PECAM1

Platelet endothelial cell adhesion molecule

740 amino acids

Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-692 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. Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions. Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils. Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal. Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes. Modulates bradykinin receptor BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells. Induces susceptibility to atherosclerosis.

82.379 kDa

MRLRWTQGGNMWLGVLLTLQLCSSLEGQENSFTINSIHMEMLPGQEVHNGENLTLQCIVDVSTTSSVKPQHQVLFYKDDVLFHNVSSTKNTESYFISEARVYNSGRYKCTVILNNKEKTTAEYKVVVEGVSNPRVTLDKKEVIEGGVVKVTCSVPEEKPPVHFIIEKFELNVRDVKQRREKTANNQNSVTLEFTVEEQDRVILFSCQANVIFGTRVEISDSVRSDLVTVRESFSNPKFHISPKGVIIEGDQLLIKCTIQVTHQAQSFPEIIIQKDKEIVAHSRNGSEAVYSVMATVEHNSNYTCKVEASRISKVSSIMVNITELFSRPKLKSSATRLDQGESLRLWCSIPGAPPEANFTIQKGGMMMLQDQNLTKVASERDSGTYTCVAGIGKVVKRSNEVQIAVCEMLSKPSIFHDSGSEVIKGQTIEVSCQSINGTSPISYQLLKGSDLLASQNVSSNEPAVFKDNPTKDVEYQCIADNCHSHAGMPSKVLRVKVIAPVEEVKLSILLSEEVESGQAIVLQCSVKEGSGPITYKFYKEKENKPFHQVTLNDTQAIWHKPKASKDQEGQYYCLASNRATPSKNFLQSNILAVRVYLAPWKKGLIAVVVIAVIIAVLLLGARFYFLKKSKAKQMPVEMCRPAAPLLNSNNEKTLSDPNTEANRHYGYNEDVGNHAMKPLNENKEPLTLDVEYTEVEVTSPEPHRGLGTKGTETVYSEIRKADPDLVENRYSRTEGSLDGT

PECAM1

Platelet endothelial cell adhesion molecule

739 amino acids

Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-689 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. Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions. Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils. Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal. Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes. Modulates bradykinin receptor BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells. Induces susceptibility to atherosclerosis.

82.586 kDa

MQLRWTQRGMMWLGALLTLLLCSSLKGQENSFTINSIHMQILPHSTVQNGENLTLQCLVDVSTTSRVKPLHQVLFYKDDVLLHNVSSRRNTESYLIPHVRVCDSGRYKCNVILNNKEKTTPEYEVWVKGVSDPRVTLDKKEVIEGGVVVVNCSVPEEKAPVHFTIEKFELNIRGAKKKREKTSQNQNFVTLEFTVEEQDRTIRFQCQAKIFSGSNVESSRPIQSDLVTVRESFSNPKFHIIPEGKVMEGDDLQVKCTVQVTHQAQSFPEIIIQKDREIVAHNSLSSEAVYSVMATTEHNGNYTCKVEASRISKVSSVVVNVTELFSKPKLESSATHLDQGEDLNLLCSIPGAPPANFTIQKGGMTVSQTQNFTKRVSEWDSGLYTCVAGVGRVFKRSNTVQITVCEMLSKPSIFHDSRSEVIKGQTIEVSCQSVNGTAPIFYQLSNTSKPVANQSVGSNKPAIFRVKPTKDVEYCCSADNCHSHSKMFSEVLRVKVIAPVDEAQLVVLKGEVEPGEPIVFYCSVNEGSFPITYKFYKEKESKPFYQDTINATQIMWHKTTASKEYEGQYYCTASNRANLSKHVIQSNTLTVRVYLPLEKGLIAVVVIGVIIVTLVLGAKCYFLKKAKAKQMPVEMSRPAVPLLNSNNEKTLSDAGTEADRHYGYNEDVGNHAMKPLNENKEPLTLDVEYTEVEVTSPEPHQGLGTKGTETETVYSEIRKADPDFVENRYSRTEGSLDGS

PECAM1

Platelet endothelial cell adhesion molecule

738 amino acids

Isoform Delta15: Does not protect against apoptosis.

82.522 kDa

MQPRWAQGATMWLGVLLTLLLCSSLEGQENSFTINSVDMKSLPDWTVQNGKNLTLQCFADVSTTSHVKPQHQMLFYKDDVLFYNISSMKSTESYFIPEVRIYDSGTYKCTVIVNNKEKTTAEYQVLVEGVPSPRVTLDKKEAIQGGIVRVNCSVPEEKAPIHFTIEKLELNEKMVKLKREKNSRDQNFVILEFPVEEQDRVLSFRCQARIISGIHMQTSESTKSELVTVTESFSTPKFHISPTGMIMEGAQLHIKCTIQVTHLAQEFPEIIIQKDKAIVAHNRHGNKAVYSVMAMVEHSGNYTCKVESSRISKVSSIVVNITELFSKPELESSFTHLDQGERLNLSCSIPGAPPANFTIQKEDTIVSQTQDFTKIASKSDSGTYICTAGIDKVVKKSNTVQIVVCEMLSQPRISYDAQFEVIKGQTIEVRCESISGTLPISYQLLKTSKVLENSTKNSNDPAVFKDNPTEDVEYQCVADNCHSHAKMLSEVLRVKVIAPVDEVQISILSSKVVESGEDIVLQCAVNEGSGPITYKFYREKEGKPFYQMTSNATQAFWTKQKASKEQEGEYYCTAFNRANHASSVPRSKILTVRVILAPWKKGLIAVVIIGVIIALLIIAAKCYFLRKAKAKQMPVEMSRPAVPLLNSNNEKMSDPNMEANSHYGHNDDVRNHAMKPINDNKEPLNSDVQYTEVQVSSAESHKDLGKKDTETVYSEVRKAVPDAVESRYSRTEGSLDGT

Pecam1

Platelet endothelial cell adhesion molecule

727 amino acids

Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (By similarity). Tyr-679 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 (By similarity). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (By similarity). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (By similarity). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (By similarity). Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes (By similarity). Modulates bradykinin receptor BDKRB2 activation (By similarity). Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (By similarity). Induces susceptibility to atherosclerosis (PubMed:19048083).

81.263 kDa

MLLALGLTLVLYASLQAEENSFTINSIHMESLPSWEVMNGQQLTLECLVDISTTSKSRSQHRVLFYKDDAMVYNVTSREHTESYVIPQARVFHSGKYKCTVMLNNKEKTTIEYEVKVHGVSKPKVTLDKKEVTEGGVVTVNCSLQEEKPPIFFKIEKLEVGTKFVKRRIDKTSNENFVLMEFPIEAQDHVLVFRCQAGILSGFKLQESEPIRSEYVTVQESFSTPKFEIKPPGMIIEGDQLHIRCIVQVTHLVQEFTEIIIQKDKAIVATSKQSSEAVYSVMAMVEYSGHYTCKVESNRISKASSIMVNITELFPKPKLEFSSSRLDQGELLDLSCSVSGTPVANFTIQKEETVLSQYQNFSKIAEESDSGEYSCTAGIGKVVKRSGLVPIQVCEMLSKPSIFHDAKSEIIKGHAIGISCQSENGTAPITYHLMKAKSDFQTLEVTSNDPATFTDKPTRDMEYQCRADNCHSHPAVFSEILRVRVIAPVDEVVISILSSNEVQSGSEMVLRCSVKEGTSPITFQFYKEKEDRPFHQAVVNDTQAFWHNKQASKKQEGQYYCTASNRASSMRTSPRSSTLAVRVFLAPWKKGLIAVVVIGVVIATLIVAAKCYFLRKAKAKQKPVEMSRPAAPLLNSNSEKISEPSVEANSHYGYDDVSGNDAVKPINQNKDPQNMDVEYTEVEVSSLEPHQALGTRATETVYSEIRKVDPNLMENRYSRTEGSLNGT

Pecam1

Platelet endothelial cell adhesion molecule

678 amino acids

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. Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions. Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils. Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal. Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes. Modulates bradykinin receptor BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells. Induces susceptibility to atherosclerosis.

76.189 kDa

MLLALLLTMLLYASLQAQENSFTINSIHMESRPSWEVSNGQKLTLQCLVDISTTSKSRPQHQVLFYKDDALVYNVSSSEHTESFVIPQSRVFHAGKYKCTVILNSKEKTTIEYQLTVNGVPMPEVTVDKKEVTEGGIVTVNCSMQEEKPPIYFKIEKVELGTKNVKLSREKTSNMNFVLIEFPIEEQDHLLVFRCQAGVLSGIKMQTSEFIRSEYVTVQEFFSTPKFQIQPPEMIIEGNQLHIKCSVQVAHLAQEFPEIIIQKDKAIVATSKQSKEAVYSVMALVEHSGHYTCKVESNRISKASSILVNITELFPRPKLELSSSRLDQGEMLDLSCSVSGAPVANFTIQKEETVLSQYQNFSKIAEERDSGLYSCTAGIGKVVKRSNLVPVQVCEMLSKPRIFHDAKFEIIKGQIIGISCQSVNGTAPITYRLLRAKSNFQTVQKNSNDPVTFTDKPTRDMEYQCIVDNCHSHPEVRSEILRVKVIAPVDEVTISILSGNDVQSGDEMVLRCSVKEGTGPVTFQFYKEKEGRPFHEETVNDTQVFWHHEQTSKEQEGQYYCTAFNRASIVTSLRSGPLTVRVFLAPWKKGLIAVVVIGVVIAALIVAAKYYFLRKAKAKQKPVEMSRPAVPLLNSNSEKVSEPSVETNSHYDSQNMDVEYTEVEVSSLEPHQENGRLP