| Tag |
Content |
LipidDB ID |
LipidDB-9606-01193 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
5.58 |
Molecular Weight |
71607.41 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Cell surface glycoprotein MUC18 |
Protein Synonyms/Alias |
Cell surface glycoprotein P1H12; Melanoma cell adhesion molecule; Melanoma-associated antigen A32; Melanoma-associated antigen MUC18; S-endo 1 endothelial-associated antigen; CD146; |
Gene Name |
MCAM |
Gene Synonyms/Alias |
MUC18; |
Created Date |
01-NOV-1995 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
8 | Canonical | MGLPRLVCAFLLAAC | [1] | S-Palmitoylation | 15 | Canonical | CAFLLAACCCCPRVA | [1] | S-Palmitoylation | 16 | Canonical | AFLLAACCCCPRVAG | [1] | S-Palmitoylation | 17 | Canonical | FLLAACCCCPRVAGV | [1] | S-Palmitoylation | 18 | Canonical | LLAACCCCPRVAGVP | [1] | S-Palmitoylation | 590 | Canonical | YKKGKLPCRRSGKQE | [1] | S-Palmitoylation |
|
Organism |
Homo sapiens (Human) |
NCBI Taxa ID |
9606 |
Reference |
[1] Predicted from GPS-Lipid
|
Functional Description |
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. |
Sequence Annotation |
Topological domain: 24 559 Extracellular.
Transmembrane: 560 583 Helical.
Topological domain: 584 646 Cytoplasmic.
Domain: 24 129 Ig-like V-type 1.
Domain: 139 242 Ig-like V-type 2.
Domain: 244 330 Ig-like C2-type 1.
Domain: 335 424 Ig-like C2-type 2.
Domain: 430 510 Ig-like C2-type 3.
Modified residue: 614 614 Phosphoserine.
Modified residue: 628 628 Phosphoserine.
|
Protein Length |
646 AA. |
Protein Sequence
(Canonical) |
MGLPRLVCAF LLAACCCCPR VAGVPGEAEQ PAPELVEVEV GSTALLKCGL SQSQGNLSHV 60
DWFSVHKEKR TLIFRVRQGQ GQSEPGEYEQ RLSLQDRGAT LALTQVTPQD ERIFLCQGKR 120
PRSQEYRIQL RVYKAPEEPN IQVNPLGIPV NSKEPEEVAT CVGRNGYPIP QVIWYKNGRP 180
LKEEKNRVHI QSSQTVESSG LYTLQSILKA QLVKEDKDAQ FYCELNYRLP SGNHMKESRE 240
VTVPVFYPTE KVWLEVEPVG MLKEGDRVEI RCLADGNPPP HFSISKQNPS TREAEEETTN 300
DNGVLVLEPA RKEHSGRYEC QGLDLDTMIS LLSEPQELLV NYVSDVRVSP AAPERQEGSS 360
LTLTCEAESS QDLEFQWLRE ETGQVLERGP VLQLHDLKRE AGGGYRCVAS VPSIPGLNRT 420
QLVNVAIFGP PWMAFKERKV WVKENMVLNL SCEASGHPRP TISWNVNGTA SEQDQDPQRV 480
LSTLNVLVTP ELLETGVECT ASNDLGKNTS ILFLELVNLT TLTPDSNTTT GLSTSTASPH 540
TRANSTSTER KLPEPESRGV VIVAVIVCIL VLAVLGAVLY FLYKKGKLPC RRSGKQEITL 600
PPSRKSELVV EVKSDKLPEE MGLLQGSSGD KRAPGDQGEK YIDLRH 646
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FASTA
(Canonical) |
>LipidDB-9606-01193|P43121
MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQSQGNLSHV
DWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDERIFLCQGKR
PRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIPQVIWYKNGRP
LKEEKNRVHIQSSQTVESSGLYTLQSILKAQLVKEDKDAQFYCELNYRLPSGNHMKESRE
VTVPVFYPTEKVWLEVEPVGMLKEGDRVEIRCLADGNPPPHFSISKQNPSTREAEEETTN
DNGVLVLEPARKEHSGRYECQGLDLDTMISLLSEPQELLVNYVSDVRVSPAAPERQEGSS
LTLTCEAESSQDLEFQWLREETGQVLERGPVLQLHDLKREAGGGYRCVASVPSIPGLNRT
QLVNVAIFGPPWMAFKERKVWVKENMVLNLSCEASGHPRPTISWNVNGTASEQDQDPQRV
LSTLNVLVTPELLETGVECTASNDLGKNTSILFLELVNLTTLTPDSNTTTGLSTSTASPH
TRANSTSTERKLPEPESRGVVIVAVIVCILVLAVLGAVLYFLYKKGKLPCRRSGKQEITL
PPSRKSELVVEVKSDKLPEEMGLLQGSSGDKRAPGDQGEKYIDLRH
|
Gene Ontology |
GO:0009897; C:external side of plasma membrane; IDA:UniProtKB GO:0005925; C:focal adhesion; IDA:UniProtKB GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0005886; C:plasma membrane; NAS:ProtInc GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc GO:0007155; P:cell adhesion; TAS:ProtInc GO:0003094; P:glomerular filtration; IEP:UniProtKB GO:0061042; P:vascular wound healing; IEP:UniProtKB |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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