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P14555 (PA2GA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipase A2, membrane associated

EC=3.1.1.4
Alternative name(s):
GIIC sPLA2
Group IIA phospholipase A2
Non-pancreatic secretory phospholipase A2
Short name=NPS-PLA2
Phosphatidylcholine 2-acylhydrolase 2A
Gene names
Name:PLA2G2A
Synonyms:PLA2B, PLA2L, RASF-A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length144 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit.

Subcellular location

Membrane; Peripheral membrane protein.

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.

Sequence similarities

Belongs to the phospholipase A2 family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to Gram-positive bacterium

Traceable author statement PubMed 18827909. Source: BHF-UCL

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

low-density lipoprotein particle remodeling

Traceable author statement PubMed 18827909. Source: BHF-UCL

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phosphatidic acid metabolic process

Inferred from direct assay PubMed 9032461. Source: BHF-UCL

phosphatidylcholine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylethanolamine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylglycerol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylinositol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylserine acyl-chain remodeling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Inferred from direct assay PubMed 17069818. Source: BHF-UCL

positive regulation of inflammatory response

Traceable author statement PubMed 18827909. Source: BHF-UCL

positive regulation of macrophage derived foam cell differentiation

Traceable author statement PubMed 18827909. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Inferred from direct assay. Source: LIFEdb

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 17069818. Source: BHF-UCL

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipase A2 activity

Traceable author statement PubMed 9272153. Source: UniProtKB

phospholipase A2 activity

Inferred from direct assay PubMed 17069818. Source: BHF-UCL

phospholipid binding

Inferred from direct assay PubMed 9032461. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.11 Ref.12 Ref.13 Ref.14
Chain21 – 144124Phospholipase A2, membrane associated
PRO_0000022750

Sites

Active site671 By similarity
Active site1111 By similarity
Metal binding471Calcium; via carbonyl oxygen
Metal binding491Calcium; via carbonyl oxygen
Metal binding511Calcium; via carbonyl oxygen
Metal binding681Calcium

Amino acid modifications

Disulfide bond46 ↔ 137
Disulfide bond48 ↔ 64
Disulfide bond63 ↔ 117
Disulfide bond69 ↔ 144
Disulfide bond70 ↔ 110
Disulfide bond79 ↔ 103
Disulfide bond97 ↔ 108

Natural variations

Natural variant191H → Y. Ref.6
Corresponds to variant rs11573162 [ dbSNP | Ensembl ].
VAR_018953

Experimental info

Sequence conflict121I → Y in AAT73043. Ref.4

Secondary structure

......................... 144
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14555 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 923C5FA0C6979CDA

FASTA14416,083
        10         20         30         40         50         60 
MKTLLLLAVI MIFGLLQAHG NLVNFHRMIK LTTGKEAALS YGFYGCHCGV GGRGSPKDAT 

        70         80         90        100        110        120 
DRCCVTHDCC YKRLEKRGCG TKFLSYKFSN SGSRITCAKQ DSCRSQLCEC DKAAATCFAR 

       130        140 
NKTTYNKKYQ YYSNKHCRGS TPRC 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid."
Seilhamer J.J., Pruzanski W., Vadas P., Plant S., Miller J.A., Kloss J., Johnson L.K.
J. Biol. Chem. 264:5335-5338(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Rheumatoid arthritic synovial fluid.
[2]"Structure and properties of a human non-pancreatic phospholipase A2."
Kramer R.M., Hession C., Johansen B., Hayes G., McGray P., Chow E.P., Tizard R., Pepinsky R.B.
J. Biol. Chem. 264:5768-5775(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structure and properties of a secretable phospholipase A2 from human platelets."
Kramer R.M., Johansen B., Hession C., Pepinsky R.B.
Adv. Exp. Med. Biol. 275:35-53(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning and sequence determination of human platelet phospholipase A2 from liver tissues."
Liang N.S., Fang Z.W., Li Y., Yang F., Lu Y., Xie Y.A.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]NIEHS SNPs program
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-19.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[8]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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].
Tissue: Prostate.
[11]"The primary structure of a membrane-associated phospholipase A2 from human spleen."
Kanda A., Ono T., Yoshida N., Tojo H., Okamoto M.
Biochem. Biophys. Res. Commun. 163:42-48(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-144.
Tissue: Spleen.
[12]"Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid."
Hara S., Kudo I., Matsuta K., Miyamoto T., Inoue K.
J. Biochem. 104:326-328(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-54.
Tissue: Synovial fluid.
[13]"Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme."
Lai C.Y., Wada K.
Biochem. Biophys. Res. Commun. 157:488-493(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-33.
Tissue: Synovial fluid.
[14]"Purification and characterization of a phospholipase A2 from human ileal mucosa."
Minami T., Tojo H., Shinomura Y., Matsuzawa Y., Okamoto M.
Biochim. Biophys. Acta 1170:125-130(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-75.
Tissue: Ileal mucosa.
[15]"Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2-A resolution."
Wery J.-P., Schevitz R.W., Clawson D.K., Bobbitt J.L., Dow E.R., Gamboa G., Goodson T. Jr., Hermann R.B., Kramer R.M., McClure D.B., Mihelich E.D., Putnam J.E., Sharp J.D., Stark D.H., Teater C., Warrick M.W., Jones N.D.
Nature 352:79-82(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[16]"Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate."
Scott D.L., White S.P., Browning J.L., Rosa J.J., Gelb M.H., Sigler P.B.
Science 254:1007-1010(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[17]"Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2."
Schevitz R.W., Bach N.J., Carlson D.G., Chirgadze N.Y., Clawson D.K., Dillard R.D., Draheim S.E., Hartley L.W., Jones N.D., Mihelich E.D., Olkowski J.L., Snyder D.W., Dand S.C., Wery J.-P.
Nat. Struct. Biol. 2:458-465(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[18]"Crystal structure of human secretory phospholipase A2-IIA complex with the potent indolizine inhibitor 120-1032."
Kitadokoro K., Hagishita S., Sato T., Ohtan M., Miki K.
J. Biochem. 123:619-623(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22430 mRNA. Translation: AAA36550.1.
M22431 Genomic DNA. Translation: AAA36549.1.
AY656695 mRNA. Translation: AAT73043.1.
CR456865 mRNA. Translation: CAG33146.1.
AY462114 Genomic DNA. Translation: AAR16084.1.
AL358253 Genomic DNA. Translation: CAH74017.1.
AK291302 mRNA. Translation: BAF83991.1.
CH471134 Genomic DNA. Translation: EAW94907.1.
BC005919 mRNA. Translation: AAH05919.1.
CCDSCCDS201.1.
PIRPSHUYF. A32862.
RefSeqNP_000291.1. NM_000300.3.
NP_001155199.1. NM_001161727.1.
NP_001155200.1. NM_001161728.1.
NP_001155201.1. NM_001161729.1.
UniGeneHs.466804.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYPX-ray2.57A/B/C/D/E/F21-144[»]
1BBCX-ray2.20A21-144[»]
1DB4X-ray2.20A21-144[»]
1DB5X-ray2.80A21-144[»]
1DCYX-ray2.70A21-144[»]
1J1AX-ray2.20A/B21-144[»]
1KQUX-ray2.10A21-144[»]
1KVOX-ray2.00A/B/C/D/E/F21-144[»]
1N28X-ray1.50A/B21-144[»]
1N29X-ray2.60A21-144[»]
1PODX-ray2.10A21-144[»]
1POEX-ray2.10A/B21-144[»]
2GNYmodel-A21-144[»]
3U8BX-ray2.30A21-144[»]
3U8DX-ray1.80A/B21-144[»]
3U8HX-ray2.30A/B21-144[»]
3U8IX-ray1.10A/B21-144[»]
ProteinModelPortalP14555.
SMRP14555. Positions 21-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111337. 20 interactions.
IntActP14555. 3 interactions.
MINTMINT-1206447.
STRING9606.ENSP00000364252.

Chemistry

BindingDBP14555.
ChEMBLCHEMBL3474.
GuidetoPHARMACOLOGY1417.

PTM databases

PhosphoSiteP14555.

Polymorphism databases

DMDM129483.

Proteomic databases

PaxDbP14555.
PeptideAtlasP14555.
PRIDEP14555.

Protocols and materials databases

DNASU5320.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375111; ENSP00000364252; ENSG00000188257.
ENST00000400520; ENSP00000383364; ENSG00000188257.
GeneID5320.
KEGGhsa:5320.
UCSCuc001bcu.3. human.

Organism-specific databases

CTD5320.
GeneCardsGC01M020301.
HGNCHGNC:9031. PLA2G2A.
HPAHPA015236.
MIM172411. gene.
neXtProtNX_P14555.
PharmGKBPA270.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271943.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidP14555.
KOK01047.
OMAFNNDELN.
OrthoDBEOG7N63PF.
PhylomeDBP14555.
TreeFamTF319283.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP14555.
CleanExHS_PLA2G2A.
GenevestigatorP14555.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERPTHR11716. PTHR11716. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. SSF48619. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLA2G2A. human.
EvolutionaryTraceP14555.
GeneWikiPLA2G2A.
GenomeRNAi5320.
NextBio20582.
PROP14555.
SOURCESearch...

Entry information

Entry namePA2GA_HUMAN
AccessionPrimary (citable) accession number: P14555
Secondary accession number(s): A8K5I7 expand/collapse secondary AC list , Q6DN24, Q6IBD9, Q9UCD2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM