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   22-FEB-2023, entry version 79.
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   GlyCosmos; Q5R880; 2 sites, No reported glycans.
DR   GeneID; 100173143; -.
DR   KEGG; pon:100173143; -.
DR   CTD; 22925; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   InParanoid; Q5R880; -.
DR   OrthoDB; 4271106at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; cd00037; CLECT; 8.
DR   CDD; cd00062; FN2; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR   PANTHER; PTHR22803:SF74; SECRETORY PHOSPHOLIPASE A2 RECEPTOR; 1.
DR   Pfam; PF00040; fn2; 1.
DR   Pfam; PF00059; Lectin_C; 8.
DR   PRINTS; PR00013; FNTYPEII.
DR   SMART; SM00034; CLECT; 8.
DR   SMART; SM00059; FN2; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 8.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
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
//