305}.
CONFLICT 1920 1921 Missing (in Ref. 2; CAC14143).
{ECO:0000305}.
CONFLICT 2039 2039 G -> E (in Ref. 1; CAB85604/CAB85605/
CAB85606, 4; CAD22550 and 5; CAB38059).
{ECO:0000305}.
SEQUENCE 2169 AA; 231518 MW; 53615AF8DD416957 CRC64;
MKGARWRRVP WVSLSCLCLC LLPHVVPGTT EDTLITGSKT AAPVTSTGST TATLEGQSTA
ASSRTSNQDI SASSQNHQTK STETTSKAQT DTLTQMMTST LFSSPSVHNV METVTQETAP
PDEMTTSFPS SVTNTLMMTS KTITMTTSTD STLGNTEETS TAGTESSTPV TSAVSITAGQ
EGQSRTTSWR TSIQDTSASS QNHWTRSTQT TRESQTSTLT HRTTSTPSFS PSVHNVTGTV
SQKTSPSGET ATSSLCSVTN TSMMTSEKIT VTTSTGSTLG NPGETSSVPV TGSLMPVTSA
ALVTVDPEGQ SPATFSRTST QDTTAFSKNH QTQSVETTRV SQINTLNTLT PVTTSTVLSS
PSGFNPSGTV SQETFPSGET TISSPSSVSN TFLVTSKVFR MPISRDSTLG NTEETSLSVS
GTISAITSKV STIWWSDTLS TALSPSSLPP KISTAFHTQQ SEGAETTGRP HERSSFSPGV
SQEIFTLHET TTWPSSFSSK GHTTWSQTEL PSTSTGAATR LVTGNPSTRA AGTIPRVPSK
VSAIGEPGEP TTYSSHSTTL PKTTGAGAQT QWTQETGTTG EALLSSPSYS VIQMIKTATS
PSSSPMLDRH TSQQITTAPS TNHSTIHSTS TSPQESPAVS QRGHTRAPQT TQESQTTRSV
SPMTDTKTVT TPGSSFTASG HSPSEIVPQD APTISAATTF APAPTGNGHT TQAPTTALQA
APSSHDATLG PSGGTSLSKT GALTLANSVV STPGGPEGQW TSASASTSPD TAAAMTHTHQ
AESTEASGQT QTSEPASSGS RTTSAGTATP SSSGASGTTP SGSEGISTSG ETTRFSSNPS
RDSHTTQSTT ELLSASASHG AIPVSTGMAS SIVPGTFHPT LSEASTAGRP TGQSSPTSPS
ASPQETAAIS RMAQTQRTGT SRGSDTISLA SQATDTFSTV PPTPPSITSS GLTSPQTQTH
TLSPSGSGKT FTTALISNAT PLPVTSTSSA STGHATPLAV SSATSASTVS SDSPLKMETS
GMTTPSLKTD GGRRTATSPP PTTSQTIIST IPSTAMHTRS TAAPIPILPE RGVSLFPYGA
GAGDLEFVRR TVDFTSPLFK PATGFPLGSS LRDSLYFTDN GQIIFPESDY QIFSYPNPLP
TGFTGRDPVA LVAPFWDDAD FSTGRGTTFY QEYETFYGEH SLLVQQAESW IRKMTNNGGY
KARWALKVTW VNAHAYPAQW TLGSNTYQAI LSTDGSRSYA LFLYQSGGMQ WDVAQRSGNP
VLMGFSSGDG YFENSPLMSQ PVWERYRPDR FLNSNSGLQG LQFYRLHREE RPNYRLECLQ
WLKSQPRWPS WGWNQVSCPC SWQQGRRDLR FQPVSIGRWG LGSRQLCSFT SWRGGVCCSY
GPWGEFREGW HVQRPWQLAQ ELEPQSWCCR WNDKPYLCAL YQQRRPHVGC ATYRPPQPAW
MFGDPHITTL DGVSYTFNGL GDFLLVGAQD GNSSFLLQGR TAQTGSAQAT NFIAFAAQYR
SSSLGPVTVQ WLLEPHDAIR VLLDNQTVTF QPDHEDGGGQ ETFNATGVLL SRNGSEVSAS
FDGWATVSVI ALSNILHASA SLPPEYQNRT EGLLGVWNNN PEDDFRMPNG STIPPGSPEE
MLFHFGMTWQ INGTGLLGKR NDQLPSNFTP VFYSQLQKNS SWAEHLISNC DGDSSCIYDT
LALRNASIGL HTREVSKNYE QANATLNQYP PSINGGRVIE AYKGQTTLIQ YTSNAEDANF
TLRDSCTDLE LFENGTLLWT PKSLEPFTLE ILARSAKIGL ASALQPRTVV CHCNAESQCL
YNQTSRVGNS SLEVAGCKCD GGTFGRYCEG SEDACEEPCF PSVHCVPGKG CEACPPNLTG
DGRHCAALGS SFLCQNQSCP VNYCYNQGHC YISQTLGCQP MCTCPPAFTD SRCFLAGNNF
SPTVNLELPL RVIQLLLSEE ENASMAEVNA SVAYRLGTLD MRAFLRNSQV ERIDSAAPAS
GSPIQHWMVI SEFQYRPRGP VIDFLNNQLL AAVVEAFLYH VPRRSEEPRN DVVFQPISGE
DVRDVTALNV STLKAYFRCD GYKGYDLVYS PQSGFTCVSP CSRGYCDHGG QCQHLPSGPR
CSCVSFSIYT AWGEHCEHLS MKLDAFFGIF FGALGGLLLL GVGTFVVLRF WGCSGARFSY
FLNSAEALP


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