MUC18_MOUSE
ID MUC18_MOUSE Reviewed; 648 AA.
AC Q8R2Y2; Q9EPF1; Q9ESS7; Q9JHQ2; Q9JHQ3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cell surface glycoprotein MUC18;
DE AltName: Full=Gicerin;
DE AltName: Full=Melanoma cell adhesion molecule;
DE AltName: Full=Melanoma-associated antigen MUC18;
DE AltName: CD_antigen=CD146;
DE Flags: Precursor;
GN Name=Mcam; Synonyms=Muc18;
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).
RC STRAIN=BALB/cJ;
RA Taira E., Okumura S., Miki N.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 561-648 (ISOFORMS 1 AND 2).
RX PubMed=11329371; DOI=10.1242/jcs.114.10.1847;
RA Alais S., Allioli N., Pujades C., Duband J.-L., Vainio O., Imhof B.A.,
RA Dunon D.;
RT "HEMCAM/CD146 down regulates cell surface expression of beta-1 integrins.";
RL J. Cell Sci. 114:1847-1859(2001).
RN [4]
RP TISSUE SPECIFICITY, AND ROLE IN MELANOMA.
RX PubMed=11255016; DOI=10.1016/s0378-1119(01)00349-3;
RA Yang H., Wang S.-W., Liu Z., Wu M.-W.H., McAlpine B., Ansel J.,
RA Armstrong C., Wu G.-J.;
RT "Isolation and characterization of mouse MUC18 cDNA gene, and correlation
RT of MUC18 expression in mouse melanoma cell lines with metastatic ability.";
RL Gene 265:133-145(2001).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58 AND ASN-510.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Plays a role in cell adhesion, and in cohesion of the
CC endothelial monolayer at intercellular junctions in vascular tissue.
CC Its expression may allow melanoma cells to interact with cellular
CC elements of the vascular system, thereby enhancing hematogeneous tumor
CC spread. Could be an adhesion molecule active in neural crest cells
CC during embryonic development. Acts as surface receptor that triggers
CC tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase
CC in the intracellular calcium concentration (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=L-gicerin;
CC IsoId=Q8R2Y2-1; Sequence=Displayed;
CC Name=2; Synonyms=S-gicerin;
CC IsoId=Q8R2Y2-2; Sequence=VSP_016940;
CC -!- TISSUE SPECIFICITY: Detected in melanoma cell lines.
CC {ECO:0000269|PubMed:11255016}.
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DR EMBL; AB035508; BAB16050.1; -; mRNA.
DR EMBL; AB035509; BAB16051.1; -; mRNA.
DR EMBL; BC026985; AAH26985.1; -; mRNA.
DR EMBL; AJ297450; CAB97362.1; -; mRNA.
DR EMBL; AJ297451; CAB97363.1; -; mRNA.
DR CCDS; CCDS23097.1; -. [Q8R2Y2-1]
DR CCDS; CCDS90545.1; -. [Q8R2Y2-2]
DR RefSeq; NP_075548.2; NM_023061.2. [Q8R2Y2-1]
DR RefSeq; XP_006510779.1; XM_006510716.2.
DR AlphaFoldDB; Q8R2Y2; -.
DR SMR; Q8R2Y2; -.
DR STRING; 10090.ENSMUSP00000034650; -.
DR BindingDB; Q8R2Y2; -.
DR GlyConnect; 2202; 1 N-Linked glycan (1 site).
DR GlyGen; Q8R2Y2; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8R2Y2; -.
DR PhosphoSitePlus; Q8R2Y2; -.
DR SwissPalm; Q8R2Y2; -.
DR jPOST; Q8R2Y2; -.
DR MaxQB; Q8R2Y2; -.
DR PaxDb; Q8R2Y2; -.
DR PeptideAtlas; Q8R2Y2; -.
DR PRIDE; Q8R2Y2; -.
DR ProteomicsDB; 287521; -. [Q8R2Y2-1]
DR ProteomicsDB; 287522; -. [Q8R2Y2-2]
DR Antibodypedia; 2244; 1987 antibodies from 47 providers.
DR DNASU; 84004; -.
DR Ensembl; ENSMUST00000034650; ENSMUSP00000034650; ENSMUSG00000032135. [Q8R2Y2-1]
DR Ensembl; ENSMUST00000098852; ENSMUSP00000096451; ENSMUSG00000032135. [Q8R2Y2-2]
DR GeneID; 84004; -.
DR KEGG; mmu:84004; -.
DR UCSC; uc009pbw.2; mouse. [Q8R2Y2-1]
DR UCSC; uc009pbx.2; mouse. [Q8R2Y2-2]
DR CTD; 4162; -.
DR MGI; MGI:1933966; Mcam.
DR VEuPathDB; HostDB:ENSMUSG00000032135; -.
DR eggNOG; ENOG502QV1U; Eukaryota.
DR GeneTree; ENSGT00940000155838; -.
DR HOGENOM; CLU_028888_3_0_1; -.
DR InParanoid; Q8R2Y2; -.
DR OMA; RCMASVP; -.
DR OrthoDB; 864786at2759; -.
DR PhylomeDB; Q8R2Y2; -.
DR TreeFam; TF330534; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 84004; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Mcam; mouse.
DR PRO; PR:Q8R2Y2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R2Y2; protein.
DR Bgee; ENSMUSG00000032135; Expressed in aorta tunica media and 187 other tissues.
DR ExpressionAtlas; Q8R2Y2; baseline and differential.
DR Genevisible; Q8R2Y2; MM.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0061042; P:vascular wound healing; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..648
FT /note="Cell surface glycoprotein MUC18"
FT /id="PRO_0000045460"
FT TOPO_DOM 24..563
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..131
FT /note="Ig-like V-type 1"
FT DOMAIN 141..244
FT /note="Ig-like V-type 2"
FT DOMAIN 246..332
FT /note="Ig-like C2-type 1"
FT DOMAIN 337..426
FT /note="Ig-like C2-type 2"
FT DOMAIN 432..512
FT /note="Ig-like C2-type 3"
FT REGION 281..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43121"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 50..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 163..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 274..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 367..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 454..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 600..648
FT /note="ITLPPTRKSEFVVEVKSDKLPEEMALLQGSNGDKRAPGDQGEKYIDLRH ->
FT MERNTSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11329371, ECO:0000303|Ref.1"
FT /id="VSP_016940"
FT CONFLICT 584
FT /note="F -> L (in Ref. 1; BAB16050/BAB16051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 71545 MW; E468DABDB56C28FD CRC64;
MGLPKLVCVF LFAACCCCRR AAGVPGEEKQ PVPTPDLVEA EVGSTALLKC GPSRASGNFS
QVDWFLIHKE RQILIFRVHQ GKGQREPGEY EHRLSLQDSV ATLALSHVTP HDERMFLCKS
KRPRLQDHYV ELQVFKAPEE PTIQANVVGI HVDRQELREV ATCVGRNGYP IPQVLWYKNS
LPLQEEENRV HIQSSQIVES SGLYTLKSVL SARLVKEDKD AQFYCELSYR LPSGNHMKES
KEVTVPVFYP AEKVWVEVEP VGLLKEGDHV TIRCLTDGNP QPHFTINKKD PSTGEMEEES
TDENGLLSLE PAEKHHSGLY QCQSLDLETT ITLSSDPLEL LVNYVSDVQV NPTAPEVQEG
ESLTLTCEAE SNQDLEFEWL RDKTGQLLGK GPVLQLNNVR REAGGRYLCM ASVPRVPGLN
RTQLVSVGIF GSPWMALKER KVWVQENAVL NLSCEASGHP QPTISWNVNG SATEWNPDPQ
TVVSTLNVLV TPELLETGAE CTASNSLGSN TTTIVLKLVT LTTLIPDSSQ TTGLSTLTVS
PHTRANSTST EKKLPQPESK GVVIVAVIVC TLVLAVLGAA LYFFYKKGKL PCGRSGKQEI
TLPPTRKSEF VVEVKSDKLP EEMALLQGSN GDKRAPGDQG EKYIDLRH
