Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00584
Entry Name
UniProt Accession
Theoretical PI
6.55
Molecular Weight
82536.21
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Platelet endothelial cell adhesion molecule
Protein Synonyms/Alias
PECAM-1; EndoCAM; GPIIA'; PECA1; CD31;
Gene Name
PECAM1
Gene Synonyms/Alias
Created Date
01-APR-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
622
Canonical
LLIIAAKCYFLRKAK
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Sardjono CT, Harbour SN, Yip JC, Paddock C, Tridandapani S, Newman PJ, JacksonDE. Palmitoylation at Cys595 is essential for PECAM-1 localisation into membrane microdomains and for efficient PECAM-1-mediated cytoprotection. Thromb Haemost.2006 Dec;96(6):756-66.[PMID:17139370]
Functional Description
Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).
Sequence Annotation
Topological domain: 28 601 Extracellular.
Transmembrane: 602 620 Helical.
Topological domain: 621 738 Cytoplasmic.
Domain: 35 121 Ig-like C2-type 1.
Domain: 145 233 Ig-like C2-type 2.
Domain: 236 315 Ig-like C2-type 3.
Domain: 328 401 Ig-like C2-type 4.
Domain: 424 493 Ig-like C2-type 5.
Domain: 499 591 Ig-like C2-type 6.
Region: 721 738 May play a role in cytoprotectivesignaling.
Modified residue: 690 690 Phosphotyrosine; by FER.
Modified residue: 713 713 Phosphotyrosine; by FER.
Protein Length
738 AA.
Protein Sequence
(Canonical)
MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD  60
VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT  120
AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE  180
KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI  240
SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG  300
NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ  360
KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE  420
VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN  480
CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK  540
EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK  600
KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN  660
SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES HKDLGKKDTE TVYSEVRKAV  720
PDAVESRYSR TEGSLDGT                                                738
FASTA
(Canonical)
>LipidDB-9606-00584|P16284
MQPRWAQGATMWLGVLLTLLLCSSLEGQENSFTINSVDMKSLPDWTVQNGKNLTLQCFAD
VSTTSHVKPQHQMLFYKDDVLFYNISSMKSTESYFIPEVRIYDSGTYKCTVIVNNKEKTT
AEYQLLVEGVPSPRVTLDKKEAIQGGIVRVNCSVPEEKAPIHFTIEKLELNEKMVKLKRE
KNSRDQNFVILEFPVEEQDRVLSFRCQARIISGIHMQTSESTKSELVTVTESFSTPKFHI
SPTGMIMEGAQLHIKCTIQVTHLAQEFPEIIIQKDKAIVAHNRHGNKAVYSVMAMVEHSG
NYTCKVESSRISKVSSIVVNITELFSKPELESSFTHLDQGERLNLSCSIPGAPPANFTIQ
KEDTIVSQTQDFTKIASKSDSGTYICTAGIDKVVKKSNTVQIVVCEMLSQPRISYDAQFE
VIKGQTIEVRCESISGTLPISYQLLKTSKVLENSTKNSNDPAVFKDNPTEDVEYQCVADN
CHSHAKMLSEVLRVKVIAPVDEVQISILSSKVVESGEDIVLQCAVNEGSGPITYKFYREK
EGKPFYQMTSNATQAFWTKQKASKEQEGEYYCTAFNRANHASSVPRSKILTVRVILAPWK
KGLIAVVIIGVIIALLIIAAKCYFLRKAKAKQMPVEMSRPAVPLLNSNNEKMSDPNMEAN
SHYGHNDDVRNHAMKPINDNKEPLNSDVQYTEVQVSSAESHKDLGKKDTETVYSEVRKAV
PDAVESRYSRTEGSLDGT
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0005615; C:extracellular space; IDA:BHF-UCL
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0031092; C:platelet alpha granule membrane; TAS:Reactome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0007155; P:cell adhesion; IEA:UniProtKB-KW
GO:0008037; P:cell recognition; TAS:ProtInc
GO:0050904; P:diapedesis; IDA:UniProtKB
GO:0030198; P:extracellular matrix organization; TAS:Reactome
GO:0072011; P:glomerular endothelium development; IEP:UniProtKB
GO:0050900; P:leukocyte migration; TAS:Reactome
GO:0006909; P:phagocytosis; IDA:UniProtKB
GO:0030168; P:platelet activation; TAS:Reactome
GO:0002576; P:platelet degranulation; TAS:Reactome
GO:0007165; P:signal transduction; TAS:ProtInc
Interpro
InterPro; IPR007110; Ig-like_dom
InterPro; IPR013783; Ig-like_fold
InterPro; IPR003599; Ig_sub
Pfam
SMART
SMART; SM00409; IG;
PROSITE
PROSITE; PS50835; IG_LIKE;
PRINTS