Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phospholipase A2, membrane associated

Gene

Pla2g2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481Calcium; via carbonyl oxygenBy similarity
Metal bindingi50 – 501Calcium; via carbonyl oxygenBy similarity
Metal bindingi52 – 521Calcium; via carbonyl oxygenBy similarity
Active sitei68 – 681By similarity
Metal bindingi69 – 691CalciumBy similarity
Active sitei113 – 1131By similarity

GO - Molecular functioni

  • calcium-dependent phospholipase A2 activity Source: RGD
  • calcium ion binding Source: InterPro
  • phospholipase A2 activity Source: RGD
  • phospholipid binding Source: Ensembl

GO - Biological processi

  • lipid catabolic process Source: RGD
  • phosphatidic acid metabolic process Source: Ensembl
  • phospholipid metabolic process Source: RGD
  • positive regulation of ERK1 and ERK2 cascade Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-1482788. Acyl chain remodelling of PC.
R-RNO-1482801. Acyl chain remodelling of PS.
R-RNO-1482839. Acyl chain remodelling of PE.
R-RNO-1482922. Acyl chain remodelling of PI.
R-RNO-1482925. Acyl chain remodelling of PG.
R-RNO-1483166. Synthesis of PA.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A2, membrane associated (EC:3.1.1.4)
Alternative name(s):
GIIC sPLA2
Group IIA phospholipase A2
Phosphatidylcholine 2-acylhydrolase 2A
Gene namesi
Name:Pla2g2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi620857. Pla2g2a.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extracellular space Source: Ensembl
  • membrane Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: RGD
  • secretory granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3686.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21214 PublicationsAdd
BLAST
Chaini22 – 146125Phospholipase A2, membrane associatedPRO_0000022752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 139By similarity
Disulfide bondi49 ↔ 65By similarity
Disulfide bondi64 ↔ 119By similarity
Disulfide bondi70 ↔ 146By similarity
Disulfide bondi71 ↔ 112By similarity
Disulfide bondi80 ↔ 105By similarity
Disulfide bondi98 ↔ 110By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP14423.
PRIDEiP14423.

Expressioni

Gene expression databases

GenevisibleiP14423. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022827.

Chemistry

BindingDBiP14423.

Structurei

3D structure databases

ProteinModelPortaliP14423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP14423.
KOiK01047.
OMAiKQDSCRS.
OrthoDBiEOG7N63PF.
PhylomeDBiP14423.
TreeFamiTF319283.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14423-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVLLLLAVV IMAFGSIQVQ GSLLEFGQMI LFKTGKRADV SYGFYGCHCG
60 70 80 90 100
VGGRGSPKDA TDWCCVTHDC CYNRLEKRGC GTKFLTYKFS YRGGQISCST
110 120 130 140
NQDSCRKQLC QCDKAAAECF ARNKKSYSLK YQFYPNKFCK GKTPSC
Length:146
Mass (Da):16,294
Last modified:February 1, 1991 - v2
Checksum:i60DDC9E79BF109F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221S → D AA sequence (PubMed:2722857).Curated
Sequence conflicti63 – 631W → E AA sequence (PubMed:3235451).Curated
Sequence conflicti69 – 691D → E AA sequence (PubMed:3235451).Curated
Sequence conflicti78 – 781R → S AA sequence (PubMed:3235451).Curated
Sequence conflicti85 – 851L → V in AAA41920 (PubMed:2764915).Curated
Sequence conflicti121 – 1211A → S AA sequence (PubMed:3235451).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti135 – 1351P → L Polymorphism.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00523 mRNA. Translation: BAA00410.1.
M37127 Genomic DNA. Translation: AAA41223.1.
M25148 mRNA. Translation: AAA41920.1.
X51529 Genomic DNA. Translation: CAA35909.1.
PIRiA33394.
A35493.
JU0283.
JX0052.
RefSeqiNP_113786.3. NM_031598.3.
XP_006239208.1. XM_006239146.2.
UniGeneiRn.11346.

Genome annotation databases

EnsembliENSRNOT00000022827; ENSRNOP00000022827; ENSRNOG00000016945.
GeneIDi29692.
KEGGirno:29692.
UCSCiRGD:620857. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00523 mRNA. Translation: BAA00410.1.
M37127 Genomic DNA. Translation: AAA41223.1.
M25148 mRNA. Translation: AAA41920.1.
X51529 Genomic DNA. Translation: CAA35909.1.
PIRiA33394.
A35493.
JU0283.
JX0052.
RefSeqiNP_113786.3. NM_031598.3.
XP_006239208.1. XM_006239146.2.
UniGeneiRn.11346.

3D structure databases

ProteinModelPortaliP14423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022827.

Chemistry

BindingDBiP14423.
ChEMBLiCHEMBL3686.

Proteomic databases

PaxDbiP14423.
PRIDEiP14423.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022827; ENSRNOP00000022827; ENSRNOG00000016945.
GeneIDi29692.
KEGGirno:29692.
UCSCiRGD:620857. rat.

Organism-specific databases

CTDi5320.
RGDi620857. Pla2g2a.

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP14423.
KOiK01047.
OMAiKQDSCRS.
OrthoDBiEOG7N63PF.
PhylomeDBiP14423.
TreeFamiTF319283.

Enzyme and pathway databases

ReactomeiR-RNO-1482788. Acyl chain remodelling of PC.
R-RNO-1482801. Acyl chain remodelling of PS.
R-RNO-1482839. Acyl chain remodelling of PE.
R-RNO-1482922. Acyl chain remodelling of PI.
R-RNO-1482925. Acyl chain remodelling of PG.
R-RNO-1483166. Synthesis of PA.

Miscellaneous databases

NextBioi610080.
PROiP14423.

Gene expression databases

GenevisibleiP14423. RN.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structure of cDNA coding for rat platelet phospholipase A2."
    Komada M., Kudo I., Mizushima H., Kitamura N., Inoue K.
    J. Biochem. 106:545-547(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Platelet.
  2. "Structure of gene coding for rat group II phospholipase A2."
    Komada M., Kudo I., Inoue K.
    Biochem. Biophys. Res. Commun. 168:1059-1065(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Spleen.
  3. "cDNA cloning and sequence determination of rat membrane-associated phospholipase A2."
    Ishizaki J., Ohara O., Nakamura E., Tamaki M., Ono T., Kanda A., Yoshida N., Teraoka H., Tojo H., Okamoto M.
    Biochem. Biophys. Res. Commun. 162:1030-1036(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Structure of genomic DNA for rat platelet phospholipase A2."
    Kusunoki C., Satoh S., Kobayashi M., Niwa M.
    Biochim. Biophys. Acta 1087:95-97(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  5. "The primary structure of rat platelet phospholipase A2."
    Hayakawa M., Kudo I., Tomita M., Nojima S., Inoue K.
    J. Biochem. 104:767-772(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-146.
    Strain: Wistar.
    Tissue: Platelet.
  6. "Purification and characterization of a membrane-associated phospholipase A2 from rat spleen. Its comparison with a cytosolic phospholipase A2 S-1."
    Ono T., Tojo H., Kuramitsu S., Kagamiyama H., Okamoto M.
    J. Biol. Chem. 263:5732-5738(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-57.
    Tissue: Spleen.
  7. "Amino acid composition and NH2-terminal amino acid sequence of rat platelet secretory phospholipase A2."
    Hayakawa M., Horigome K., Kudo I., Tomita M., Nojima S., Inoue K.
    J. Biochem. 101:1311-1314(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-46.
    Tissue: Platelet.
  8. "Immunoaffinity purification, partial sequence, and subcellular localization of rat liver phospholipase A2."
    Aarsman A.J., de Jong J.G.N., Arnoldussen E., Neys F.W., van Wassenaar P.D., van den Bosch H.
    J. Biol. Chem. 264:10008-10014(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-45.
    Tissue: Liver.

Entry informationi

Entry nameiPA2GA_RAT
AccessioniPrimary (citable) accession number: P14423
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1991
Last modified: May 11, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Group II phospholipase A2 is found in many cells and also extracellularly. The membrane-bound and secreted forms are identical and are encoded by a single gene.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.