PLA2R_BOVIN
ID PLA2R_BOVIN Reviewed; 1463 AA.
AC P49259;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=7509792; DOI=10.1016/s0021-9258(17)37546-4;
RA Ishizaki J., Hanasaki K., Higashino K., Kishino J., Kikuchi N., Ohara O.,
RA Arita H.;
RT "Molecular cloning of pancreatic group I phospholipase A2 receptor.";
RL J. Biol. Chem. 269:5897-5904(1994).
RN [2]
RP FUNCTION.
RX PubMed=7726849; DOI=10.1006/bbrc.1995.1502;
RA Fujita H., Kawamoto K., Hanasaki K., Arita H.;
RT "Glycosylation-dependent binding of pancreatic type I phospholipase A2 to
RT its specific receptor.";
RL Biochem. Biophys. Res. Commun. 209:293-299(1995).
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. {ECO:0000269|PubMed:7726849}.
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}.
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DR EMBL; D16109; BAA03683.1; -; mRNA.
DR PIR; A53210; A53210.
DR RefSeq; NP_778221.1; NM_175051.1.
DR AlphaFoldDB; P49259; -.
DR SMR; P49259; -.
DR STRING; 9913.ENSBTAP00000043437; -.
DR PaxDb; P49259; -.
DR Ensembl; ENSBTAT00000046112; ENSBTAP00000043437; ENSBTAG00000032515.
DR GeneID; 317777; -.
DR KEGG; bta:317777; -.
DR CTD; 22925; -.
DR VEuPathDB; HostDB:ENSBTAG00000032515; -.
DR VGNC; VGNC:32966; PLA2R1.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244842; -.
DR HOGENOM; CLU_002069_2_0_1; -.
DR InParanoid; P49259; -.
DR OrthoDB; 29241at2759; -.
DR TreeFam; TF316663; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000032515; Expressed in omental fat pad and 97 other tissues.
DR ExpressionAtlas; P49259; baseline and differential.
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:0043235; C:receptor complex; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Endocytosis;
KW Glycoprotein; Lectin; Membrane; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:7509792"
FT CHAIN 21..1463
FT /note="Secretory phospholipase A2 receptor"
FT /id="PRO_0000017550"
FT CHAIN 21..?
FT /note="Soluble secretory phospholipase A2 receptor"
FT /evidence="ECO:0000250"
FT /id="PRO_0000311249"
FT TOPO_DOM 21..1392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1393..1421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1422..1463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..115
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 173..221
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 229..353
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 357..500
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 504..641
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 646..795
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 799..937
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 941..1095
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1099..1230
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1235..1376
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 1436..1442
FT /note="Endocytosis signal"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 178..204
FT /evidence="ECO:0000250"
FT DISULFID 192..219
FT /evidence="ECO:0000250"
FT DISULFID 260..354
FT /evidence="ECO:0000250"
FT DISULFID 330..346
FT /evidence="ECO:0000250"
FT DISULFID 406..501
FT /evidence="ECO:0000250"
FT DISULFID 478..493
FT /evidence="ECO:0000250"
FT DISULFID 617..634
FT /evidence="ECO:0000250"
FT DISULFID 699..796
FT /evidence="ECO:0000250"
FT DISULFID 774..788
FT /evidence="ECO:0000250"
FT DISULFID 840..938
FT /evidence="ECO:0000250"
FT DISULFID 915..930
FT /evidence="ECO:0000250"
FT DISULFID 992..1096
FT /evidence="ECO:0000250"
FT DISULFID 1068..1088
FT /evidence="ECO:0000250"
FT DISULFID 1209..1223
FT /evidence="ECO:0000250"
FT DISULFID 1280..1377
FT /evidence="ECO:0000250"
FT DISULFID 1354..1369
FT /evidence="ECO:0000250"
SQ SEQUENCE 1463 AA; 168651 MW; 4276FF206F92A397 CRC64;
MPLLSLSLLL LLLQVPAGSA ETAAWAVTPE RLREWQDKGI FIIQSENLEK CIQASKSTLT
LENCKPPNKY MLWKWVSNHR LFNIGGSGCL GLNVSSPEQP LSIYECDSTH VSLKWHCNKK
TITGPLQYLV QVKQDNTLVA SRKYLHKWVS YMSGGGGICD YLHKDLYTIK GNAHGTPCMF
PFQYNQQWHH ECTREGREDN LLWCATTSRY ERDEKWGFCP DPTSTEVGCD AVWEKDLHSR
ICYQFNLLSS LSWSEAHSSC QMQGAALLSI ADETEENFVR KHLGSEAVEV WMGLNQLDED
AGWQWSDRTP LNYLNWKPEI NFEPFVEYHC GTFNAFMPKA WKSRDCESTL PYVCKKYLNP
TDHGVVEKDA WKYYATHCEP GWNPHNRNCY KLQKEKKTWN EALQSCQSNN SVLTDITSLA
EVEFLVTLLG DENASETWIG LSSHKIPVSF EWSNGSSVTF TNWHTLEPHI FPNRSQLCVS
AEQSEGHWKV KNCEETLFYL CKKTGLVLSD TESGCQKGWE RHGKFCYKID TVLRSFDHAS
SGYYCPPALI TITSRFEQAF ITSLISSVVK TKDTYFWIAL QDQNNTGEYT WKTAGQQLEP
VKYTHWNTRQ PRYSGGCVVM RGRSHPGRWE VRDCRHFKAM SLCKQPVENR EKTKQEEGWP
FHPCYLDWES EPGLASCFKV FHSEKVLMKR TWRQAEEFCE EFGAHLASFA HIEEENFVNE
LLHSKFNRTE ERQFWIGFNK RNPLNAGSWE WSDGTPVVSS FLDNSYFGED ARNCAVYKAN
KTLLPSYCGS KREWICKIPR DVRPKVPPWY QYDAPWLFYQ DAEYLFHISA SEWSSFEFVC
GWLRSDILTI HSAHEQEFIH SKIRALSKYG VNWWIGLREE RASDEFRWRD GSPVIYQNWD
KGKERSMGLN ESQRCGFISS ITGLWASEEC SISMPSICKR KKVWVIEKKK DIPKQHGTCP
KGWLYFDYKC LLLKIPEGPS DWKNWTSAQD FCVEEGGTLV AIENEVEQAF ITMNLFGHTT
NVWIGLQDDD YEKWLNGRPV SYSNWSPFDT KNIPNHNTTE VQKRIPLCGL LSNNPNFHFT
GKWYFEDCRE GYGFVCEKMQ DASGHSINTS DMYPIPNTLE YGNRTYKIIN ANMTWYTALK
TCLMHGAELA SITDQYHQSF LTVILNRVGY AHWIGLFTED NGLSFDWSDG TKSSFTFWKD
DESSFLGDCV FADTSGRWSS TACESYLQGA ICQVPTETRL SGRLELCSET SIPWIKFKSN
CYSFSTVLES TSFEAAHEFC KKKGSNLLTI KDEAENSFLL EELLAFRSSV QMIWLNAQFD
GDNETIKWFD GTPTDQSNWG IRKPEVYHFK PHLCVALRIP EGVWQLSSCQ DKKGFICKME
ADIHTVKKHP GKGPSHSVIP LTVALTLLVI LAISTLSFCM YKHSHIIFGR LAQFRNPYYP
SANFSTVHLE ENILISDLEK NDQ
