P47712 (PA24A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytosolic phospholipase A2
Short name=cPLA2

Alternative name(s):
Phospholipase A2 group IVA

Including the following 2 domains:

1. Phospholipase A2
   EC=3.1.1.4
   Alternative name(s):
   Phosphatidylcholine 2-acylhydrolase
2. Lysophospholipase
   EC=3.1.1.5

Gene names

Name:	PLA2G4A
Synonyms:	CPLA2, PLA2G4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	749 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. Ref.8 Ref.9 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate. Ref.8 Ref.9
Enzyme regulation	Stimulated by agonists such as ATP, EGF, thrombin and bradykinin as well as by cytosolic Ca2+.
Subunit structure	Interacts with KAT5. Ref.11
Subcellular location	Cytoplasm. Cytoplasmic vesicle. Note: Translocates to membrane vesicles in a calcium-dependent fashion. Ref.8 Ref.20
Tissue specificity	Expressed in various tissues such as macrophages, platelets, neutrophils, fibroblasts and lung endothelium.
Domain	The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca2+. Ref.19 Ref.20
Post-translational modification	Activated by phosphorylation at both Ser-505 and Ser-727.
Sequence similarities	Contains 1 C2 domain. Contains 1 PLA2c domain.
Biophysicochemical properties	Kinetic parameters: Vmax=2.7 µmol/min/mg enzyme for the phospholipase A2 reaction Ref.7 Vmax=4.6 µmol/min/mg enzyme for the lysophosphatase reaction

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Cytoplasm Cytoplasmic vesicle
Coding sequence diversity	Polymorphism
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	arachidonic acid secretion Inferred from electronic annotation. Source: Compara cardiolipin acyl-chain remodeling Traceable author statement. Source: Reactome cellular response to antibiotic Inferred from electronic annotation. Source: Compara icosanoid biosynthetic process Inferred from electronic annotation. Source: Compara icosanoid metabolic process Non-traceable author statement Ref.19. Source: UniProtKB phosphatidic acid biosynthetic process Traceable author statement. Source: Reactome 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 catabolic process Inferred from electronic annotation. Source: InterPro platelet activating factor biosynthetic process Non-traceable author statement Ref.19. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome regulation of cell proliferation Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Non-traceable author statement Ref.6. Source: UniProtKB endoplasmic reticulum membrane Traceable author statement. Source: Reactome mitochondrial inner membrane Traceable author statement. Source: Reactome
Molecular_function	calcium ion binding Inferred from direct assay Ref.19Ref.20. Source: UniProtKB calcium-dependent phospholipid binding Inferred from direct assay Ref.20. Source: UniProtKB lysophospholipase activity Inferred from electronic annotation. Source: EC phospholipase A2 activity Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 749

749

Cytosolic phospholipase A2

PRO_0000187262

Regions

Domain

5 – 106

102

C2

Domain

140 – 740

601

PLA2c

Region

1 – 178

178

Phospholipid binding Probable

Sites

Active site

228

1

Nucleophile Ref.7 Ref.8 Ref.9 Ref.21

Active site

549

1

Proton acceptor Ref.7 Ref.8 Ref.9 Ref.21

Metal binding

40

1

Calcium 1

Metal binding

40

1

Calcium 2

Metal binding

41

1

Calcium 1; via carbonyl oxygen

Metal binding

43

1

Calcium 1

Metal binding

43

1

Calcium 2

Metal binding

65

1

Calcium 1

Metal binding

93

1

Calcium 2

Metal binding

94

1

Calcium 2; via carbonyl oxygen

Metal binding

95

1

Calcium 2

Amino acid modifications

Modified residue

268

1

Phosphothreonine Ref.15 Ref.16

Modified residue

437

1

Phosphoserine Ref.15 Ref.16 Ref.18

Modified residue

505

1

Phosphoserine; by MAPK Ref.6 Ref.10

Modified residue

727

1

Phosphoserine Ref.10 Ref.15

Modified residue

729

1

Phosphoserine Ref.13 Ref.15 Ref.16

Natural variations

Natural variant

103

1

G → R.
Corresponds to variant rs28395828 [ dbSNP | Ensembl ].

VAR_029276

Natural variant

224

1

V → I. Ref.3
Corresponds to variant rs12720588 [ dbSNP | Ensembl ].

VAR_018760

Natural variant

442

1

H → Q in a breast cancer sample; somatic mutation. Ref.22

VAR_035826

Natural variant

637

1

I → V.
Corresponds to variant rs28395831 [ dbSNP | Ensembl ].

VAR_062128

Natural variant

651

1

R → K. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs2307198 [ dbSNP | Ensembl ].

VAR_018424

Experimental info

Mutagenesis

139

1

C → A: No effect on phospholipase activity; when associated with A-141 and A-151. Ref.7

Mutagenesis

141

1

C → A: No effect on phospholipase activity; when associated with A-139 and A-151. Ref.7

Mutagenesis

151

1

C → A: No effect on phospholipase activity; when associated with A-139 and A-141. Ref.7

Mutagenesis

195

1

S → A: 5-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-577. Ref.7

Mutagenesis

200

1

R → A or H: Abolishes phospholipase activity. Ref.9

Mutagenesis

200

1

R → K: Reduces phospholipase activity 200-fold. Ref.9

Mutagenesis

215

1

S → A: No effect on phospholipase or lysophosphatase activity. Ref.7

Mutagenesis

220

1

C → A: No effect on phospholipase activity. Ref.7

Mutagenesis

228

1

S → A, C or T: Abolishes both phospholipase and lysophosphatase activities. Ref.7 Ref.8 Ref.9

Mutagenesis

324

1

C → A: No effect on phospholipase activity; when associated with A-331. Ref.7

Mutagenesis

331

1

C → A: No effect on phospholipase activity; when associated with A-324. Ref.7

Mutagenesis

505

1

S → A: Decreases agonist-stimulated release of arachidonic acid. Ref.6

Mutagenesis

549

1

D → A: Abolishes phospholipiase activity. Ref.9

Mutagenesis

549

1

D → E: Reduces phospholipiase activity 2000-fold. Ref.9

Mutagenesis

549

1

D → N: Reduces phospholipiase activity 300-fold. Ref.9

Mutagenesis

577

1

S → A: 7-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-195. Ref.7

Mutagenesis

620

1

C → A: No effect on phospholipase activity; when associated with A-634. Ref.7

Mutagenesis

634

1

C → A: No effect on phospholipase activity; when associated with A-620. Ref.7

Mutagenesis

726

1

C → A: No effect on phospholipase activity. Ref.7

Secondary structure

1

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749

Helix Strand Turn

Details...

Beta strand

18 – 29

12

Helix

34 – 39

6

Beta strand

44 – 49

6

Beta strand

51 – 54

4

Beta strand

57 – 60

4

Beta strand

70 – 79

10

Beta strand

86 – 93

8

Beta strand

96 – 98

3

Beta strand

100 – 108

9

Helix

109 – 111

3

Beta strand

117 – 124

8

Turn

125 – 127

3

Beta strand

128 – 137

10

Beta strand

143 – 146

4

Helix

152 – 177

26

Helix

179 – 181

3

Beta strand

190 – 194

5

Helix

198 – 214

17

Helix

218 – 220

3

Beta strand

221 – 226

6

Helix

228 – 239

12

Turn

241 – 245

5

Helix

248 – 260

13

Helix

263 – 266

4

Helix

269 – 284

16

Helix

291 – 304

14

Helix

305 – 307

3

Helix

313 – 318

6

Turn

319 – 321

3

Beta strand

326 – 333

8

Helix

341 – 343

3

Beta strand

344 – 349

6

Beta strand

354 – 356

3

Turn

357 – 360

4

Beta strand

361 – 363

3

Helix

365 – 367

3

Beta strand

370 – 373

4

Beta strand

376 – 379

4

Helix

386 – 393

8

Helix

396 – 399

4

Helix

401 – 404

4

Helix

417 – 423

7

Helix

426 – 429

4

Helix

463 – 476

14

Beta strand

488 – 490

3

Turn

492 – 495

4

Beta strand

543 – 548

6

Helix

550 – 552

3

Helix

558 – 561

4

Helix

564 – 566

3

Beta strand

570 – 575

6

Helix

588 – 599

12

Helix

611 – 615

5

Beta strand

619 – 623

5

Beta strand

636 – 641

6

Helix

646 – 648

3

Beta strand

650 – 652

3

Helix

660 – 666

7

Beta strand

670 – 672

3

Helix

687 – 702

16

Helix

705 – 718

14

Sequences

	Sequence		Length	Mass (Da)
	P47712 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: EE71CA0EBE617856	FASTA	749	85,239
	10 20 30 40 50 60 MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI STTPDSRKRT 70 80 90 100 110 120 RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE TLGTATFTVS SMKVGEKKEV 130 140 150 160 170 180 PFIFNQVTEM VLEMSLEVCS CPDLRFSMAL CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG 190 200 210 220 230 240 LHSARDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH 250 260 270 280 290 300 PDFPEKGPEE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG 310 320 330 340 350 360 ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG 370 380 390 400 410 420 TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QSRGSTMEEE 430 440 450 460 470 480 LENITTKHIV SNDSSDSDDE SHEPKGTENE DAGSDYQSDN QASWIHRMIM ALVSDSALFN 490 500 510 520 530 540 TREGRAGKVH NFMLGLNLNT SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV 550 560 570 580 590 600 KSKKIHVVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN 610 620 630 640 650 660 KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY RAPGVPRETE 670 680 690 700 710 720 EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN TLNNIDVIKE AMVESIEYRR 730 740 QNPSRCSVSL SNVEARRFFN KEFLSKPKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP." Clark J.D., Lin L.-L., Kriz R.W., Ramesha C.S., Sultzman L.A., Lin A.Y., Milona N., Knopf J.L. Cell 65:1043-1051(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT LYS-651.
[2]	"Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2." Sharp J., White D., Chiou G., Goodson T., Gamboa G., McClure D., Burgett S., Hoskins J., Skatrud P., Sportsman J., Becker G., Kang L., Roberts E., Kramer R. J. Biol. Chem. 266:14850-14853(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-651.
[3]	NIEHS SNPs program Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-224 AND LYS-651.
[4]	"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. , 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].
[5]	"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], VARIANT LYS-651.
[6]	"cPLA2 is phosphorylated and activated by MAP kinase." Lin L.-L., Wartmann M., Lin A.Y., Knopf J.L., Seth A., Davis R.J. Cell 72:269-278(1993) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-505, PHOSPHORYLATION AT SER-505.
[7]	"Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2." Sharp J.D., Pickard R.T., Chiou X.G., Manetta J.V., Kovacevic S., Miller J.R., Varshavsky A.D., Roberts E.F., Strifler B.A., Brems D.N., Kramer R.M. J. Biol. Chem. 269:23250-23254(1994) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE, MUTAGENESIS OF CYS-139; CYS-141; CYS-151; SER-195; SER-215; CYS-220; SER-228; CYS-324; CYS-331; SER-577; CYS-620; CYS-634 AND CYS-726, BIOPHYSICOCHEMICAL PROPERTIES.
[8]	"Functional identification of the active-site nucleophile of the human 85-kDa cytosolic phospholipase A2." Huang Z., Payette P., Abdullah K., Cromlish W.A., Kennedy B.P. Biochemistry 35:3712-3721(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVE SITE, MUTAGENESIS OF SER-228.
[9]	"Identification of essential residues for the catalytic function of 85-kDa cytosolic phospholipase A2. Probing the role of histidine, aspartic acid, cysteine, and arginine." Pickard R.T., Chiou X.G., Strifler B.A., DeFelippis M.R., Hyslop P.A., Tebbe A.L., Yee Y.K., Reynolds L.J., Dennis E.A., Kramer R.M., Sharp J.D. J. Biol. Chem. 271:19225-19231(1996) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-200; SER-228 AND ASP-549.
[10]	"Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells." Boersch-Haubold A.G., Bartoli F., Asselin J., Dudler T., Kramer R.M., Apitz-Castro R., Watson S.P., Gelb M.H. J. Biol. Chem. 273:4449-4458(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-505 AND SER-727.
[11]	"PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production." Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G., Taheri M.R., Bonventre J.V. Mol. Cell. Biol. 21:4470-4481(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KAT5.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-437; SER-727 AND SER-729, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-437 AND SER-729, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, MASS SPECTROMETRY.
[19]	"Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2." Perisic O., Fong S., Lynch D.E., Bycroft M., Williams R.L. J. Biol. Chem. 273:1596-1604(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 16-141 IN COMPLEX WITH CALCIUM IONS, DOMAIN.
[20]	"Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2." Xu G.-Y., McDonagh T., Yu H.-A., Nalefski E.A., Clark J.D., Cumming D.A. J. Mol. Biol. 280:485-500(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-138 IN COMPLEX WITH CALCIUM IONS, DOMAIN, SUBCELLULAR LOCATION.
[21]	"Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism." Dessen A., Tang J., Schmidt H., Stahl M., Clark J.D., Seehra J., Somers W.S. Cell 97:349-360(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, ACTIVE SITE.
[22]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-442.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M72393 mRNA. Translation: AAB00789.1.
M68874 mRNA. Translation: AAA60105.1.
AY552098 Genomic DNA. Translation: AAS45712.1.
AL022147 Genomic DNA. Translation: CAB42689.2.
AL049797, AL022147 Genomic DNA. Translation: CAI22252.1.
BC114340 mRNA. Translation: AAI14341.1.

IPI

IPI00026108.

PIR

A39329.

RefSeq

NP_077734.1. NM_024420.2.

UniGene

Hs.497200.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BCI	NMR	-	A	1-138	[»]
1CJY	X-ray	2.50	A/B	1-749	[»]
1RLW	X-ray	2.40	A	17-138	[»]

ProteinModelPortal

P47712.

SMR

P47712. Positions 13-721.

ModBase

Search...

Protein-protein interaction databases

IntAct

P47712. 1 interaction.

STRING

9606.ENSP00000356436.

PTM databases

PhosphoSite

P47712.

Polymorphism databases

DMDM

1352707.

Proteomic databases

PaxDb

P47712.

PRIDE

P47712.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367466; ENSP00000356436; ENSG00000116711.

GeneID

5321.

KEGG

hsa:5321.

UCSC

uc001gsc.3. human.

Organism-specific databases

CTD

5321.

GeneCards

GC01P186798.

HGNC

HGNC:9035. PLA2G4A.

HPA

CAB010050.

MIM

600522. gene.

neXtProt

NX_P47712.

PharmGKB

PA271.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG257248.

HOGENOM

HOG000115420.

HOVERGEN

HBG053479.

InParanoid

P47712.

KO

K16342.

OMA

ETLIHNR.

OrthoDB

EOG4Z62MZ.

PhylomeDB

P47712.

Enzyme and pathway databases

BRENDA

3.1.1.4. 2681.

Pathway_Interaction_DB

endothelinpathway. Endothelins.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P47712.

Bgee

P47712.

CleanEx

HS_PLA2G4A.

Genevestigator

P47712.

GermOnline

ENSG00000116711. Homo sapiens.

Family and domain databases

InterPro

IPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]

Pfam

PF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]

SMART

SM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]

SUPFAM

SSF52151. Acyl_Trfase/lysoPlipase. 1 hit.
SSF49562. C2_CaLB. 1 hit.

PROSITE

PS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P47712.

ChEMBL

CHEMBL3816.

DrugBank

DB00180. Flunisolide.
DB00591. Fluocinolone Acetonide.
DB01047. Fluocinonide.
DB00324. Fluorometholone.
DB00846. Flurandrenolide.
DB00588. Fluticasone Propionate.
DB00253. Medrysone.
DB01103. Quinacrine.

EvolutionaryTrace

P47712.

GenomeRNAi

5321.

NextBio

20586.

PMAP-CutDB

P47712.

SOURCE

Search...

Entry information

Entry name

PA24A_HUMAN

Accession

Primary (citable) accession number: P47712
Secondary accession number(s): B1AKG4, Q29R80

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 11, 2011
Last modified:	April 3, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.