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Q13018

- PLA2R_HUMAN

UniProt

Q13018 - PLA2R_HUMAN

Protein

Secretory phospholipase A2 receptor

Gene

PLA2R1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Receptor for secretory phospholipase A2 (sPLA2). Acts as a receptor for phosholipase sPLA2-IB/PLA2G1B but not 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.2 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

    Protein family/group databases

    MEROPSiS63.015.

    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
    C-type lectin domain family 13 member C
    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:CLEC13C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9042. PLA2R1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. extracellular region Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of membrane Source: UniProtKB-KW
    5. integral component of plasma membrane Source: UniProtKB
    6. plasma membrane Source: UniProtKB
    7. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33369.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Chaini21 – 14631443Secretory phospholipase A2 receptorPRO_5000144349Add
    BLAST
    Chaini21 – ?Soluble secretory phospholipase A2 receptorBy similarityPRO_0000311250

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi51 ↔ 64By similarity
    Disulfide bondi89 ↔ 106By similarity
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi178 ↔ 204By similarity
    Disulfide bondi192 ↔ 219By similarity
    Disulfide bondi260 ↔ 354By similarity
    Disulfide bondi330 ↔ 346By similarity
    Disulfide bondi406 ↔ 501By similarity
    Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi478 ↔ 493By similarity
    Disulfide bondi617 ↔ 634By similarity
    Disulfide bondi699 ↔ 796By similarity
    Disulfide bondi774 ↔ 788By similarity
    Disulfide bondi840 ↔ 937By similarity
    Disulfide bondi914 ↔ 929By similarity
    Disulfide bondi1067 ↔ 1087By similarity
    Disulfide bondi1209 ↔ 1223By similarity
    Disulfide bondi1280 ↔ 1377By similarity
    Disulfide bondi1354 ↔ 1369By 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, or by alternative splicing, as in the case of isoform 2 that shares all characteristics of secretory phospholipase A2 receptor form By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ13018.
    PRIDEiQ13018.

    Expressioni

    Tissue specificityi

    Present in lung macrophage (at protein level). Highly expressed in kidney. Also expressed in pancreas, amnion, choriodecidua and placenta. Isoform 2 is expressed at much lower level.4 Publications

    Gene expression databases

    BgeeiQ13018.
    CleanExiHS_PLA2R1.
    GenevestigatoriQ13018.

    Organism-specific databases

    HPAiHPA012657.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000283243.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13018.
    SMRiQ13018. Positions 132-223, 229-355, 377-502, 664-805, 816-939, 957-1101, 1119-1232, 1254-1382.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 13971377ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1419 – 146345CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1398 – 141821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 161124Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 22149Fibronectin type-IIPROSITE-ProRule annotationAdd
    BLAST
    Domaini238 – 355118C-type lectin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini385 – 502118C-type lectin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini522 – 643122C-type lectin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini673 – 797125C-type lectin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini819 – 938120C-type lectin 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini965 – 1096132C-type lectin 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1121 – 1232112C-type lectin 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1257 – 1378122C-type lectin 8PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1436 – 14427Endocytosis signal

    Domaini

    C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B.
    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.
    HOVERGENiHBG108261.
    InParanoidiQ13018.
    KOiK06560.
    OMAiWCATTSR.
    OrthoDBiEOG7FFMQR.
    PhylomeDBiQ13018.
    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. 3 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: Q13018-1) [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

    MLLSPSLLLL LLLGAPRGCA EGVAAALTPE RLLEWQDKGI FVIQSESLKK     50
    CIQAGKSVLT LENCKQANKH MLWKWVSNHG LFNIGGSGCL GLNFSAPEQP 100
    LSLYECDSTL VSLRWRCNRK MITGPLQYSV QVAHDNTVVA SRKYIHKWIS 150
    YGSGGGDICE YLHKDLHTIK GNTHGMPCMF PFQYNHQWHH ECTREGREDD 200
    LLWCATTSRY ERDEKWGFCP DPTSAEVGCD TIWEKDLNSH ICYQFNLLSS 250
    LSWSEAHSSC QMQGGTLLSI TDETEENFIR EHMSSKTVEV WMGLNQLDEH 300
    AGWQWSDGTP LNYLNWSPEV NFEPFVEDHC GTFSSFMPSA WRSRDCESTL 350
    PYICKKYLNH IDHEIVEKDA WKYYATHCEP GWNPYNRNCY KLQKEEKTWH 400
    EALRSCQADN SALIDITSLA EVEFLVTLLG DENASETWIG LSSNKIPVSF 450
    EWSNDSSVIF TNWHTLEPHI FPNRSQLCVS AEQSEGHWKV KNCEERLFYI 500
    CKKAGHVLSD AESGCQEGWE RHGGFCYKID TVLRSFDQAS SGYYCPPALV 550
    TITNRFEQAF ITSLISSVVK MKDSYFWIAL QDQNDTGEYT WKPVGQKPEP 600
    VQYTHWNTHQ PRYSGGCVAM RGRHPLGRWE VKHCRHFKAM SLCKQPVENQ 650
    EKAEYEERWP FHPCYLDWES EPGLASCFKV FHSEKVLMKR TWREAEAFCE 700
    EFGAHLASFA HIEEENFVNE LLHSKFNWTE ERQFWIGFNK RNPLNAGSWE 750
    WSDRTPVVSS FLDNTYFGED ARNCAVYKAN KTLLPLHCGS KREWICKIPR 800
    DVKPKIPFWY QYDVPWLFYQ DAEYLFHTFA SEWLNFEFVC SWLHSDLLTI 850
    HSAHEQEFIH SKIKALSKYG ASWWIGLQEE RANDEFRWRD GTPVIYQNWD 900
    TGRERTVNNQ SQRCGFISSI TGLWGSEECS VSMPSICKRK KVWLIEKKKD 950
    TPKQHGTCPK GWLYFNYKCL LLNIPKDPSS WKNWTHAQHF CAEEGGTLVA 1000
    IESEVEQAFI TMNLFGQTTS VWIGLQNDDY ETWLNGKPVV YSNWSPFDII 1050
    NIPSHNTTEV QKHIPLCALL SSNPNFHFTG KWYFEDCGKE GYGFVCEKMQ 1100
    DTSGHGVNTS DMYPMPNTLE YGNRTYKIIN ANMTWYAAIK TCLMHKAQLV 1150
    SITDQYHQSF LTVVLNRLGY AHWIGLFTTD NGLNFDWSDG TKSSFTFWKD 1200
    EESSLLGDCV FADSNGRWHS TACESFLQGA ICHVPPETRQ SEHPELCSET 1250
    SIPWIKFKSN CYSFSTVLDS MSFEAAHEFC KKEGSNLLTI KDEAENAFLL 1300
    EELFAFGSSV QMVWLNAQFD GNNETIKWFD GTPTDQSNWG IRKPDTDYFK 1350
    PHHCVALRIP EGLWQLSPCQ EKKGFICKME ADIHTAEALP EKGPSHSIIP 1400
    LAVVLTLIVI VAICTLSFCI YKHNGGFFRR LAGFRNPYYP ATNFSTVYLE 1450
    ENILISDLEK SDQ 1463
    Length:1,463
    Mass (Da):168,600
    Last modified:November 13, 2007 - v2
    Checksum:i4E65EA5AC5D597E2
    GO
    Isoform 2 (identifier: Q13018-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1323-1324: NE → SK
         1325-1463: Missing.

    Show »
    Length:1,324
    Mass (Da):152,805
    Checksum:iE00D5FDFF05DC9FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 173APR → GAA in AAA70110. (PubMed:7721806)Curated
    Sequence conflicti15 – 173APR → GAA in AAC50163. (PubMed:7721806)Curated
    Sequence conflicti62 – 643ENC → GRTGS in AAA70110. (PubMed:7721806)Curated
    Sequence conflicti62 – 643ENC → GRTGS in AAC50163. (PubMed:7721806)Curated
    Sequence conflicti521 – 5233RHG → ETC in AAA70110. (PubMed:7721806)Curated
    Sequence conflicti521 – 5233RHG → ETC in AAC50163. (PubMed:7721806)Curated
    Sequence conflicti724 – 7241S → P in AAA70110. (PubMed:7721806)Curated
    Sequence conflicti724 – 7241S → P in AAC50163. (PubMed:7721806)Curated
    Sequence conflicti779 – 7791A → P in AAA70110. (PubMed:7721806)Curated
    Sequence conflicti779 – 7791A → P in AAC50163. (PubMed:7721806)Curated
    Sequence conflicti1224 – 12241E → D in AAA70110. (PubMed:7721806)Curated
    Sequence conflicti1224 – 12241E → D in AAC50163. (PubMed:7721806)Curated
    Sequence conflicti1263 – 12631S → K in AAA70110. (PubMed:7721806)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti142 – 1421R → Q.
    Corresponds to variant rs12327936 [ dbSNP | Ensembl ].
    VAR_037203
    Natural varianti177 – 1771P → S.
    Corresponds to variant rs13394676 [ dbSNP | Ensembl ].
    VAR_037204
    Natural varianti279 – 2791I → V.
    Corresponds to variant rs965290 [ dbSNP | Ensembl ].
    VAR_037205
    Natural varianti292 – 2921M → V.1 Publication
    Corresponds to variant rs3749117 [ dbSNP | Ensembl ].
    VAR_037206
    Natural varianti300 – 3001H → D.1 Publication
    Corresponds to variant rs35771982 [ dbSNP | Ensembl ].
    VAR_037207
    Natural varianti370 – 3701A → E.
    Corresponds to variant rs34916310 [ dbSNP | Ensembl ].
    VAR_061354
    Natural varianti404 – 4041R → H.
    Corresponds to variant rs33985939 [ dbSNP | Ensembl ].
    VAR_037208
    Natural varianti1106 – 11061G → S.
    Corresponds to variant rs3828323 [ dbSNP | Ensembl ].
    VAR_037209

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1323 – 13242NE → SK in isoform 2. 1 PublicationVSP_029493
    Alternative sequencei1325 – 1463139Missing in isoform 2. 1 PublicationVSP_029494Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17033 mRNA. Translation: AAA70110.1.
    U17034 mRNA. Translation: AAC50163.1.
    AC080166 Genomic DNA. Translation: AAY24052.1.
    AC093873 Genomic DNA. Translation: AAY24190.1.
    CH471058 Genomic DNA. Translation: EAX11392.1.
    CH471058 Genomic DNA. Translation: EAX11393.1.
    BC140823 mRNA. Translation: AAI40824.1.
    D30780 mRNA. Translation: BAA06444.1.
    CCDSiCCDS33309.1. [Q13018-1]
    CCDS42767.1. [Q13018-2]
    PIRiA56395.
    B56395.
    RefSeqiNP_001007268.1. NM_001007267.2. [Q13018-2]
    NP_001182570.1. NM_001195641.1.
    NP_031392.3. NM_007366.4. [Q13018-1]
    XP_005246449.1. XM_005246392.1. [Q13018-1]
    UniGeneiHs.410477.

    Genome annotation databases

    EnsembliENST00000283243; ENSP00000283243; ENSG00000153246. [Q13018-1]
    ENST00000392771; ENSP00000376524; ENSG00000153246. [Q13018-2]
    GeneIDi22925.
    KEGGihsa:22925.
    UCSCiuc002ube.2. human. [Q13018-1]
    uc002ubf.3. human. [Q13018-2]

    Polymorphism databases

    DMDMi160419241.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Phospholipase A2 receptor

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17033 mRNA. Translation: AAA70110.1 .
    U17034 mRNA. Translation: AAC50163.1 .
    AC080166 Genomic DNA. Translation: AAY24052.1 .
    AC093873 Genomic DNA. Translation: AAY24190.1 .
    CH471058 Genomic DNA. Translation: EAX11392.1 .
    CH471058 Genomic DNA. Translation: EAX11393.1 .
    BC140823 mRNA. Translation: AAI40824.1 .
    D30780 mRNA. Translation: BAA06444.1 .
    CCDSi CCDS33309.1. [Q13018-1 ]
    CCDS42767.1. [Q13018-2 ]
    PIRi A56395.
    B56395.
    RefSeqi NP_001007268.1. NM_001007267.2. [Q13018-2 ]
    NP_001182570.1. NM_001195641.1.
    NP_031392.3. NM_007366.4. [Q13018-1 ]
    XP_005246449.1. XM_005246392.1. [Q13018-1 ]
    UniGenei Hs.410477.

    3D structure databases

    ProteinModelPortali Q13018.
    SMRi Q13018. Positions 132-223, 229-355, 377-502, 664-805, 816-939, 957-1101, 1119-1232, 1254-1382.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000283243.

    Protein family/group databases

    MEROPSi S63.015.

    Polymorphism databases

    DMDMi 160419241.

    Proteomic databases

    PaxDbi Q13018.
    PRIDEi Q13018.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000283243 ; ENSP00000283243 ; ENSG00000153246 . [Q13018-1 ]
    ENST00000392771 ; ENSP00000376524 ; ENSG00000153246 . [Q13018-2 ]
    GeneIDi 22925.
    KEGGi hsa:22925.
    UCSCi uc002ube.2. human. [Q13018-1 ]
    uc002ubf.3. human. [Q13018-2 ]

    Organism-specific databases

    CTDi 22925.
    GeneCardsi GC02M160788.
    H-InvDB HIX0024010.
    HGNCi HGNC:9042. PLA2R1.
    HPAi HPA012657.
    MIMi 604939. gene.
    neXtProti NX_Q13018.
    PharmGKBi PA33369.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG288621.
    HOVERGENi HBG108261.
    InParanoidi Q13018.
    KOi K06560.
    OMAi WCATTSR.
    OrthoDBi EOG7FFMQR.
    PhylomeDBi Q13018.
    TreeFami TF316663.

    Miscellaneous databases

    ChiTaRSi PLA2R1. human.
    GenomeRNAii 22925.
    NextBioi 43633.
    PROi Q13018.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13018.
    CleanExi HS_PLA2R1.
    Genevestigatori Q13018.

    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. 3 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. "The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization."
      Ancian P., Lambeau G., Mattei M.-G., Lazdunski M.
      J. Biol. Chem. 270:8963-8970(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANTS VAL-292 AND ASP-300.
      Tissue: Kidney.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Brain.
    5. "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] OF 532-942, TISSUE SPECIFICITY.
      Tissue: Placenta.
    6. "Distribution of the phospholipase A2 receptor messenger RNA in human gestational tissues."
      Moses E.K., Freed K.A., Brennecke S.P., Rice G.E.
      Placenta 19:35-40(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Activation of cytokine production by secreted phospholipase A2 in human lung macrophages expressing the M-type receptor."
      Granata F., Petraroli A., Boilard E., Bezzine S., Bollinger J., Del Vecchio L., Gelb M.H., Lambeau G., Marone G., Triggiani M.
      J. Immunol. 174:464-474(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPLA2R_HUMAN
    AccessioniPrimary (citable) accession number: Q13018
    Secondary accession number(s): B2RTU9
    , D3DPB1, Q13019, Q15095, Q53R45, Q53RR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3