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Protein

Phospholipase A2, membrane associated

Gene

PLA2G2A

Organism
Homo sapiens (Human)
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+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Calcium; via carbonyl oxygen
Metal bindingi49 – 491Calcium; via carbonyl oxygen
Metal bindingi51 – 511Calcium; via carbonyl oxygen
Active sitei67 – 671By similarity
Metal bindingi68 – 681Calcium
Active sitei111 – 1111By similarity

GO - Molecular functioni

  • calcium-dependent phospholipase A2 activity Source: UniProtKB
  • calcium ion binding Source: InterPro
  • phospholipase A2 activity Source: BHF-UCL
  • phospholipid binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.4. 2681.
ReactomeiREACT_120722. Acyl chain remodelling of PI.
REACT_120829. Acyl chain remodelling of PC.
REACT_120906. Synthesis of PA.
REACT_121324. Acyl chain remodelling of PG.
REACT_121369. Acyl chain remodelling of PE.
REACT_121384. Acyl chain remodelling of PS.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PLA2G2A
Synonyms:PLA2B, PLA2L, RASF-A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9031. PLA2G2A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA270.

Chemistry

DrugBankiDB00586. Diclofenac.
DB01381. Ginkgo biloba.
DB00328. Indomethacin.
DB04786. Suramin.

Polymorphism and mutation databases

BioMutaiPLA2G2A.
DMDMi129483.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20204 PublicationsAdd
BLAST
Chaini21 – 144124Phospholipase A2, membrane associatedPRO_0000022750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 137
Disulfide bondi48 ↔ 64
Disulfide bondi63 ↔ 117
Disulfide bondi69 ↔ 144
Disulfide bondi70 ↔ 110
Disulfide bondi79 ↔ 103
Disulfide bondi97 ↔ 108

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP14555.
PeptideAtlasiP14555.
PRIDEiP14555.

PTM databases

PhosphoSiteiP14555.

Expressioni

Gene expression databases

BgeeiP14555.
CleanExiHS_PLA2G2A.
ExpressionAtlasiP14555. baseline and differential.
GenevisibleiP14555. HS.

Organism-specific databases

HPAiHPA015236.

Interactioni

Protein-protein interaction databases

BioGridi111337. 21 interactions.
IntActiP14555. 3 interactions.
MINTiMINT-1206447.
STRINGi9606.ENSP00000364252.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3312Combined sources
Helixi37 – 404Combined sources
Turni41 – 433Combined sources
Turni45 – 473Combined sources
Beta strandi48 – 503Combined sources
Helixi59 – 7618Combined sources
Beta strandi81 – 833Combined sources
Beta strandi88 – 914Combined sources
Beta strandi94 – 974Combined sources
Helixi102 – 12019Combined sources
Helixi122 – 1243Combined sources
Helixi127 – 1293Combined sources
Helixi134 – 1363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP14555.
SMRiP14555. Positions 21-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14555.

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG271943.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP14555.
KOiK01047.
OMAiKQDSCRS.
OrthoDBiEOG7N63PF.
PhylomeDBiP14555.
TreeFamiTF319283.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[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.

P14555-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLLLLAVI MIFGLLQAHG NLVNFHRMIK LTTGKEAALS YGFYGCHCGV
60 70 80 90 100
GGRGSPKDAT DRCCVTHDCC YKRLEKRGCG TKFLSYKFSN SGSRITCAKQ
110 120 130 140
DSCRSQLCEC DKAAATCFAR NKTTYNKKYQ YYSNKHCRGS TPRC
Length:144
Mass (Da):16,083
Last modified:April 1, 1990 - v2
Checksum:i923C5FA0C6979CDA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121I → Y in AAT73043 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191H → Y.1 Publication
Corresponds to variant rs11573162 [ dbSNP | Ensembl ].
VAR_018953

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS201.1.
PIRiA32862. PSHUYF.
RefSeqiNP_000291.1. NM_000300.3.
NP_001155199.1. NM_001161727.1.
NP_001155200.1. NM_001161728.1.
NP_001155201.1. NM_001161729.1.
UniGeneiHs.466804.

Genome annotation databases

EnsembliENST00000375111; ENSP00000364252; ENSG00000188257.
ENST00000400520; ENSP00000383364; ENSG00000188257.
GeneIDi5320.
KEGGihsa:5320.
UCSCiuc001bcu.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS201.1.
PIRiA32862. PSHUYF.
RefSeqiNP_000291.1. NM_000300.3.
NP_001155199.1. NM_001161727.1.
NP_001155200.1. NM_001161728.1.
NP_001155201.1. NM_001161729.1.
UniGeneiHs.466804.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP14555.
SMRiP14555. Positions 21-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111337. 21 interactions.
IntActiP14555. 3 interactions.
MINTiMINT-1206447.
STRINGi9606.ENSP00000364252.

Chemistry

BindingDBiP14555.
ChEMBLiCHEMBL3474.
DrugBankiDB00586. Diclofenac.
DB01381. Ginkgo biloba.
DB00328. Indomethacin.
DB04786. Suramin.
GuidetoPHARMACOLOGYi1417.

PTM databases

PhosphoSiteiP14555.

Polymorphism and mutation databases

BioMutaiPLA2G2A.
DMDMi129483.

Proteomic databases

PaxDbiP14555.
PeptideAtlasiP14555.
PRIDEiP14555.

Protocols and materials databases

DNASUi5320.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375111; ENSP00000364252; ENSG00000188257.
ENST00000400520; ENSP00000383364; ENSG00000188257.
GeneIDi5320.
KEGGihsa:5320.
UCSCiuc001bcu.3. human.

Organism-specific databases

CTDi5320.
GeneCardsiGC01M020301.
HGNCiHGNC:9031. PLA2G2A.
HPAiHPA015236.
MIMi172411. gene.
neXtProtiNX_P14555.
PharmGKBiPA270.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG271943.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP14555.
KOiK01047.
OMAiKQDSCRS.
OrthoDBiEOG7N63PF.
PhylomeDBiP14555.
TreeFamiTF319283.

Enzyme and pathway databases

BRENDAi3.1.1.4. 2681.
ReactomeiREACT_120722. Acyl chain remodelling of PI.
REACT_120829. Acyl chain remodelling of PC.
REACT_120906. Synthesis of PA.
REACT_121324. Acyl chain remodelling of PG.
REACT_121369. Acyl chain remodelling of PE.
REACT_121384. Acyl chain remodelling of PS.

Miscellaneous databases

ChiTaRSiPLA2G2A. human.
EvolutionaryTraceiP14555.
GeneWikiiPLA2G2A.
GenomeRNAii5320.
NextBioi20582.
PROiP14555.
SOURCEiSearch...

Gene expression databases

BgeeiP14555.
CleanExiHS_PLA2G2A.
ExpressionAtlasiP14555. baseline and differential.
GenevisibleiP14555. HS.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[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

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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).

Entry informationi

Entry nameiPA2GA_HUMAN
AccessioniPrimary (citable) accession number: P14555
Secondary accession number(s): A8K5I7
, Q6DN24, Q6IBD9, Q9UCD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 1, 1990
Last modified: July 22, 2015
This is version 178 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

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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.