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Cell surface glycoprotein MUC18 (Gicerin) (Melanoma cell adhesion molecule) (Melanoma-associated antigen MUC18) (CD antigen CD146)

 MUC18_RAT               Reviewed;         648 AA.
Q9EPF2; Q6IRH8; Q9ESS8;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 2.
22-NOV-2017, entry version 120.
RecName: Full=Cell surface glycoprotein MUC18;
AltName: Full=Gicerin;
AltName: Full=Melanoma cell adhesion molecule;
AltName: Full=Melanoma-associated antigen MUC18;
AltName: CD_antigen=CD146;
Flags: Precursor;
Name=Mcam; Synonyms=Muc18;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Heart;
PubMed=14755543; DOI=10.1002/jcp.10413;
Taira E., Kohama K., Tsukamoto Y., Okumura S., Miki N.;
"Characterization of Gicerin/MUC18/CD146 in the rat nervous system.";
J. Cell. Physiol. 198:377-387(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Plays a role in cell adhesion, and in cohesion of the
endothelial monolayer at intercellular junctions in vascular
tissue. Its expression may allow melanoma cells to interact with
cellular elements of the vascular system, thereby enhancing
hematogeneous tumor spread. Could be an adhesion molecule active
in neural crest cells during embryonic development. Acts as
surface receptor that triggers tyrosine phosphorylation of FYN and
PTK2/FAK1, and a transient increase in the intracellular calcium
concentration (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14755543};
Single-pass type I membrane protein {ECO:0000269|PubMed:14755543}.
Perikaryon {ECO:0000269|PubMed:14755543}. Note=Detected at the
surface of the cell body of motor neurons.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=L-gicerin;
IsoId=Q9EPF2-1; Sequence=Displayed;
Name=2; Synonyms=S-gicerin;
IsoId=Q9EPF2-2; Sequence=VSP_016941;
-!- TISSUE SPECIFICITY: Detected in lung, uterus and placenta (at
protein level). Detected in heart, lung, kidney, adrenal gland,
intestine, testis, skeletal muscle and aorta. Detected at low
levels in adult brain, in particular in brain stem and spinal
cord, but also in hippocampus, olfactory bulb and striatum (at
protein level). {ECO:0000269|PubMed:14755543}.
-!- DEVELOPMENTAL STAGE: Detected at high levels in brain throughout
embryonic development (at protein level). Levels are lower in
neonates and decrease during the first days after birth (at
protein level).
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EMBL; AB035506; BAB16048.1; -; mRNA.
EMBL; AB035507; BAB16049.1; -; mRNA.
EMBL; BC070916; AAH70916.1; -; mRNA.
RefSeq; NP_001029181.1; NM_001034009.1. [Q9EPF2-2]
RefSeq; NP_076473.2; NM_023983.3. [Q9EPF2-1]
UniGene; Rn.2694; -.
ProteinModelPortal; Q9EPF2; -.
BioGrid; 249375; 1.
STRING; 10116.ENSRNOP00000010464; -.
PhosphoSitePlus; Q9EPF2; -.
SwissPalm; Q9EPF2; -.
PaxDb; Q9EPF2; -.
PRIDE; Q9EPF2; -.
Ensembl; ENSRNOT00000010463; ENSRNOP00000010464; ENSRNOG00000007726. [Q9EPF2-1]
Ensembl; ENSRNOT00000090780; ENSRNOP00000069860; ENSRNOG00000007726. [Q9EPF2-2]
GeneID; 78967; -.
KEGG; rno:78967; -.
UCSC; RGD:620463; rat. [Q9EPF2-1]
CTD; 4162; -.
RGD; 620463; Mcam.
eggNOG; ENOG410IEC2; Eukaryota.
eggNOG; ENOG4110RPG; LUCA.
GeneTree; ENSGT00530000063457; -.
HOGENOM; HOG000015427; -.
HOVERGEN; HBG002808; -.
InParanoid; Q9EPF2; -.
KO; K06534; -.
OMA; GDQGEKY; -.
OrthoDB; EOG091G072E; -.
PhylomeDB; Q9EPF2; -.
PRO; PR:Q9EPF2; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000007726; -.
Genevisible; Q9EPF2; RN.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0001525; P:angiogenesis; ISO:RGD.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0003094; P:glomerular filtration; ISO:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
GO; GO:0061042; P:vascular wound healing; ISO:RGD.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 5.
SUPFAM; SSF48726; SSF48726; 5.
PROSITE; PS50835; IG_LIKE; 4.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000250}.
CHAIN 24 648 Cell surface glycoprotein MUC18.
/FTId=PRO_0000045461.
TOPO_DOM 24 560 Extracellular. {ECO:0000255}.
TRANSMEM 561 581 Helical. {ECO:0000255}.
TOPO_DOM 582 648 Cytoplasmic. {ECO:0000255}.
DOMAIN 24 131 Ig-like V-type 1.
DOMAIN 141 244 Ig-like V-type 2.
DOMAIN 246 332 Ig-like C2-type 1.
DOMAIN 337 426 Ig-like C2-type 2.
DOMAIN 432 512 Ig-like C2-type 3.
MOD_RES 608 608 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R2Y2}.
MOD_RES 616 616 Phosphoserine.
{ECO:0000250|UniProtKB:P43121}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 510 510 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 118 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 163 225 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 274 322 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 367 409 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 454 501 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 600 648 ITLPPTRKSEFVVEVKSDKLPEEMALLQGSNGDKRAPGDQG
EKYIDLRH -> MERNTSI (in isoform 2).
{ECO:0000303|PubMed:14755543,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_016941.
CONFLICT 214 214 L -> V (in Ref. 1; BAB16048/BAB16049).
{ECO:0000305}.
CONFLICT 227 227 L -> V (in Ref. 1; BAB16048/BAB16049).
{ECO:0000305}.
CONFLICT 231 231 L -> P (in Ref. 1; BAB16048/BAB16049).
{ECO:0000305}.
CONFLICT 510 510 N -> Y (in Ref. 1; BAB16048/BAB16049).
{ECO:0000305}.
CONFLICT 526 526 P -> H (in Ref. 1; BAB16048/BAB16049).
{ECO:0000305}.
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


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