PLA2R_RABIT
ID PLA2R_RABIT Reviewed; 1458 AA.
AC P49260;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 124.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Skeletal muscle;
RX PubMed=8294398; DOI=10.1016/s0021-9258(17)42060-6;
RA Lambeau G., Ancian P., Barhanin J., Lazdunski M.;
RT "Cloning and expression of a membrane receptor for secretory phospholipases
RT A2.";
RL J. Biol. Chem. 269:1575-1578(1994).
RN [2]
RP FUNCTION.
RX PubMed=7548076; DOI=10.1021/bi00040a028;
RA Ancian P., Lambeau G., Lazdunski M.;
RT "Multifunctional activity of the extracellular domain of the M-type (180
RT kDa) membrane receptor for secretory phospholipases A2.";
RL Biochemistry 34:13146-13151(1995).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1432-ASN--THR-1438;
RP SER-1433; 1434-TYR-TYR-1435; PRO-1436 AND SER-1452.
RX PubMed=8550569; DOI=10.1074/jbc.271.1.250;
RA Zvaritch E., Lambeau G., Lazdunski M.;
RT "Endocytic properties of the M-type 180-kDa receptor for secretory
RT phospholipases A2.";
RL J. Biol. Chem. 271:250-257(1996).
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:7548076, ECO:0000269|PubMed:8550569}.
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:0000269|PubMed:8550569};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:8550569}.
CC -!- SUBCELLULAR LOCATION: [Soluble secretory phospholipase A2 receptor]:
CC Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Lung, skeletal muscle, brain, kidney and heart.
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.
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; U03455; AAC48402.1; -; mRNA.
DR PIR; A49707; A49707.
DR RefSeq; NP_001075803.1; NM_001082334.1.
DR AlphaFoldDB; P49260; -.
DR SMR; P49260; -.
DR STRING; 9986.ENSOCUP00000012759; -.
DR PRIDE; P49260; -.
DR GeneID; 100009180; -.
DR KEGG; ocu:100009180; -.
DR CTD; 22925; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P49260; -.
DR OrthoDB; 29241at2759; -.
DR Proteomes; UP000001811; 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 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1458
FT /note="Secretory phospholipase A2 receptor"
FT /id="PRO_0000017551"
FT CHAIN 24..?
FT /note="Soluble secretory phospholipase A2 receptor"
FT /evidence="ECO:0000250"
FT /id="PRO_0000311254"
FT TOPO_DOM 24..1393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1394..1416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1417..1458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..113
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 171..219
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 227..356
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 374..502
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 511..645
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 660..798
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 815..939
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 954..1098
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1117..1231
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1243..1376
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 1432..1438
FT /note="Endocytosis signal"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..62
FT /evidence="ECO:0000250"
FT DISULFID 87..104
FT /evidence="ECO:0000250"
FT DISULFID 176..202
FT /evidence="ECO:0000250"
FT DISULFID 190..217
FT /evidence="ECO:0000250"
FT DISULFID 258..352
FT /evidence="ECO:0000250"
FT DISULFID 328..344
FT /evidence="ECO:0000250"
FT DISULFID 404..499
FT /evidence="ECO:0000250"
FT DISULFID 476..491
FT /evidence="ECO:0000250"
FT DISULFID 615..632
FT /evidence="ECO:0000250"
FT DISULFID 697..794
FT /evidence="ECO:0000250"
FT DISULFID 772..786
FT /evidence="ECO:0000250"
FT DISULFID 838..935
FT /evidence="ECO:0000250"
FT DISULFID 912..927
FT /evidence="ECO:0000250"
FT DISULFID 1065..1085
FT /evidence="ECO:0000250"
FT DISULFID 1207..1221
FT /evidence="ECO:0000250"
FT DISULFID 1278..1373
FT /evidence="ECO:0000250"
FT DISULFID 1350..1365
FT /evidence="ECO:0000250"
FT MUTAGEN 1432..1438
FT /note="Missing: Abolishes receptor internalization."
FT /evidence="ECO:0000269|PubMed:8550569"
FT MUTAGEN 1433
FT /note="S->P: Increases receptor internalization."
FT /evidence="ECO:0000269|PubMed:8550569"
FT MUTAGEN 1434..1435
FT /note="YY->AA: Reduces receptor internalization."
FT /evidence="ECO:0000269|PubMed:8550569"
FT MUTAGEN 1436
FT /note="P->A: Does not affect receptor internalization."
FT /evidence="ECO:0000269|PubMed:8550569"
FT MUTAGEN 1452
FT /note="S->A: Does not affect receptor internalization."
FT /evidence="ECO:0000269|PubMed:8550569"
SQ SEQUENCE 1458 AA; 167200 MW; 686163066DAB9511 CRC64;
MLLSLLLLLL LGAPRRCTEG AAAALSPERV LKWQEKGIFI IQSESLKSCI QAGKSVLTLE
SCKQPNKNML WKWVSNQHLF NIGGSGCLGL NLSNPEQPLG LYECDSTHVS LRWRCNRKMI
TGPLQHTVQV KQDNIIVASG KRLHKWISYM SDSGDICQHV HKDLYTRKGN AHGTPCMFPF
QYNHQWHHEC TREGRQDDSL WCATTSRYER DEKWGFCPDP TSAEVGCDAV WEKDLNSHIC
YQFNLLSSLS WSEAHSSCQM HGGALLSIVD EAEENFIRKQ VSGEAVEVWT GLNQLDVNAG
WQWSDGTPLS YLNWSPEISF EPFVEYHCGT FNSFMPRAWR SRNCESTLPY ICKKYLNHVD
DEIVEKDAWK YYATDCEPGW APYHRNCYKL QKEEKTWNEA LHSCLSSNST LIDIGSLAEV
EFLVTLLGNE NASETWIGLS SNTFPVSFEW SNGSSVIFTN WHTLEPQIFP NRSQLCVSAE
QSEGHWKVTD CEETHFYVCK KPGHVLSDAE SGCQEGWERH GGFCYKIDTV LRSFDHASSG
YYCPPALVTI ADRFEQAFIT SLISSVVNMK DSYFWIALQD QNDTGEYTWK TAGQKSEPVQ
YTHWNAHQPR SSGGCVAIRG RNPIGRWEVK DCVHFKAMSL CKQPVETREK MEHEERWPFH
PCYLDWESQP GLASCFKVFH SEKVLMKRTW REAEAFCEEF GAHLASFAHI EEENFVNELL
HPKFNRSEER QFWIGFNKRN PLNAGSWEWS DGTPVISSFL DNNYFGEDTR NCAVYKANKT
LLPLHCGSKR EWICKIPRDV RPKIPSWYQY DAPWLFHQDA EYLFYPHSSE WSSFEFVCGW
LRSDILTIHS AHEQEFILSK IKALSKYGAN WWIGLQEETA NDELRWRDGT PVIYQNWDKE
RDRSMNNQSQ RCAFISSITG LWDREECSVS MPSICKRKTF WVIEKEKDTP KQHGTCPKGW
LYFDYKCLLV NVPKDPSNWK NWTQARDFCF DEGGTLVAIE SEVEQAFITM NLFGQTTNVW
IGLQNDDYEK WLNGNPVAYS NWSPSDIINI PSYNTTADQK PIPLCALLSS NPNFHFTGKW
YFEDCGKEGY GFVCEKIQDS AGHEVNTSIM DPIPNTLEYG NRTYKIINAN MTWYAAIKSC
QLHGAELVSI TDQYHQSFLT VILSRLGHAH WIGLFTADNG LHFDWSDGTK SSFTFWKDED
SSFLGDCVFA DTSGRWHSTA CESFLQGAIC HVPTETRPFE HPELCSETSI PWIKFKSNCY
SFSTVLHSAS FEAAHEFCKK EGSNLLTIKD EAENSFLLEE PFAFGASVQM VWLNAQFDNE
TVKWLDGTPA DQSNWGIRKP DMAHFEPHQC LALRIPEGVW QLSPCQKNMG FICKMKADIH
TVKEHPGKGP SHSIVPLAVA LTLVVILAII TLSFYIYKQN KGFFRRLAGV GNSYYPTTNF
STIHLEENIL ISDLEKND
