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Q13018

- PLA2R_HUMAN

UniProt

Q13018 - PLA2R_HUMAN

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Protein

Secretory phospholipase A2 receptor

Gene

PLA2R1

Organism
Homo sapiens (Human)
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 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: 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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 13971377ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1398 – 141821HelicalSequence AnalysisAdd
BLAST
Topological domaini1419 – 146345CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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...

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.
GeneTreeiENSGT00720000108514.
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

        10         20         30         40         50
MLLSPSLLLL LLLGAPRGCA EGVAAALTPE RLLEWQDKGI FVIQSESLKK
60 70 80 90 100
CIQAGKSVLT LENCKQANKH MLWKWVSNHG LFNIGGSGCL GLNFSAPEQP
110 120 130 140 150
LSLYECDSTL VSLRWRCNRK MITGPLQYSV QVAHDNTVVA SRKYIHKWIS
160 170 180 190 200
YGSGGGDICE YLHKDLHTIK GNTHGMPCMF PFQYNHQWHH ECTREGREDD
210 220 230 240 250
LLWCATTSRY ERDEKWGFCP DPTSAEVGCD TIWEKDLNSH ICYQFNLLSS
260 270 280 290 300
LSWSEAHSSC QMQGGTLLSI TDETEENFIR EHMSSKTVEV WMGLNQLDEH
310 320 330 340 350
AGWQWSDGTP LNYLNWSPEV NFEPFVEDHC GTFSSFMPSA WRSRDCESTL
360 370 380 390 400
PYICKKYLNH IDHEIVEKDA WKYYATHCEP GWNPYNRNCY KLQKEEKTWH
410 420 430 440 450
EALRSCQADN SALIDITSLA EVEFLVTLLG DENASETWIG LSSNKIPVSF
460 470 480 490 500
EWSNDSSVIF TNWHTLEPHI FPNRSQLCVS AEQSEGHWKV KNCEERLFYI
510 520 530 540 550
CKKAGHVLSD AESGCQEGWE RHGGFCYKID TVLRSFDQAS SGYYCPPALV
560 570 580 590 600
TITNRFEQAF ITSLISSVVK MKDSYFWIAL QDQNDTGEYT WKPVGQKPEP
610 620 630 640 650
VQYTHWNTHQ PRYSGGCVAM RGRHPLGRWE VKHCRHFKAM SLCKQPVENQ
660 670 680 690 700
EKAEYEERWP FHPCYLDWES EPGLASCFKV FHSEKVLMKR TWREAEAFCE
710 720 730 740 750
EFGAHLASFA HIEEENFVNE LLHSKFNWTE ERQFWIGFNK RNPLNAGSWE
760 770 780 790 800
WSDRTPVVSS FLDNTYFGED ARNCAVYKAN KTLLPLHCGS KREWICKIPR
810 820 830 840 850
DVKPKIPFWY QYDVPWLFYQ DAEYLFHTFA SEWLNFEFVC SWLHSDLLTI
860 870 880 890 900
HSAHEQEFIH SKIKALSKYG ASWWIGLQEE RANDEFRWRD GTPVIYQNWD
910 920 930 940 950
TGRERTVNNQ SQRCGFISSI TGLWGSEECS VSMPSICKRK KVWLIEKKKD
960 970 980 990 1000
TPKQHGTCPK GWLYFNYKCL LLNIPKDPSS WKNWTHAQHF CAEEGGTLVA
1010 1020 1030 1040 1050
IESEVEQAFI TMNLFGQTTS VWIGLQNDDY ETWLNGKPVV YSNWSPFDII
1060 1070 1080 1090 1100
NIPSHNTTEV QKHIPLCALL SSNPNFHFTG KWYFEDCGKE GYGFVCEKMQ
1110 1120 1130 1140 1150
DTSGHGVNTS DMYPMPNTLE YGNRTYKIIN ANMTWYAAIK TCLMHKAQLV
1160 1170 1180 1190 1200
SITDQYHQSF LTVVLNRLGY AHWIGLFTTD NGLNFDWSDG TKSSFTFWKD
1210 1220 1230 1240 1250
EESSLLGDCV FADSNGRWHS TACESFLQGA ICHVPPETRQ SEHPELCSET
1260 1270 1280 1290 1300
SIPWIKFKSN CYSFSTVLDS MSFEAAHEFC KKEGSNLLTI KDEAENAFLL
1310 1320 1330 1340 1350
EELFAFGSSV QMVWLNAQFD GNNETIKWFD GTPTDQSNWG IRKPDTDYFK
1360 1370 1380 1390 1400
PHHCVALRIP EGLWQLSPCQ EKKGFICKME ADIHTAEALP EKGPSHSIIP
1410 1420 1430 1440 1450
LAVVLTLIVI VAICTLSFCI YKHNGGFFRR LAGFRNPYYP ATNFSTVYLE
1460
ENILISDLEK SDQ
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00720000108514.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 116 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