secretory phospholipase A2 receptor (PLA2-R, PLA2R, 180 kD secretory phospholipase A2 receptor, M-type receptor) [Contains: soluble secretory phospholipase A2 receptor (Soluble PLA2-R, Soluble PLA2R)] (PLA2R1)

Function: - precise function uncertain - receptor for secretory phospholipase A2 (sPLA2) - acts as a receptor for phosholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A - able to bind to snake PA2-like toxins - binding of sPLA2 to its receptor participates in both positive & negative regulation of sPLA2 functions as well as clearance of sPLA2 - binding of sPLA2-IB/PLA2G1B induces various effects depending on cell type, including a) activation of MAPK cascade to induce cell proliferation b) production of lipid mediators c) selective release of arachidonic acid in bone marrow- derived mast cells - in neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release & cell adhesion - may be involved in responses in proinflammatory cytokine productions during endotoxic shock - also has endocytic properties & rapidly internalizes sPLA2 ligands, - the soluble secretory phospholipase A2 receptor form is circulating & acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B - the secretory phospholipase A2 receptor form may be produced by the action of metalloproteinases; it - contains all extracellular domains & only lacks transmembrane & cytosolic regions; unclear whether secretory form is produced by proteolytic cleavage or by alternative splicing Structure: - C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B - endocytosis signal probably mediates endocytosis via clathrin-coated pits (putative) - contains 8 C-type lectin domains - contains 1 fibronectin type-2 domain - contains 1 ricin B-type lectin domain Compartment: - cell membrane, secreted (putative) - isoform 2: secreted (putative) Alternative splicing: named isoforms=2 Expression: - present in lung macrophage (at protein level) - highly expressed in kidney - also expressed in pancreas, amnion, choriodecidua & placenta - isoform 2 is expressed at much lower level Pathology: - 85% of membranous glomerulonephritis with PLA2R antibody

General

glycoprotein lectin membrane protein secreted protein

Properties

SIZE: entity length = 1463 aa MW = 169 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-20} Ricin B-type lectin {38-161} MOTIF: cysteine residue {C51} MODIFICATION: cysteine residue {C64} cysteine residue {C64} MODIFICATION: cysteine residue {C51} cysteine residue {C89} MODIFICATION: cysteine residue {C106} N-glycosylation site {N93} cysteine residue {C106} MODIFICATION: cysteine residue {C89} fibronectin type II domain or F2 module SITE: 173-221 FOR-BINDING-OF: collagen MOTIF: cysteine residue {*1} MODIFICATION: cysteine residue {*3} cysteine residue {*2} MODIFICATION: cysteine residue {*4} cysteine residue {*3} MODIFICATION: cysteine residue {*1} cysteine residue {*4} MODIFICATION: cysteine residue {*2} cysteine residue {C178} MODIFICATION: cysteine residue {C204} cysteine residue {C192} MODIFICATION: cysteine residue {C219} cysteine residue {C204} MODIFICATION: cysteine residue {C178} cysteine residue {C219} MODIFICATION: cysteine residue {C192} C-type lectin 1 {238-355} MOTIF: cysteine residue {C260} MODIFICATION: cysteine residue {C354} cysteine residue {C330} MODIFICATION: cysteine residue {C346} cysteine residue {C346} MODIFICATION: cysteine residue {C330} cysteine residue {C354} MODIFICATION: cysteine residue {C260} C-type lectin 2 {385-502} MOTIF: cysteine residue {C406} MODIFICATION: cysteine residue {C501} N-glycosylation site {N454} cysteine residue {C478} MODIFICATION: cysteine residue {C493} cysteine residue {C493} MODIFICATION: cysteine residue {C478} cysteine residue {C501} MODIFICATION: cysteine residue {C406} C-type lectin 3 {522-643} MOTIF: cysteine residue {C617} MODIFICATION: cysteine residue {C634} cysteine residue {C634} MODIFICATION: cysteine residue {C617} C-type lectin 4 {673-797} MOTIF: cysteine residue {C699} MODIFICATION: cysteine residue {C796} cysteine residue {C774} MODIFICATION: cysteine residue {C788} cysteine residue {C788} MODIFICATION: cysteine residue {C774} cysteine residue {C796} MODIFICATION: cysteine residue {C699} C-type lectin 5 {819-938} MOTIF: cysteine residue {C840} MODIFICATION: cysteine residue {C937} cysteine residue {C914} MODIFICATION: cysteine residue {C929} cysteine residue {C929} MODIFICATION: cysteine residue {C914} cysteine residue {C937} MODIFICATION: cysteine residue {C840} C-type lectin 6 {965-1096} MOTIF: cysteine residue {C1067} MODIFICATION: cysteine residue {C1087} cysteine residue {C1087} MODIFICATION: cysteine residue {C1067} C-type lectin 7 {1121-1232} MOTIF: cysteine residue {C1209} MODIFICATION: cysteine residue {C1223} cysteine residue {C1223} MODIFICATION: cysteine residue {C1209} C-type lectin 8 {1257-1378} MOTIF: cysteine residue {C1280} MODIFICATION: cysteine residue {C1377} cysteine residue {C1354} MODIFICATION: cysteine residue {C1369} cysteine residue {C1369} MODIFICATION: cysteine residue {C1354} cysteine residue {C1377} MODIFICATION: cysteine residue {C1280} transmembrane domain {1398-1418} Endocytosis signal {1436-1442}

Database Correlations

OMIM 604939 UniProt Q13018 PFAM correlations

References

UniProt :accession Q13018