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Q62028

- PLA2R_MOUSE

UniProt

Q62028 - PLA2R_MOUSE

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Protein

Secretory phospholipase A2 receptor

Gene

Pla2r1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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: UniProtKB-KW
  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
Complete GO annotation...

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. extracellular region Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB
  4. receptor complex Source: MGI
Complete GO annotation...

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, 517-613, 664-798, 816-1096, 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

        10         20         30         40         50
MVQWLAMLQL LWLQQLLLLG IHQGIAQDLT HIQEPSLEWR DKGIFIIQSE
60 70 80 90 100
SLKTCIQAGK SVLTLENCKQ PNEHMLWKWV SDDHLFNVGG SGCLGLNISA
110 120 130 140 150
LEQPLKLYEC DSTLISLRWH CDRKMIEGPL QYKVQVKSDN TVVARKQIHR
160 170 180 190 200
WIAYTSSGGD ICEHPSRDLY TLKGNAHGMP CVFPFQFKGH WHHDCIREGQ
210 220 230 240 250
KEHLLWCATT SRYEEDEKWG FCPDPTSMKV FCDATWQRNG SSRICYQFNL
260 270 280 290 300
LSSLSWNQAH SSCLMQGGAL LSIADEDEED FIRKHLSKVV KEVWIGLNQL
310 320 330 340 350
DEKAGWQWSD GTPLSYLNWS QEITPGPFVE HHCGTLEVVS AAWRSRDCES
360 370 380 390 400
TLPYICKRDL NHTAQGILEK DSWKYHATHC DPDWTPFNRK CYKLKKDRKS
410 420 430 440 450
WLGALHSCQS NDSVLMDVAS LAEVEFLVSL LRDENASETW IGLSSNKIPV
460 470 480 490 500
SFEWSSGSSV IFTNWYPLEP RILPNRRQLC VSAEESDGRW KVKDCKERLF
510 520 530 540 550
YICKKAGQVP ADEQSGCPAG WERHGRFCYK IDTVLRSFEE ASSGYYCSPA
560 570 580 590 600
LLTITSRFEQ AFITSLISSV AEKDSYFWIA LQDQNNTGEY TWKTVGQREP
610 620 630 640 650
VQYTYWNTRQ PSNRGGCVVV RGGSSLGRWE VKDCSDFKAM SLCKTPVKIW
660 670 680 690 700
EKTELEERWP FHPCYMDWES ATGLASCFKV FHSEKVLMKR SWREAEAFCE
710 720 730 740 750
EFGAHLASFA HIEEENFVNE LLHSKFNWTQ ERQFWIGFNR RNPLNAGSWA
760 770 780 790 800
WSDGSPVVSS FLDNAYFEED AKNCAVYKAN KTLLPSNCAS KHEWICRIPR
810 820 830 840 850
DVRPKFPDWY QYDAPWLFYQ NAEYLFHTHP AEWATFEFVC GWLRSDFLTI
860 870 880 890 900
YSAQEQEFIH SKIKGLTKYG VKWWIGLEEG GARDQIQWSN GSPVIFQNWD
910 920 930 940 950
KGREERVDSQ RKRCVFISSI TGLWGTENCS VPLPSICKRV KIWVIEKEKP
960 970 980 990 1000
PTQPGTCPKG WLYFNYKCFL VTIPKDPREL KTWTGAQEFC VAKGGTLVSI
1010 1020 1030 1040 1050
KSELEQAFIT MNLFGQTTNV WIGLQSTNHE KWVNGKPLVY SNWSPSDIIN
1060 1070 1080 1090 1100
IPSYNTTEFQ KHIPLCALMS SNPNFHFTGK WYFDDCGKEG YGFVCEKMQD
1110 1120 1130 1140 1150
TLEHHVNVSD TSAIPSTLEY GNRTYKIIRG NMTWYAAGKS CRMHRAELAS
1160 1170 1180 1190 1200
IPDAFHQAFL TVLLSRLGHT HWIGLSTTDN GQTFDWSDGT KSPFTYWKDE
1210 1220 1230 1240 1250
ESAFLGDCAF ADTNGRWHST ACESFLQGAI CHVVTETKAF EHPGLCSETS
1260 1270 1280 1290 1300
VPWIKFKGNC YSFSTVLDSR SFEDAHEFCK SEGSNLLAIR DAAENSFLLE
1310 1320 1330 1340 1350
ELLAFGSSVQ MVWLNAQFDN NNKTLRWFDG TPTEQSNWGL RKPDMDHLKP
1360 1370 1380 1390 1400
HPCVVLRIPE GIWHFTPCED KKGFICKMEA GIPAVTAQPE KGLSHSIVPV
1410 1420 1430 1440 1450
TVTLTLIIAL GIFMLCFWIY KQKSDIFQRL TGSRGSYYPT LNFSTAHLEE
1460 1470 1480
NILISDLEKN TNDEEVRDAP ATESKRGHKG RPICISP
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, 517-613, 664-798, 816-1096, 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

« Hide 'large scale' publications
  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 29, 2014
This is version 108 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