PLA2R_PONAB
ID PLA2R_PONAB Reviewed; 1464 AA.
AC Q5R880;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Secretory phospholipase A2 receptor;
DE Short=PLA2-R;
DE Short=PLA2R;
DE AltName: Full=180 kDa secretory phospholipase A2 receptor;
DE AltName: Full=M-type receptor;
DE Contains:
DE RecName: Full=Soluble secretory phospholipase A2 receptor;
DE Short=Soluble PLA2-R;
DE Short=Soluble PLA2R;
DE Flags: Precursor;
GN Name=PLA2R1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for secretory phospholipase A2 (sPLA2). Also able to
CC bind to snake PA2-like toxins. Although its precise function remains
CC unclear, binding of sPLA2 to its receptor participates in both positive
CC and negative regulation of sPLA2 functions as well as clearance of
CC sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on
CC the cell type, such as activation of the mitogen-activated protein
CC kinase (MAPK) cascade to induce cell proliferation, the production of
CC lipid mediators, selective release of arachidonic acid in bone marrow-
CC derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can
CC activate p38 MAPK to stimulate elastase release and cell adhesion. May
CC be involved in responses in pro-inflammatory cytokine productions
CC during endotoxic shock. Also has endocytic properties and rapidly
CC internalizes sPLA2 ligands, which is particularly important for the
CC clearance of extracellular sPLA2s to protect their potent enzymatic
CC activities. The soluble secretory phospholipase A2 receptor form is
CC circulating and acts as a negative regulator of sPLA2 functions by
CC blocking the biological functions of sPLA2-IB/PLA2G1B and sPLA2-
CC X/PLA2G10 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with sPLA2-IB/PLA2G1B; this interaction mediates
CC intracellular signaling as well as clearance of extracellular sPLA2-
CC IB/PLA2G1B via endocytotic pathway (By similarity). Interacts with
CC sPLA2-X/PLA2G10; this interaction mediates sPLA2-X/PLA2G10 clearance
CC and inactivation (By similarity). {ECO:0000250|UniProtKB:Q13018,
CC ECO:0000250|UniProtKB:Q62028}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Soluble secretory phospholipase A2 receptor]:
CC Secreted {ECO:0000250}.
CC -!- DOMAIN: C-type lectin domains 3-5 mediate the interaction with
CC phospholipase PLA2G1B. {ECO:0000250}.
CC -!- DOMAIN: The endocytosis signal probably mediates endocytosis via
CC clathrin-coated pits. {ECO:0000250}.
CC -!- PTM: The secretory phospholipase A2 receptor form may be produced by
CC the action of metalloproteinases. It contains all extracellular domains
CC and only lacks transmembrane and cytosolic regions. It is however
CC unclear whether this form is produced by proteolytic cleavage as
CC suggested by some experiments, or by alternative splicing (By
CC similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH92030.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR859874; CAH92030.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001126180.1; NM_001132708.1.
DR AlphaFoldDB; Q5R880; -.
DR SMR; Q5R880; -.
DR STRING; 9601.ENSPPYP00000014368; -.
DR PRIDE; Q5R880; -.
DR GeneID; 100173143; -.
DR KEGG; pon:100173143; -.
DR CTD; 22925; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q5R880; -.
DR OrthoDB; 29241at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0043274; F:phospholipase binding; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0090403; P:oxidative stress-induced premature senescence; ISS:UniProtKB.
DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0090399; P:replicative senescence; ISS:UniProtKB.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 3.10.100.10; -; 8.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF56436; SSF56436; 8.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endocytosis; Glycoprotein; Lectin; Membrane;
KW Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..1464
FT /note="Secretory phospholipase A2 receptor"
FT /id="PRO_0000311252"
FT CHAIN 23..?
FT /note="Soluble secretory phospholipase A2 receptor"
FT /evidence="ECO:0000250"
FT /id="PRO_0000311253"
FT TOPO_DOM 23..1398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1399..1419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1420..1464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..163
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 175..223
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 240..357
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 387..504
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 524..645
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 675..799
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 821..940
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 967..1098
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1123..1234
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1259..1379
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 1437..1443
FT /note="Endocytosis signal"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..66
FT /evidence="ECO:0000250"
FT DISULFID 91..108
FT /evidence="ECO:0000250"
FT DISULFID 180..206
FT /evidence="ECO:0000250"
FT DISULFID 194..221
FT /evidence="ECO:0000250"
FT DISULFID 262..356
FT /evidence="ECO:0000250"
FT DISULFID 332..348
FT /evidence="ECO:0000250"
FT DISULFID 408..503
FT /evidence="ECO:0000250"
FT DISULFID 480..495
FT /evidence="ECO:0000250"
FT DISULFID 619..636
FT /evidence="ECO:0000250"
FT DISULFID 701..798
FT /evidence="ECO:0000250"
FT DISULFID 776..790
FT /evidence="ECO:0000250"
FT DISULFID 842..939
FT /evidence="ECO:0000250"
FT DISULFID 916..931
FT /evidence="ECO:0000250"
FT DISULFID 1069..1089
FT /evidence="ECO:0000250"
FT DISULFID 1211..1225
FT /evidence="ECO:0000250"
FT DISULFID 1282..1378
FT /evidence="ECO:0000250"
FT DISULFID 1356..1370
FT /evidence="ECO:0000250"
SQ SEQUENCE 1464 AA; 168437 MW; 8D4DEA5A43CB1C8A CRC64;
MLLSPSLLLP LLLLLGAPRG CAEGVAAALT PERLLEWQDK GIFVIQSESL KKCIQAGKSV
LTLENCKQAN KHMLWKWVSN HGLFNIGGSG CLGLNFSAPE QPLSLYECDS TLVSLRWRCD
RKMITGPLQY SVQVAHDNTV VASRKYFHKW ISYGSGGGDI CEYLHKDLHT IKGNAHGMPC
MFPFQYNHQW HHECTREGRE DDLLWCATTS RYERDEKWGF CPDPTSAEVG CDTIWEKDLN
SHICYQFNLL SSLSWSEAHS SCQMQGGALL SITDETEENF IREHMSSKTV EVWMGLNQLD
EHAGWQWSDG TPLNYLNWSP EVNFEPFVED HCGTFSSFIP SAWRSRDCAS TLPYVCKKYL
NHIDHEIVEK DAWKYYATHC EPGWNPYNRN CYKLQKEEKT WHEALRSCQA DNSALIDITS
LAEVEFLVTL LGDENASETW IGLSSNKIPV SFEWSNDSSV IFTNWHTLEP QIFPNRSQLC
VSAEQSEGHW KVKNCEETLF YVCKKAGHVL SDAESGCQEG WERHGGFCYK IDTVLRSFDQ
ASSGYYCPPA LVTITNRFEQ AFITSLIGSV VKMKDSYFWI ALQDQNDTGE YTWKPAGQKP
EPVQYTHWNA HQPRYSGGCV AMRGRHPPGR WEVKHCRHFK AMSLCKQPVE NQEKAEYEER
WPFHPCYLDW ESEPGLASCF KVFHSEKVLM KRTWREAEAF CEEFGAHLAS FAHIEEENFV
NELLYSKFNW TEERQFWIGF NKRNPLNAGS WEWSDRIPVV SSFLDNNYFG EDARNCAVYK
ANKTLLPLHC GSKREWICKI PRDVKPKIPF WYQYDVPWLF YQDAEYLFHT FASEWLNFEF
VCSWLHSDLL TIHSAHEQEF IHSKIKALSK YGASWWIGLQ EERANDEFRW RDGTPVIYQN
WDTGRERPVN NQSQRCGFIS SITGLWGSEE CSVSMPSICK RKKVLLIEKK KDTPKQHGTC
PKGWLYFNYK CLLLNIPKDP NSWKNWMHAQ HFCAEEGGTL VAIESEVEQA FITMNLFGQT
TNVWIGLQND DYETWLNGKP VVYSNWSPFD IINIPSHNTT DVQKHIPLCA LLSSNPNFHF
TGKWYFEDCG KEGYGFVCEK MQDTSGHGVN TSDMYPMPNT LEYGNRTYKI INANMTWYAA
IKTCLMHGTQ LVSITDQYHQ SFLTVVLNRL GYAHWIGLFT TDNGLNFDWS DGTKSSFTFW
KDEESSLLGD CVFADTNGLW HSTACESFLQ GAICHVPPET RQSEHPELCS ETSIPWIKFK
SNCYSFSTVL DRMSFEAAHE FCKKEGSNLL TIKDEAENAF LLEELFAFGS SVQMVWLNAQ
FDGNNETIKW FDGTPTDQSN WGIRKPDTDY FKPHHCVALR IPEGLQLSLC QEKKGFICKM
EADIRTAEEL PEKGPSHSII PLAVVLTLIV IVAICTLSFC IYKHNGGFFR RLAGFRNPYY
PATNFSTVHL EENILISDLE KSDQ
