CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012966
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Platelet endothelial cell adhesion molecule 
Protein Synonyms/Alias
 PECAM-1; CD31 
Gene Name
 Pecam1 
Gene Synonyms/Alias
 Pecam 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
96SRVFHAGKYKCTVILacetylation[1]
157PIYFKIEKVELGTKNacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-660 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). Modulates BDKRB2 activation. Induces susceptibility to atherosclerosis (By similarity). 
Sequence Annotation
 DOMAIN 40 126 Ig-like C2-type 1.
 DOMAIN 135 213 Ig-like C2-type 2.
 DOMAIN 225 309 Ig-like C2-type 3.
 DOMAIN 315 391 Ig-like C2-type 4.
 DOMAIN 413 472 Ig-like C2-type 5.
 DOMAIN 488 577 Ig-like C2-type 6.
 MOD_RES 660 660 Phosphotyrosine; by FER (By similarity).
 CARBOHYD 74 74 N-linked (GlcNAc...) (Potential).
 CARBOHYD 141 141 N-linked (GlcNAc...) (Potential).
 CARBOHYD 309 309 N-linked (GlcNAc...) (Potential).
 CARBOHYD 345 345 N-linked (GlcNAc...) (Potential).
 CARBOHYD 360 360 N-linked (GlcNAc...) (Potential).
 CARBOHYD 424 424 N-linked (GlcNAc...) (Potential).
 CARBOHYD 540 540 N-linked (GlcNAc...) (Potential).
 DISULFID 47 99 Potential.
 DISULFID 142 195 Potential.
 DISULFID 245 293 Potential.
 DISULFID 336 375 Potential.
 DISULFID 420 465 Potential.
 DISULFID 512 561 Potential.  
Keyword
 Cell adhesion; Cell junction; Complete proteome; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 678 AA 
Protein Sequence
MLLALLLTML LYASLQAQEN SFTINSIHME SRPSWEVSNG QKLTLQCLVD ISTTSKSRPQ 60
HQVLFYKDDA LVYNVSSSEH TESFVIPQSR VFHAGKYKCT VILNSKEKTT IEYQLTVNGV 120
PMPEVTVDKK EVTEGGIVTV NCSMQEEKPP IYFKIEKVEL GTKNVKLSRE KTSNMNFVLI 180
EFPIEEQDHL LVFRCQAGVL SGIKMQTSEF IRSEYVTVQE FFSTPKFQIQ PPEMIIEGNQ 240
LHIKCSVQVA HLAQEFPEII IQKDKAIVAT SKQSKEAVYS VMALVEHSGH YTCKVESNRI 300
SKASSILVNI TELFPRPKLE LSSSRLDQGE MLDLSCSVSG APVANFTIQK EETVLSQYQN 360
FSKIAEERDS GLYSCTAGIG KVVKRSNLVP VQVCEMLSKP RIFHDAKFEI IKGQIIGISC 420
QSVNGTAPIT YRLLRAKSNF QTVQKNSNDP VTFTDKPTRD MEYQCIVDNC HSHPEVRSEI 480
LRVKVIAPVD EVTISILSGN DVQSGDEMVL RCSVKEGTGP VTFQFYKEKE GRPFHEETVN 540
DTQVFWHHEQ TSKEQEGQYY CTAFNRASIV TSLRSGPLTV RVFLAPWKKG LIAVVVIGVV 600
IAALIVAAKY YFLRKAKAKQ KPVEMSRPAV PLLNSNSEKV SEPSVETNSH YDSQNMDVEY 660
TEVEVSSLEP HQENGRLP 678 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
 GO:0009986; C:cell surface; IDA:RGD.
 GO:0009897; C:external side of plasma membrane; IEA:Compara.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0045121; C:membrane raft; IEA:Compara.
 GO:0030485; C:smooth muscle contractile fiber; IEA:Compara.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0006928; P:cellular component movement; IDA:RGD.
 GO:0030837; P:negative regulation of actin filament polymerization; IDA:RGD.
 GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
 GO:0034259; P:negative regulation of Rho GTPase activity; IDA:RGD.
 GO:0002687; P:positive regulation of leukocyte migration; IMP:RGD.
 GO:0042523; P:positive regulation of tyrosine phosphorylation of Stat5 protein; IEA:Compara.
 GO:0034097; P:response to cytokine stimulus; IEP:RGD.
 GO:0007266; P:Rho protein signal transduction; IEA:Compara.
 GO:0042060; P:wound healing; IEA:Compara. 
Interpro
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR003599; Ig_sub. 
Pfam
  
SMART
 SM00409; IG 
PROSITE
 PS50835; IG_LIKE 
PRINTS