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Q62028

- PLA2R_MOUSE

UniProt

Q62028 - PLA2R_MOUSE

Protein

Secretory phospholipase A2 receptor

Gene

Pla2r1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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/PLA2G10.11 Publications

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. phospholipase binding Source: UniProtKB
    3. receptor activity Source: UniProtKB

    GO - Biological processi

    1. cytokine production Source: UniProtKB
    2. negative regulation of arachidonic acid secretion Source: UniProtKB
    3. negative regulation of phospholipase A2 activity Source: UniProtKB
    4. oxidative stress-induced premature senescence Source: UniProtKB
    5. positive regulation of arachidonic acid secretion Source: UniProtKB
    6. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    7. reactive oxygen species metabolic process Source: UniProtKB
    8. receptor-mediated endocytosis Source: UniProtKB
    9. replicative senescence Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended 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:
    Soluble secretory phospholipase A2 receptor
    Short name:
    Soluble PLA2-R
    Short name:
    Soluble PLA2R
    Gene namesi
    Name:Pla2r1
    Synonyms:Pla2g1br
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:102468. Pla2r1.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. extracellular region Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB
    5. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626By similarityAdd
    BLAST
    Chaini27 – 14871461Secretory phospholipase A2 receptorPRO_5000139804Add
    BLAST
    Chaini27 – ?Soluble secretory phospholipase A2 receptorCuratedPRO_0000311251

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi55 ↔ 68By similarity
    Disulfide bondi93 ↔ 110By similarity
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi181 ↔ 207By similarity
    Disulfide bondi195 ↔ 222By similarity
    Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi263 ↔ 356By similarity
    Disulfide bondi333 ↔ 348By similarity
    Disulfide bondi408 ↔ 503By similarity
    Disulfide bondi480 ↔ 495By similarity
    Disulfide bondi617 ↔ 634By similarity
    Disulfide bondi699 ↔ 796By similarity
    Disulfide bondi774 ↔ 788By similarity
    Disulfide bondi840 ↔ 937By similarity
    Disulfide bondi914 ↔ 929By similarity
    Glycosylationi928 – 9281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1066 ↔ 1086By similarity
    Glycosylationi1107 – 11071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1122 – 11221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1131 – 11311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1208 ↔ 1222By similarity
    Disulfide bondi1279 ↔ 1376By similarity
    Disulfide bondi1353 ↔ 1368By similarity

    Post-translational modificationi

    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 PubMed:11830583, or by alternative splicing.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ62028.
    PRIDEiQ62028.

    Expressioni

    Tissue specificityi

    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).3 Publications

    Inductioni

    Following exposure to endotoxin (at protein level).1 Publication

    Gene expression databases

    BgeeiQ62028.
    CleanExiMM_PLA2R1.
    GenevestigatoriQ62028.

    Interactioni

    Protein-protein interaction databases

    IntActiQ62028. 1 interaction.
    MINTiMINT-4109893.
    STRINGi10090.ENSMUSP00000108144.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62028.
    SMRiQ62028. Positions 120-358, 380-505, 516-647, 662-797, 812-939, 957-1096, 1112-1235, 1253-1379.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 13961370ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1418 – 148770CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1397 – 141721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 165124Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST
    Domaini176 – 22449Fibronectin type-IIPROSITE-ProRule annotationAdd
    BLAST
    Domaini241 – 357117C-type lectin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini387 – 504118C-type lectin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini524 – 643120C-type lectin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini673 – 797125C-type lectin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini819 – 938120C-type lectin 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini964 – 1095132C-type lectin 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1120 – 1231112C-type lectin 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1256 – 1377122C-type lectin 8PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1435 – 14417Endocytosis signal

    Domaini

    C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B.1 Publication
    The endocytosis signal probably mediates endocytosis via clathrin-coated pits.By similarity

    Sequence similaritiesi

    Contains 8 C-type lectin domains.PROSITE-ProRule annotation
    Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG288621.
    GeneTreeiENSGT00720000108514.
    HOGENOMiHOG000231191.
    HOVERGENiHBG108261.
    InParanoidiQ62028.
    KOiK06560.
    OrthoDBiEOG7FFMQR.
    PhylomeDBiQ62028.
    TreeFamiTF316663.

    Family and domain databases

    Gene3Di2.10.10.10. 1 hit.
    3.10.100.10. 8 hits.
    InterProiIPR001304. 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]
    PfamiPF00040. fn2. 1 hit.
    PF00059. Lectin_C. 8 hits.
    [Graphical view]
    SMARTiSM00034. CLECT. 8 hits.
    SM00059. FN2. 1 hit.
    SM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF56436. SSF56436. 8 hits.
    PROSITEiPS00615. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q62028-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MVQWLAMLQL LWLQQLLLLG IHQGIAQDLT HIQEPSLEWR DKGIFIIQSE     50
    SLKTCIQAGK SVLTLENCKQ PNEHMLWKWV SDDHLFNVGG SGCLGLNISA 100
    LEQPLKLYEC DSTLISLRWH CDRKMIEGPL QYKVQVKSDN TVVARKQIHR 150
    WIAYTSSGGD ICEHPSRDLY TLKGNAHGMP CVFPFQFKGH WHHDCIREGQ 200
    KEHLLWCATT SRYEEDEKWG FCPDPTSMKV FCDATWQRNG SSRICYQFNL 250
    LSSLSWNQAH SSCLMQGGAL LSIADEDEED FIRKHLSKVV KEVWIGLNQL 300
    DEKAGWQWSD GTPLSYLNWS QEITPGPFVE HHCGTLEVVS AAWRSRDCES 350
    TLPYICKRDL NHTAQGILEK DSWKYHATHC DPDWTPFNRK CYKLKKDRKS 400
    WLGALHSCQS NDSVLMDVAS LAEVEFLVSL LRDENASETW IGLSSNKIPV 450
    SFEWSSGSSV IFTNWYPLEP RILPNRRQLC VSAEESDGRW KVKDCKERLF 500
    YICKKAGQVP ADEQSGCPAG WERHGRFCYK IDTVLRSFEE ASSGYYCSPA 550
    LLTITSRFEQ AFITSLISSV AEKDSYFWIA LQDQNNTGEY TWKTVGQREP 600
    VQYTYWNTRQ PSNRGGCVVV RGGSSLGRWE VKDCSDFKAM SLCKTPVKIW 650
    EKTELEERWP FHPCYMDWES ATGLASCFKV FHSEKVLMKR SWREAEAFCE 700
    EFGAHLASFA HIEEENFVNE LLHSKFNWTQ ERQFWIGFNR RNPLNAGSWA 750
    WSDGSPVVSS FLDNAYFEED AKNCAVYKAN KTLLPSNCAS KHEWICRIPR 800
    DVRPKFPDWY QYDAPWLFYQ NAEYLFHTHP AEWATFEFVC GWLRSDFLTI 850
    YSAQEQEFIH SKIKGLTKYG VKWWIGLEEG GARDQIQWSN GSPVIFQNWD 900
    KGREERVDSQ RKRCVFISSI TGLWGTENCS VPLPSICKRV KIWVIEKEKP 950
    PTQPGTCPKG WLYFNYKCFL VTIPKDPREL KTWTGAQEFC VAKGGTLVSI 1000
    KSELEQAFIT MNLFGQTTNV WIGLQSTNHE KWVNGKPLVY SNWSPSDIIN 1050
    IPSYNTTEFQ KHIPLCALMS SNPNFHFTGK WYFDDCGKEG YGFVCEKMQD 1100
    TLEHHVNVSD TSAIPSTLEY GNRTYKIIRG NMTWYAAGKS CRMHRAELAS 1150
    IPDAFHQAFL TVLLSRLGHT HWIGLSTTDN GQTFDWSDGT KSPFTYWKDE 1200
    ESAFLGDCAF ADTNGRWHST ACESFLQGAI CHVVTETKAF EHPGLCSETS 1250
    VPWIKFKGNC YSFSTVLDSR SFEDAHEFCK SEGSNLLAIR DAAENSFLLE 1300
    ELLAFGSSVQ MVWLNAQFDN NNKTLRWFDG TPTEQSNWGL RKPDMDHLKP 1350
    HPCVVLRIPE GIWHFTPCED KKGFICKMEA GIPAVTAQPE KGLSHSIVPV 1400
    TVTLTLIIAL GIFMLCFWIY KQKSDIFQRL TGSRGSYYPT LNFSTAHLEE 1450
    NILISDLEKN TNDEEVRDAP ATESKRGHKG RPICISP 1487
    Length:1,487
    Mass (Da):170,512
    Last modified:November 1, 1996 - v1
    Checksum:iAD8D905859B0EDE8
    GO
    Isoform 2 (identifier: Q62028-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         680-689: VFHSEKVLMK → DTGKAVLDWI
         690-1487: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:689
    Mass (Da):79,127
    Checksum:i846ED8D4A79573B4
    GO

    Sequence cautioni

    The sequence CAM22305.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAM23630.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei680 – 68910VFHSEKVLMK → DTGKAVLDWI in isoform 2. 1 PublicationVSP_029495
    Alternative sequencei690 – 1487798Missing in isoform 2. 1 PublicationVSP_029496Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS16059.1. [Q62028-1]
    PIRiS48719.
    RefSeqiNP_032893.1. NM_008867.2. [Q62028-1]
    UniGeneiMm.5092.

    Genome annotation databases

    EnsembliENSMUST00000067708; ENSMUSP00000065205; ENSMUSG00000054580. [Q62028-1]
    GeneIDi18779.
    KEGGimmu:18779.
    UCSCiuc008jug.2. mouse. [Q62028-1]
    uc008juh.2. mouse. [Q62028-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Phospholipase A2 receptor

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS16059.1. [Q62028-1 ]
    PIRi S48719.
    RefSeqi NP_032893.1. NM_008867.2. [Q62028-1 ]
    UniGenei Mm.5092.

    3D structure databases

    ProteinModelPortali Q62028.
    SMRi Q62028. Positions 120-358, 380-505, 516-647, 662-797, 812-939, 957-1096, 1112-1235, 1253-1379.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q62028. 1 interaction.
    MINTi MINT-4109893.
    STRINGi 10090.ENSMUSP00000108144.

    Proteomic databases

    PaxDbi Q62028.
    PRIDEi Q62028.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067708 ; ENSMUSP00000065205 ; ENSMUSG00000054580 . [Q62028-1 ]
    GeneIDi 18779.
    KEGGi mmu:18779.
    UCSCi uc008jug.2. mouse. [Q62028-1 ]
    uc008juh.2. mouse. [Q62028-2 ]

    Organism-specific databases

    CTDi 22925.
    MGIi MGI:102468. Pla2r1.

    Phylogenomic databases

    eggNOGi NOG288621.
    GeneTreei ENSGT00720000108514.
    HOGENOMi HOG000231191.
    HOVERGENi HBG108261.
    InParanoidi Q62028.
    KOi K06560.
    OrthoDBi EOG7FFMQR.
    PhylomeDBi Q62028.
    TreeFami TF316663.

    Miscellaneous databases

    NextBioi 295027.
    PROi Q62028.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q62028.
    CleanExi MM_PLA2R1.
    Genevestigatori Q62028.

    Family and domain databases

    Gene3Di 2.10.10.10. 1 hit.
    3.10.100.10. 8 hits.
    InterProi IPR001304. 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 ]
    Pfami PF00040. fn2. 1 hit.
    PF00059. Lectin_C. 8 hits.
    [Graphical view ]
    SMARTi SM00034. CLECT. 8 hits.
    SM00059. FN2. 1 hit.
    SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF56436. SSF56436. 8 hits.
    PROSITEi PS00615. 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiPLA2R_MOUSE
    AccessioniPrimary (citable) accession number: Q62028
    Secondary accession number(s): A2AS64, B9EJ68, Q80ZL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3