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Q62028 (PLA2R_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Secretory phospholipase A2 receptor

Short name=PLA2-R
Short name=PLA2R
Alternative name(s):
180 kDa secretory phospholipase A2 receptor
M-type receptor

Cleaved into the following chain:

  1. Soluble secretory phospholipase A2 receptor
    Short name=Soluble PLA2-R
    Short name=Soluble PLA2R
Gene names
Name:Pla2r1
Synonyms:Pla2g1br
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1487 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for secretory phospholipase A2 (sPLA2). Acts as a receptor for phosholipases sPLA2-IB/PLA2G1B, sPLA2-X/PLA2G10 and, with lower affinity, sPLA2-IIA/PLA2G2A. Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, 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 and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B and sPLA2-X/PLA2G10. Ref.1 Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.12.

Soluble secretory phospholipase A2 receptor: Secreted Ref.12.

Tissue specificity

Widely expressed. Present in type II alveolar epithelial cells and a subset of splenic lymphocytes. Present at the surface of polymorphonuclear neutrophils (at protein level). Ref.1 Ref.5 Ref.11

Induction

Following exposure to endotoxin (at protein level). Ref.5

Domain

C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B. Ref.1

The endocytosis signal probably mediates endocytosis via clathrin-coated pits By similarity. Ref.1

Post-translational modification

The secretory phospholipase A2 receptor form may be produced by the action of metalloproteinases. It contains all extracellular domains and only lacks transmembrane and cytosolic regions. It is however unclear whether this form is produced by proteolytic cleavage as suggested by some experiments reported by Ref.12, or by alternative splicing.

Disruption phenotype

Mice are viable, fertile and without evident histopathological abnormalities. After challenge with bacterial lipopolysaccharide (LPS), they exhibit longer survival than wild-type mice. They are also resistant to lethal effects of exogenous sPLA2-IB/PLA2G1B after sensitization with sublethal dose of LPS, suggesting a potential role in the progression of endotoxic shock. Ref.4

Sequence similarities

Contains 8 C-type lectin domains.

Contains 1 fibronectin type-II domain.

Contains 1 ricin B-type lectin domain.

Sequence caution

The sequence CAM22305.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAM23630.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandLectin
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of arachidonic acid secretion

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of phospholipase A2 activity

Inferred from direct assay Ref.12. Source: UniProtKB

oxidative stress-induced premature senescence

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of arachidonic acid secretion

Inferred from direct assay Ref.8. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

receptor-mediated endocytosis

Inferred from direct assay Ref.1. Source: UniProtKB

replicative senescence

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from direct assay Ref.12. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

phospholipase binding

Inferred from physical interaction Ref.1Ref.12. Source: UniProtKB

receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q62028-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q62028-2)

The sequence of this isoform differs from the canonical sequence as follows:
     680-689: VFHSEKVLMK → DTGKAVLDWI
     690-1487: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 By similarity
Chain27 – 14871461Secretory phospholipase A2 receptor
PRO_5000139804
Chain27 – ?Soluble secretory phospholipase A2 receptor ProbablePRO_0000311251

Regions

Topological domain27 – 13961370Extracellular Potential
Transmembrane1397 – 141721Helical; Potential
Topological domain1418 – 148770Cytoplasmic Potential
Domain42 – 165124Ricin B-type lectin
Domain176 – 22449Fibronectin type-II
Domain241 – 357117C-type lectin 1
Domain387 – 504118C-type lectin 2
Domain524 – 643120C-type lectin 3
Domain673 – 797125C-type lectin 4
Domain819 – 938120C-type lectin 5
Domain964 – 1095132C-type lectin 6
Domain1120 – 1231112C-type lectin 7
Domain1256 – 1377122C-type lectin 8
Motif1435 – 14417Endocytosis signal

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation9281N-linked (GlcNAc...) Potential
Glycosylation11071N-linked (GlcNAc...) Potential
Glycosylation11221N-linked (GlcNAc...) Potential
Glycosylation11311N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 68 By similarity
Disulfide bond93 ↔ 110 By similarity
Disulfide bond181 ↔ 207 By similarity
Disulfide bond195 ↔ 222 By similarity
Disulfide bond263 ↔ 356 By similarity
Disulfide bond333 ↔ 348 By similarity
Disulfide bond408 ↔ 503 By similarity
Disulfide bond480 ↔ 495 By similarity
Disulfide bond617 ↔ 634 By similarity
Disulfide bond699 ↔ 796 By similarity
Disulfide bond774 ↔ 788 By similarity
Disulfide bond840 ↔ 937 By similarity
Disulfide bond914 ↔ 929 By similarity
Disulfide bond1066 ↔ 1086 By similarity
Disulfide bond1208 ↔ 1222 By similarity
Disulfide bond1279 ↔ 1376 By similarity
Disulfide bond1353 ↔ 1368 By similarity

Natural variations

Alternative sequence680 – 68910VFHSEKVLMK → DTGKAVLDWI in isoform 2.
VSP_029495
Alternative sequence690 – 1487798Missing in isoform 2.
VSP_029496

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AD8D905859B0EDE8

FASTA1,487170,512
        10         20         30         40         50         60 
MVQWLAMLQL LWLQQLLLLG IHQGIAQDLT HIQEPSLEWR DKGIFIIQSE SLKTCIQAGK 

        70         80         90        100        110        120 
SVLTLENCKQ PNEHMLWKWV SDDHLFNVGG SGCLGLNISA LEQPLKLYEC DSTLISLRWH 

       130        140        150        160        170        180 
CDRKMIEGPL QYKVQVKSDN TVVARKQIHR WIAYTSSGGD ICEHPSRDLY TLKGNAHGMP 

       190        200        210        220        230        240 
CVFPFQFKGH WHHDCIREGQ KEHLLWCATT SRYEEDEKWG FCPDPTSMKV FCDATWQRNG 

       250        260        270        280        290        300 
SSRICYQFNL LSSLSWNQAH SSCLMQGGAL LSIADEDEED FIRKHLSKVV KEVWIGLNQL 

       310        320        330        340        350        360 
DEKAGWQWSD GTPLSYLNWS QEITPGPFVE HHCGTLEVVS AAWRSRDCES TLPYICKRDL 

       370        380        390        400        410        420 
NHTAQGILEK DSWKYHATHC DPDWTPFNRK CYKLKKDRKS WLGALHSCQS NDSVLMDVAS 

       430        440        450        460        470        480 
LAEVEFLVSL LRDENASETW IGLSSNKIPV SFEWSSGSSV IFTNWYPLEP RILPNRRQLC 

       490        500        510        520        530        540 
VSAEESDGRW KVKDCKERLF YICKKAGQVP ADEQSGCPAG WERHGRFCYK IDTVLRSFEE 

       550        560        570        580        590        600 
ASSGYYCSPA LLTITSRFEQ AFITSLISSV AEKDSYFWIA LQDQNNTGEY TWKTVGQREP 

       610        620        630        640        650        660 
VQYTYWNTRQ PSNRGGCVVV RGGSSLGRWE VKDCSDFKAM SLCKTPVKIW EKTELEERWP 

       670        680        690        700        710        720 
FHPCYMDWES ATGLASCFKV FHSEKVLMKR SWREAEAFCE EFGAHLASFA HIEEENFVNE 

       730        740        750        760        770        780 
LLHSKFNWTQ ERQFWIGFNR RNPLNAGSWA WSDGSPVVSS FLDNAYFEED AKNCAVYKAN 

       790        800        810        820        830        840 
KTLLPSNCAS KHEWICRIPR DVRPKFPDWY QYDAPWLFYQ NAEYLFHTHP AEWATFEFVC 

       850        860        870        880        890        900 
GWLRSDFLTI YSAQEQEFIH SKIKGLTKYG VKWWIGLEEG GARDQIQWSN GSPVIFQNWD 

       910        920        930        940        950        960 
KGREERVDSQ RKRCVFISSI TGLWGTENCS VPLPSICKRV KIWVIEKEKP PTQPGTCPKG 

       970        980        990       1000       1010       1020 
WLYFNYKCFL VTIPKDPREL KTWTGAQEFC VAKGGTLVSI KSELEQAFIT MNLFGQTTNV 

      1030       1040       1050       1060       1070       1080 
WIGLQSTNHE KWVNGKPLVY SNWSPSDIIN IPSYNTTEFQ KHIPLCALMS SNPNFHFTGK 

      1090       1100       1110       1120       1130       1140 
WYFDDCGKEG YGFVCEKMQD TLEHHVNVSD TSAIPSTLEY GNRTYKIIRG NMTWYAAGKS 

      1150       1160       1170       1180       1190       1200 
CRMHRAELAS IPDAFHQAFL TVLLSRLGHT HWIGLSTTDN GQTFDWSDGT KSPFTYWKDE 

      1210       1220       1230       1240       1250       1260 
ESAFLGDCAF ADTNGRWHST ACESFLQGAI CHVVTETKAF EHPGLCSETS VPWIKFKGNC 

      1270       1280       1290       1300       1310       1320 
YSFSTVLDSR SFEDAHEFCK SEGSNLLAIR DAAENSFLLE ELLAFGSSVQ MVWLNAQFDN 

      1330       1340       1350       1360       1370       1380 
NNKTLRWFDG TPTEQSNWGL RKPDMDHLKP HPCVVLRIPE GIWHFTPCED KKGFICKMEA 

      1390       1400       1410       1420       1430       1440 
GIPAVTAQPE KGLSHSIVPV TVTLTLIIAL GIFMLCFWIY KQKSDIFQRL TGSRGSYYPT 

      1450       1460       1470       1480 
LNFSTAHLEE NILISDLEKN TNDEEVRDAP ATESKRGHKG RPICISP 

« Hide

Isoform 2 [UniParc].

Checksum: 846ED8D4A79573B4
Show »

FASTA68979,127

References

« Hide 'large scale' references
[1]"Structural comparison of phospholipase-A2-binding regions in phospholipase-A2 receptors from various mammals."
Higashino K., Ishizaki J., Kishino J., Ohara O., Arita H.
Eur. J. Biochem. 225:375-382(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DOMAIN, TISSUE SPECIFICITY.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Eye.
[4]"Resistance to endotoxic shock in phospholipase A2 receptor-deficient mice."
Hanasaki K., Yokota Y., Ishizaki J., Itoh T., Arita H.
J. Biol. Chem. 272:32792-32797(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"Enhanced tissue expression and elevated circulating level of phospholipase A(2) receptor during murine endotoxic shock."
Yokota Y., Ikeda M., Higashino K., Nakano K., Fujii N., Arita H., Hanasaki K.
Arch. Biochem. Biophys. 379:7-17(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[6]"Mouse group X secretory phospholipase A2 induces a potent release of arachidonic acid from spleen cells and acts as a ligand for the phospholipase A2 receptor."
Morioka Y., Saiga A., Yokota Y., Suzuki N., Ikeda M., Ono T., Nakano K., Fujii N., Ishizaki J., Arita H., Hanasaki K.
Arch. Biochem. Biophys. 381:31-42(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Identification of group X secretory phospholipase A(2) as a natural ligand for mouse phospholipase A(2) receptor."
Yokota Y., Higashino K., Nakano K., Arita H., Hanasaki K.
FEBS Lett. 478:187-191(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Secretory phospholipase A2 receptor-mediated activation of cytosolic phospholipase A2 in murine bone marrow-derived mast cells."
Fonteh A.N., Atsumi G., LaPorte T., Chilton F.H.
J. Immunol. 165:2773-2782(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Pancreatic phospholipase A2 via its receptor regulates expression of key enzymes of phospholipid and sphingolipid metabolism."
Mandal A.K., Zhang Z., Chou J.Y., Mukherjee A.B.
FASEB J. 15:1834-1836(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Clearance of group X secretory phospholipase A(2) via mouse phospholipase A(2) receptor."
Yokota Y., Notoya M., Higashino K., Ishimoto Y., Nakano K., Arita H., Hanasaki K.
FEBS Lett. 509:250-254(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Presence of the M-type sPLA(2) receptor on neutrophils and its role in elastase release and adhesion."
Silliman C.C., Moore E.E., Zallen G., Gonzalez R., Johnson J.L., Elzi D.J., Meng X., Hanasaki K., Ishizaki J., Arita H., Ao L., England K.M., Banerjee A.
Am. J. Physiol. 283:C1102-C1113(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]"Identification of a soluble form phospholipase A2 receptor as a circulating endogenous inhibitor for secretory phospholipase A2."
Higashino Ki K., Yokota Y., Ono T., Kamitani S., Arita H., Hanasaki K.
J. Biol. Chem. 277:13583-13588(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, POSSIBLE PROTEOLYTIC PROCESSING.
[13]"Binding to the high-affinity M-type receptor for secreted phospholipases A(2) is not obligatory for the presynaptic neurotoxicity of ammodytoxin A."
Prijatelj P., Vardjan N., Rowan E.G., Krizaj I., Pungercar J.
Biochimie 88:1425-1433(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Recombinant production and properties of binding of the full set of mouse secreted phospholipases A2 to the mouse M-type receptor."
Rouault M., Le Calvez C., Boilard E., Surrel F., Singer A., Ghomashchi F., Bezzine S., Scarzello S., Bollinger J., Gelb M.H., Lambeau G.
Biochemistry 46:1647-1662(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30779 mRNA. Translation: BAA06443.1.
BX679662, AL928546 Genomic DNA. Translation: CAM22305.1. Different initiation.
AL928546, BX679662 Genomic DNA. Translation: CAM23630.1. Different initiation.
BC048780 mRNA. Translation: AAH48780.1.
BC141355 mRNA. Translation: AAI41356.1.
BC141356 mRNA. Translation: AAI41357.1.
PIRS48719.
RefSeqNP_032893.1. NM_008867.2.
UniGeneMm.5092.

3D structure databases

ProteinModelPortalQ62028.
SMRQ62028. Positions 41-358, 380-505, 517-613, 664-798, 816-955, 957-1096, 1253-1379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ62028. 1 interaction.
MINTMINT-4109893.
STRING10090.ENSMUSP00000108144.

Proteomic databases

PaxDbQ62028.
PRIDEQ62028.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067708; ENSMUSP00000065205; ENSMUSG00000054580. [Q62028-1]
GeneID18779.
KEGGmmu:18779.
UCSCuc008jug.2. mouse. [Q62028-1]
uc008juh.2. mouse. [Q62028-2]

Organism-specific databases

CTD22925.
MGIMGI:102468. Pla2r1.

Phylogenomic databases

eggNOGNOG288621.
GeneTreeENSGT00720000108514.
HOGENOMHOG000231191.
HOVERGENHBG108261.
InParanoidQ62028.
KOK06560.
OrthoDBEOG7FFMQR.
PhylomeDBQ62028.
TreeFamTF316663.

Gene expression databases

BgeeQ62028.
CleanExMM_PLA2R1.
GenevestigatorQ62028.

Family and domain databases

Gene3D2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view]
SMARTSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
PROSITEPS00615. C_TYPE_LECTIN_1. 2 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295027.
PROQ62028.
SOURCESearch...

Entry information

Entry namePLA2R_MOUSE
AccessionPrimary (citable) accession number: Q62028
Secondary accession number(s): A2AS64, B9EJ68, Q80ZL5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot