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platelet endothelial aggregation receptor 1 (hPEAR1, multiple epidermal growth factor-like domains 12, multiple EGF-like-domains 12, MEGF12, PEAR1)
Function:
- when overexpressed, diminishes the number of both early & late non-adherent myeloid progenitor cells (putative)
- interacts with SHC2 upon its aggregation-induced tyrosine phosphorylation
- phosphorylated in the intracellular domain on tyrosine residues (putative)
- phosphorylated on tyrosine residues by SRC
- tyrosine phosphorylation is detected upon platelet aggregation stimulated by collagen, TRAP & thrombin & platelet-platelet contacts but not after platelet activation
- tyrosine phosphorylation enhances its association with SHC1 & SHC2
Structure:
- belongs to the MEGF family
- contains 9 EGF-like domains
- contains 1 EMI domain
Compartment:
- membrane (putative)
- detected on the cell surface in resting platelets
Expression:
- expressed in umbilical vein endothelial cells & platelets (at protein level)
- expressed in heart, kidney, skeletal muscle, pancreas, ovary, breast, lung, brain cortex, hypothalamus, spinal cord, dorsal root ganglion, endothelial cells of umbilical cord artery & vein, megakaryocytes, osteoblasts, heart muscle & erythroid cells
- weakly expressed in peripheral blood leukocytes & macrophages
General
glycoprotein
membrane protein
Properties
SIZE: entity length = 1037 aa
MW = 111 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-20}
EMI {25-103}
MOTIF: cysteine residue {C29}
MODIFICATION: cysteine residue {C91}
cysteine residue {C55}
MODIFICATION: cysteine residue {C65}
cysteine residue {C65}
MODIFICATION: cysteine residue {C55}
cysteine residue {C90}
MODIFICATION: cysteine residue {C101}
cysteine residue {C91}
MODIFICATION: cysteine residue {C29}
cysteine residue {C101}
MODIFICATION: cysteine residue {C90}
EGF domain {102-132}
MOTIF: cysteine residue {C105}
MODIFICATION: cysteine residue {C114}
cysteine residue {C109}
MODIFICATION: cysteine residue {C120}
cysteine residue {C114}
MODIFICATION: cysteine residue {C105}
cysteine residue {C120}
MODIFICATION: cysteine residue {C109}
cysteine residue {C122}
MODIFICATION: cysteine residue {C131}
cysteine residue {C131}
MODIFICATION: cysteine residue {C122}
N-glycosylation site {N152}
EGF domain {225-260}
MOTIF: cysteine residue {C235}
MODIFICATION: cysteine residue {C248}
cysteine residue {C248}
MODIFICATION: cysteine residue {C235}
cysteine residue {C250}
MODIFICATION: cysteine residue {C259}
cysteine residue {C259}
MODIFICATION: cysteine residue {C250}
EGF domain {268-303}
MOTIF: N-glycosylation site {N271}
cysteine residue {C272}
MODIFICATION: cysteine residue {C284}
cysteine residue {C278}
MODIFICATION: cysteine residue {C291}
cysteine residue {C284}
MODIFICATION: cysteine residue {C272}
cysteine residue {C291}
MODIFICATION: cysteine residue {C278}
cysteine residue {C293}
MODIFICATION: cysteine residue {C302}
cysteine residue {C302}
MODIFICATION: cysteine residue {C293}
EGF domain {311-346}
MOTIF: cysteine residue {C315}
MODIFICATION: cysteine residue {C327}
cysteine residue {C321}
MODIFICATION: cysteine residue {C334}
cysteine residue {C327}
MODIFICATION: cysteine residue {C315}
cysteine residue {C334}
MODIFICATION: cysteine residue {C321}
cysteine residue {C336}
MODIFICATION: cysteine residue {C345}
cysteine residue {C345}
MODIFICATION: cysteine residue {C336}
EGF domain {400-435}
MOTIF: cysteine residue {C404}
MODIFICATION: cysteine residue {C416}
cysteine residue {C410}
MODIFICATION: cysteine residue {C423}
cysteine residue {C416}
MODIFICATION: cysteine residue {C404}
cysteine residue {C423}
MODIFICATION: cysteine residue {C410}
cysteine residue {C425}
MODIFICATION: cysteine residue {C434}
cysteine residue {C434}
MODIFICATION: cysteine residue {C425}
N-glycosylation site {N476}
EGF domain {486-521}
MOTIF: cysteine residue {C490}
MODIFICATION: cysteine residue {C502}
cysteine residue {C496}
MODIFICATION: cysteine residue {C509}
cysteine residue {C502}
MODIFICATION: cysteine residue {C490}
cysteine residue {C509}
MODIFICATION: cysteine residue {C496}
cysteine residue {C511}
MODIFICATION: cysteine residue {C520}
cysteine residue {C520}
MODIFICATION: cysteine residue {C511}
N-glycosylation site {N575}
EGF domain {577-607}
MOTIF: cysteine residue {C580}
MODIFICATION: cysteine residue {C588}
cysteine residue {C582}
MODIFICATION: cysteine residue {C595}
cysteine residue {C588}
MODIFICATION: cysteine residue {C580}
cysteine residue {C595}
MODIFICATION: cysteine residue {C582}
cysteine residue {C597}
MODIFICATION: cysteine residue {C606}
cysteine residue {C606}
MODIFICATION: cysteine residue {C597}
EGF domain {615-649}
MOTIF: cysteine residue {C619}
MODIFICATION: cysteine residue {C630}
cysteine residue {C624}
MODIFICATION: cysteine residue {C637}
cysteine residue {C630}
MODIFICATION: cysteine residue {C619}
N-glycosylation site {N634}
cysteine residue {C637}
MODIFICATION: cysteine residue {C624}
cysteine residue {C639}
MODIFICATION: cysteine residue {C648}
cysteine residue {C648}
MODIFICATION: cysteine residue {C639}
EGF domain {657-692}
MOTIF: cysteine residue {C661}
MODIFICATION: cysteine residue {C673}
cysteine residue {C667}
MODIFICATION: cysteine residue {C680}
cysteine residue {C673}
MODIFICATION: cysteine residue {C661}
cysteine residue {C680}
MODIFICATION: cysteine residue {C667}
cysteine residue {C682}
MODIFICATION: cysteine residue {C691}
cysteine residue {C691}
MODIFICATION: cysteine residue {C682}
transmembrane domain {756-776}
proline-rich region
SITE: 807-1031
MOTIF: proline residue (SEVERAL)
Tyr phosphorylation site {Y925}
Ser phosphorylation site {S953}
Ser phosphorylation site {S1029}
Database Correlations
UniProt Q5VY43
PFAM correlations
References
UniProt :accession Q5VY43