PECA1_HUMAN » Platelet endothelial cell adhesion molecule

PECA1_HUMAN » Platelet endothelial cell adhesion molecule
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
PECA1_HUMAN » Platelet endothelial cell adhesion molecule » PECAM-1;EndoCAM;GPIIA';
Hydrophobic Thickness 38.0 ± 5.0 Å
Tilt Angle 9 ± 12°
ΔGtransfer -28.1 kcal/mol
ΔGfold -23.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 599-625 (597-630)
Pathways

Cell adhesion molecules (KEGG)

Hemostasis (Reactome)

Leukocyte transendothelial migration (KEGG)

Malaria (KEGG)

Signal Transduction (Reactome)

PDB 2ky5 (686-738)
OPM 2ky5
Complexes none
Interactions

CD38, Complex: CD38:PECA1, PubMed

EFNB2, Complex: EFNB2:PECA1, PubMed

ITA5, Complex: PECA1:ITA5, PubMed

ITB3, Complex: PECA1:ITB3, PubMed

SDC1, Complex: PECA1:SDC1, PubMed

SDC4, Complex: PECA1:SDC4, PubMed

Domains

AA: 327-404, PDBID: 1FCG, Subunit A, Seq Identity:24%, Immunoglobulin domain

UniProt annotation for PECA1_HUMAN » Platelet endothelial cell adhesion molecule
FUNCTION: 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).

SUBUNIT: Interacts with PTPN11; Tyr-713 is critical for PTPN11 recruitment. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ.

TISSUE SPECIFICITY: Expressed on platelets and leukocytes and is primarily concentrated at the borders between endothelial cells. Isoform Long predominates in all tissues examined. Isoform Delta12 is detected only in trachea. Isoform Delta14-15 is only detected in lung. Isoform Delta14 is detected in all tissues examined with the strongest expression in heart. Isoform Delta15 is expressed in brain, testis, ovary, cell surface of platelets, human umbilical vein endothelial cells (HUVECs), Jurkat T-cell leukemia, human erythroleukemia (HEL) and U-937 histiocytic lymphoma cell lines (at protein level).

DOMAIN: The Ig-like C2-type domains 2 and 3 contribute to formation of the complex with BDKRB2 and in regulation of its activity.

UniProt features for PECA1_HUMAN » Platelet endothelial cell adhesion molecule
SIGNAL 1 27
CHAIN 28 738 Platelet endothelial cell adhesion molecule.
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 cytoprotective signaling.
DISULFID 57 109 Potential.
DISULFID 152 206 Potential.
DISULFID 256 304 Potential.
DISULFID 347 386 Potential.
DISULFID 431 476 Potential.
DISULFID 523 572 Potential.
Amino Acid Sequence for PECA1_HUMAN » Platelet endothelial cell adhesion molecule
MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES HKDLGKKDTE TVYSEVRKAV PDAVESRYSR TEGSLDGT