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Protein

Mucin-4

Gene

Muc4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. 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. The MUC4-ERBB2 complex causes site-specific phosphorylation of the ERBB2 'Tyr-1248' (By similarity).By similarity1 Publication

GO - Molecular functioni

  • ErbB-2 class receptor binding Source: RGD
  • protein-containing complex binding Source: RGD

GO - Biological processi

Keywordsi

Biological processCell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Mucin-4
Short name:
MUC-4
Alternative name(s):
Ascites sialoglycoprotein
Short name:
ASGP
Pancreatic adenocarcinoma mucin
Pre-sialomucin complex
Short name:
pSMC
Sialomucin complex
Testis mucin
Cleaved into the following 2 chains:
Alternative name(s):
Ascites sialoglycoprotein 1
Short name:
ASGP-1
Alternative name(s):
Ascites sialoglycoprotein 2
Short name:
ASGP-2
Gene namesi
Name:Muc4
Synonyms:Smc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621331 Muc4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei2173 – 2193HelicalSequence analysisAdd BLAST21
Transmembranei2301 – 2321HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000027423031 – 2344Mucin-4Add BLAST2314
ChainiPRO_000027423131 – 1615Mucin-4 alpha chainAdd BLAST1585
ChainiPRO_00002742321616 – 2344Mucin-4 beta chainAdd BLAST729

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi133O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi391O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi392O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi470O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi479O-linked (GalNAc...) serineSequence analysis1
Glycosylationi1644N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1660N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1672N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1689N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1698N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1704N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1715N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1724N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1759N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1780N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1787N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1829N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1874N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1926N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1951N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1974N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1981N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2029N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2048N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2051 ↔ 2062By similarity
Disulfide bondi2056 ↔ 2074By similarity
Disulfide bondi2076 ↔ 2085By similarity
Glycosylationi2114N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2121N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2227N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2259 ↔ 2270By similarity
Disulfide bondi2264 ↔ 2279By similarity
Disulfide bondi2281 ↔ 2294By similarity

Post-translational modificationi

Proteolytically cleaved into 2 subunits, mucin-4 alpha chain and mucin-4 beta chain.
Mucin-4 alpha subunit is highly O-glycosylated.1 Publication
Mucin-4 beta subunit is predominantly N-glycosylated.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1616 – 1617Cleavage2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ63661

Expressioni

Tissue specificityi

Expression is developmentally regulated in the mammary gland, dramatically increases in the lactating gland compared with the virgin mammary gland, while decreasing again during mammary gland involution. Expressed in 13762 ascites cells. Overexpressed in some aggressive mammary tumors. Overexpression seems to block cell-cell and cell-matrix interactions to protect tumor cells from immune surveillance, and to promote metastasis.

Interactioni

Subunit structurei

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 ERBB3.3 Publications

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ63661
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati81 – 2041Add BLAST124
Repeati205 – 2912Add BLAST87
Repeati292 – 4153Add BLAST124
Repeati416 – 5394Add BLAST124
Repeati540 – 6625Add BLAST123
Repeati663 – 7886Add BLAST126
Repeati789 – 10067Add BLAST218
Domaini1332 – 1492NIDOPROSITE-ProRule annotationAdd BLAST161
Domaini1610 – 1844VWFDPROSITE-ProRule annotationAdd BLAST235
Domaini2047 – 2086EGF-like 1PROSITE-ProRule annotationAdd BLAST40
Domaini2256 – 2295EGF-like 2PROSITE-ProRule annotationAdd BLAST40

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi31 – 1266Thr-richAdd BLAST1236
Compositional biasi259 – 268Poly-Thr10
Compositional biasi445 – 1203Ser-richAdd BLAST759
Compositional biasi477 – 484Poly-Ser8
Compositional biasi874 – 883Poly-Thr10

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG081997
InParanoidiQ63661

Family and domain databases

InterProiView protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR003886 NIDO_dom
IPR001846 VWF_type-D
PfamiView protein in Pfam
PF06119 NIDO, 1 hit
PF00094 VWD, 1 hit
SMARTiView protein in SMART
SM00181 EGF, 3 hits
SM00539 NIDO, 1 hit
SM00216 VWD, 1 hit
PROSITEiView protein in PROSITE
PS00022 EGF_1, 2 hits
PS50026 EGF_3, 2 hits
PS51220 NIDO, 1 hit
PS51233 VWFD, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63661-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRGPHGVSWR VPWLCLSCLC SCLLLLPVNT STTSAPKTST ALPSSTNPSQ
60 70 80 90 100
MTSQVSNPTA SSYRMTKNTG QASPMVTSSS ITTLPQSQHT GSMKTTRNPQ
110 120 130 140 150
TTGTTEVTTT LSASSSDQVQ VETTSQTTLS PDTTTTSHAP RESSSPPSTS
160 170 180 190 200
VILTTTASTE GTSGDTGHTM AVTTQGSTPA TTEISVTPST QKMSPVSTFS
210 220 230 240 250
TSTQEITTLS QSQHTGGMKT TRNPQTTGTT EVTTTLSASS SDHPTSSPES
260 270 280 290 300
TPGNTAPRTT ETSTTTTTKV LMTSLQQKLP TGSTLGTSTQ ELTTLPQSQH
310 320 330 340 350
TGIMKTTSRT QTTTPTEVTT RTLSASSSDH RQAETSSQTT LSPDTTTTSH
360 370 380 390 400
APRESSPPST SVILTHGHRE GTSGDTGHTM AVTTQGSTPA TTEISVTPST
410 420 430 440 450
QKMSPVSTFS TSTQEITTLS QSQHTGGMKT TRNPQRTTPT EVTTSTLSAS
460 470 480 490 500
SSDQVQVETT SRATLSPDTT TTSHAPSVSS SSPSPPSTEG TSVDTGLTTA
510 520 530 540 550
VTTQDSTPAT TQGSLTSSSQ TLSTVSPLST STQETSTQEL TSSQSQHTGS
560 570 580 590 600
MKTTHNPQTT RNTEVTTTLS ASSSDQVQVE TTSQTTLSDA TTTSHAPRES
610 620 630 640 650
SSPPSTSDIL TTMASTEGTS GDTGHTMAVT TQGSTPATTE ISVTPSTQKM
660 670 680 690 700
SPVSTFSTST QEITTLSQSQ HTGGMKTTRN PQTTGTTEVT TTLSASSSDQ
710 720 730 740 750
VQAETSSQTT LSPDTTTTSH APRESSSPPS TSDMLTTTAS TEGTSGDTGH
760 770 780 790 800
TTAVTTQGSI PATTQLSTTF ASQKMSTVST PTTSSIQELS TLPQSQHTGS
810 820 830 840 850
MEISSRPQTT SVTSTLSSSP SGSTPVQTRS VTSSSDERTN PTSSGVSNTS
860 870 880 890 900
PATTEVLTPT SSPESTPGNT APRTTETSTT TTTKVLMTSL QQKLPTGSTL
910 920 930 940 950
GTSTPTEVTT TLSASSSDQV QVETTSQTTL SPDATTTSHA PRESSSPPST
960 970 980 990 1000
SVILTTMAST EGTSGDTGHT TAVTDQGSTP ATTEISVTPS TQKMSTVSTL
1010 1020 1030 1040 1050
VTSTQELTSS QSQRTGSMGT SSKPQATTPT EVTTSTLSSF SRGSLFSARN
1060 1070 1080 1090 1100
CCLQTKKPPL PAVVCLPDPS SVPSLMHSSK PQATTPTEVT TSTLSSFSRG
1110 1120 1130 1140 1150
STQTQTVSWE TSSSGKITAP STSSRRTPSV ATSDIFTTTD STSGNAGHTL
1160 1170 1180 1190 1200
LTGSHSVITS RVASTTLGRL STVAHRQSTQ RSSTHSQSYL TESMGASSTS
1210 1220 1230 1240 1250
ETSLLTEATT ETSLCLFTWT HCDRDLLSWT SSSGLTTKTD NDRSTALSAT
1260 1270 1280 1290 1300
SLTLPAPSTS TASRSTVPPA PLPPDQGISL FQIGFPLGSL CGIPSILQIT
1310 1320 1330 1340 1350
VRSFSPSQTT MSSPTPTHLK EASQEGSVCH SGHSGVMLIS LAPGEPYFRT
1360 1370 1380 1390 1400
TTSHFTMSST SLIRKVESLI NEFTSDWSFK PSDTEVTWVN VPAYPAQGRT
1410 1420 1430 1440 1450
LGANTYQAIL STDGSRSYAL FLYQSGGMRW DVTQGLYNRV LMGFSSGDGY
1460 1470 1480 1490 1500
FENSPLIFRP AVEKYRPDRF LTPNYGSGDS RSTGYTGRCG PTTGSSVCSG
1510 1520 1530 1540 1550
WKVSLSSPAG AGTRFPALAP GSRDFGSGSS TQVCGAGSYA ASLRAGRVLY
1560 1570 1580 1590 1600
VWHLGEFREG WRMHSPWQFD EDEGRHRTGL AAGTTSPLSA SSTSSGGPEL
1610 1620 1630 1640 1650
VVLGTRPPRP AWTFGDPHIT TLDNAKYTFN GLGYFLLVQA QDRNSSFLLE
1660 1670 1680 1690 1700
GRTAQTDSAN ATNFIAFAAQ YNTSSLKSPI TVQWFLEPND TIRVVHNNQT
1710 1720 1730 1740 1750
VAFNTSDTED LPVFNATGVL LIQNGSQVSA NFDGTVTISV IALSNILHAS
1760 1770 1780 1790 1800
SSLSEEYRNH TKGLLGVWND NPEDDFRMPN GSTIPSNTSE ETLFHYGMTS
1810 1820 1830 1840 1850
ETNGIGLLGV RTDPLPSEFT PIFLSQLWNK SGAGEDLISG CNEDAQCKFD
1860 1870 1880 1890 1900
ILATGNRDIG QSTNSILRTF RHVNGTLNQY PPPIHYSSKI QAYKGREQWP
1910 1920 1930 1940 1950
LRSPATLRMS YSASPTSAVA FELFENGSLH VDTNIPRRTY LEILARDVKT
1960 1970 1980 1990 2000
NLSSVLQPET VACFCSKEEQ CLYNETSKEG NSSTEVTSCK CDGNSFGRLC
2010 2020 2030 2040 2050
EHSKDLCTEP CFPNVDCIPG KGCQACPPNM TGDGRHCVAV EISEFCQNHS
2060 2070 2080 2090 2100
CPVNYCYNHG HCDISGPPDC QPTCTCAPAF TGNRCFLAGN NFTPIIYKEL
2110 2120 2130 2140 2150
PLRTITLSLR EDENASNADV NASVANVLEN LDMRAFLSNS LVELIRTSPG
2160 2170 2180 2190 2200
APVLGKPIHH WKVVSHFKYR PRGPLIHYLN NQLISAVMEA FLLQARQERR
2210 2220 2230 2240 2250
KRSGEARKNV RFFPISRADV QDGMALNLSM LDEYFTCDGY KGYHLVYSPQ
2260 2270 2280 2290 2300
DGVTCVSPCS EGYCHNGGQC KHLPDGPQCT CATFSIYTSW GERCEHLSVK
2310 2320 2330 2340
LGAFFGILFG ALGALLLLAI LACVVFHFCG CSMNKFSYPL DSEL
Length:2,344
Mass (Da):248,041
Last modified:February 6, 2007 - v2
Checksum:i0182776F4FDE997F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti81I → L in AAA85519 (PubMed:8163496).Curated1
Sequence conflicti81I → L in AAA85521 (PubMed:8163496).Curated1
Sequence conflicti92S → G in AAA85519 (PubMed:8163496).Curated1
Sequence conflicti92S → G in AAA85521 (PubMed:8163496).Curated1
Sequence conflicti103 – 104GT → RN in AAA85519 (PubMed:8163496).Curated2
Sequence conflicti103 – 104GT → RN in AAA85521 (PubMed:8163496).Curated2
Sequence conflicti110T → A in AAA85521 (PubMed:8163496).Curated1
Sequence conflicti126 – 127QT → RA in AAA85521 (PubMed:8163496).Curated2
Sequence conflicti128T → A in AAA85519 (PubMed:8163496).Curated1
Sequence conflicti133T → A in AAA85521 (PubMed:8163496).Curated1
Sequence conflicti141 – 143RES → ER in AAA85519 (PubMed:8163496).Curated3
Sequence conflicti150 – 485Missing in AAA85519 (PubMed:8163496).CuratedAdd BLAST336
Sequence conflicti156T → M in AAA85521 (PubMed:8163496).Curated1
Sequence conflicti170M → T in AAA85521 (PubMed:8163496).Curated1
Sequence conflicti174T → V in AAA85521 (PubMed:8163496).Curated1
Sequence conflicti490G → V in AAA85519 (PubMed:8163496).Curated1
Sequence conflicti498T → K in AAA85519 (PubMed:8163496).Curated1
Sequence conflicti501 – 502VT → IS in AAA85519 (PubMed:8163496).Curated2
Sequence conflicti505D → G in AAA85519 (PubMed:8163496).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06746 mRNA Translation: AAA85517.1
U06748 mRNA Translation: AAA85519.1
U06750 mRNA Translation: AAA85521.1
U06752 mRNA Translation: AAA85523.1
AF240632 Genomic DNA Translation: AAF86958.1
PIRiA43353
A53577

Genome annotation databases

UCSCiRGD:621331 rat

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06746 mRNA Translation: AAA85517.1
U06748 mRNA Translation: AAA85519.1
U06750 mRNA Translation: AAA85521.1
U06752 mRNA Translation: AAA85523.1
AF240632 Genomic DNA Translation: AAF86958.1
PIRiA43353
A53577

3D structure databases

ProteinModelPortaliQ63661
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ63661

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:621331 rat

Organism-specific databases

RGDi621331 Muc4

Phylogenomic databases

HOVERGENiHBG081997
InParanoidiQ63661

Miscellaneous databases

PROiPR:Q63661

Family and domain databases

InterProiView protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR003886 NIDO_dom
IPR001846 VWF_type-D
PfamiView protein in Pfam
PF06119 NIDO, 1 hit
PF00094 VWD, 1 hit
SMARTiView protein in SMART
SM00181 EGF, 3 hits
SM00539 NIDO, 1 hit
SM00216 VWD, 1 hit
PROSITEiView protein in PROSITE
PS00022 EGF_1, 2 hits
PS50026 EGF_3, 2 hits
PS51220 NIDO, 1 hit
PS51233 VWFD, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMUC4_RAT
AccessioniPrimary (citable) accession number: Q63661
Secondary accession number(s): Q63655
, Q63657, Q63659, Q9JIC4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: June 20, 2018
This is version 97 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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