MUC18_RAT
ID MUC18_RAT Reviewed; 648 AA.
AC Q9EPF2; Q6IRH8; Q9ESS8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=14755543; DOI=10.1002/jcp.10413;
RA Taira E., Kohama K., Tsukamoto Y., Okumura S., Miki N.;
RT "Characterization of Gicerin/MUC18/CD146 in the rat nervous system.";
RL J. Cell. Physiol. 198:377-387(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
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).
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: Cell membrane {ECO:0000269|PubMed:14755543};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:14755543}.
CC Perikaryon {ECO:0000269|PubMed:14755543}. Note=Detected at the surface
CC of the cell body of motor neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=L-gicerin;
CC IsoId=Q9EPF2-1; Sequence=Displayed;
CC Name=2; Synonyms=S-gicerin;
CC IsoId=Q9EPF2-2; Sequence=VSP_016941;
CC -!- TISSUE SPECIFICITY: Detected in lung, uterus and placenta (at protein
CC level). Detected in heart, lung, kidney, adrenal gland, intestine,
CC testis, skeletal muscle and aorta. Detected at low levels in adult
CC brain, in particular in brain stem and spinal cord, but also in
CC hippocampus, olfactory bulb and striatum (at protein level).
CC {ECO:0000269|PubMed:14755543}.
CC -!- DEVELOPMENTAL STAGE: Detected at high levels in brain throughout
CC embryonic development (at protein level). Levels are lower in neonates
CC and decrease during the first days after birth (at protein level).
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DR EMBL; AB035506; BAB16048.1; -; mRNA.
DR EMBL; AB035507; BAB16049.1; -; mRNA.
DR EMBL; BC070916; AAH70916.1; -; mRNA.
DR RefSeq; NP_001029181.1; NM_001034009.1. [Q9EPF2-2]
DR RefSeq; NP_076473.2; NM_023983.3. [Q9EPF2-1]
DR AlphaFoldDB; Q9EPF2; -.
DR SMR; Q9EPF2; -.
DR BioGRID; 249375; 1.
DR STRING; 10116.ENSRNOP00000010464; -.
DR GlyGen; Q9EPF2; 2 sites.
DR PhosphoSitePlus; Q9EPF2; -.
DR SwissPalm; Q9EPF2; -.
DR jPOST; Q9EPF2; -.
DR PaxDb; Q9EPF2; -.
DR PRIDE; Q9EPF2; -.
DR Ensembl; ENSRNOT00000010463; ENSRNOP00000010464; ENSRNOG00000007726. [Q9EPF2-1]
DR Ensembl; ENSRNOT00000090780; ENSRNOP00000069860; ENSRNOG00000007726. [Q9EPF2-2]
DR GeneID; 78967; -.
DR KEGG; rno:78967; -.
DR UCSC; RGD:620463; rat. [Q9EPF2-1]
DR CTD; 4162; -.
DR RGD; 620463; Mcam.
DR eggNOG; ENOG502QV1U; Eukaryota.
DR GeneTree; ENSGT00940000155838; -.
DR HOGENOM; CLU_028888_3_0_1; -.
DR InParanoid; Q9EPF2; -.
DR OMA; RCMASVP; -.
DR OrthoDB; 864786at2759; -.
DR PhylomeDB; Q9EPF2; -.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q9EPF2; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000007726; Expressed in lung and 20 other tissues.
DR Genevisible; Q9EPF2; RN.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0003094; P:glomerular filtration; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
DR GO; GO:0061042; P:vascular wound healing; ISO:RGD.
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; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; 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_0000045461"
FT TOPO_DOM 24..560
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..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 282..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R2Y2"
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:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:14755543,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016941"
FT CONFLICT 214
FT /note="L -> V (in Ref. 1; BAB16048/BAB16049)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="L -> V (in Ref. 1; BAB16048/BAB16049)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="L -> P (in Ref. 1; BAB16048/BAB16049)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="N -> Y (in Ref. 1; BAB16048/BAB16049)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="P -> H (in Ref. 1; BAB16048/BAB16049)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 71327 MW; 85B727C60D4BF4C3 CRC64;
MGLPRLVCAF LFAACCCCRS ATGVPGEEKQ PTPTPDPVEV EVGNTALLKC GPAHPSGNFS
QVEWFLIHKE RQIPIFRVHQ GKGQSEPGEY EHRLSLHGPG ATLALSQVTP HDDRMFLCKS
KQPRPQDHYV QLQVYKAPEE PTIQANVLGI HVDIQELKEV ATCVGRNGYP IPQVIWYKNG
RPLQEEENRV HIQSSQTVES SGLYTLKSVL SARLVKEDKD AQFYCELSYR LPSGNRMKES
KEVTVPVLYP AEKVWVEVEP VGLLKEGDHV KIRCLTDGNP QPHFTINKKN PSTEEMEEES
TDENGLLSLE PAQKHHSGVY QCQSLDLETT VMLSSDPLEL LVNYVSDVQV DPTAPEVQEG
DSLTLTCKAE SNQDLEFEWL RDKTGQLLGK GPILQLNNVK REAGGRYLCV ASVPSVPGLN
RTRRVSVGIF GSPWMAAKER KVWAQENAML NLSCEASGHP QPTISWNING SATEWNPDPQ
TVVSTLNVLV TPELLETGAE CTASNSLGSN TTVIILKLVT LTTLTPDSSQ TTGLSTPTVS
PHSRANSTST EKKLPQQESK GVVIVAVIVC TLVLAVLGAT LYYFYKKGKL PCGRSGKQEI
TLPPTRKSEF VVEVKSDKLP EEMALLQGSN GDKRAPGDQG EKYIDLRH
