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Q9NZK7 (PA2GE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Group IIE secretory phospholipase A2

Short name=GIIE sPLA2
Short name=sPLA2-IIE
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase 2E
Gene names
Name:PLA2G2E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit.

Subcellular location

Secreted.

Tissue specificity

Restricted to the brain, heart, lung, and placenta.

Sequence similarities

Belongs to the phospholipase A2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 142123Group IIE secretory phospholipase A2
PRO_0000022757

Sites

Active site651 By similarity
Active site1091 By similarity
Metal binding451Calcium; via carbonyl oxygen By similarity
Metal binding471Calcium; via carbonyl oxygen By similarity
Metal binding491Calcium; via carbonyl oxygen By similarity
Metal binding661Calcium By similarity

Amino acid modifications

Disulfide bond44 ↔ 135 By similarity
Disulfide bond46 ↔ 62 By similarity
Disulfide bond61 ↔ 115 By similarity
Disulfide bond67 ↔ 142 By similarity
Disulfide bond68 ↔ 108 By similarity
Disulfide bond77 ↔ 101 By similarity
Disulfide bond95 ↔ 106 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9NZK7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3C360EA710E141FB

FASTA14215,989
        10         20         30         40         50         60 
MKSPHVLVFL CLLVALVTGN LVQFGVMIEK MTGKSALQYN DYGCYCGIGG SHWPVDQTDW 

        70         80         90        100        110        120 
CCHAHDCCYG RLEKLGCEPK LEKYLFSVSE RGIFCAGRTT CQRLTCECDK RAALCFRRNL 

       130        140 
GTYNRKYAHY PNKLCTGPTP PC 

« Hide

References

« Hide 'large scale' references
[1]"Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s."
Suzuki N., Ishizaki J., Yokota Y., Higashino K., Ono T., Ikeda M., Fujii N., Kawamoto K., Hanasaki K.
J. Biol. Chem. 275:5785-5793(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF189279 mRNA. Translation: AAF36541.1.
AL358253 Genomic DNA. Translation: CAH74016.1.
RefSeqNP_055404.1. NM_014589.2.
UniGeneHs.272372.

3D structure databases

ProteinModelPortalQ9NZK7.
SMRQ9NZK7. Positions 20-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000364257.

Chemistry

BindingDBQ9NZK7.
ChEMBLCHEMBL2154.

Polymorphism databases

DMDM20139240.

Proteomic databases

PaxDbQ9NZK7.
PRIDEQ9NZK7.

Protocols and materials databases

DNASU30814.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375116; ENSP00000364257; ENSG00000188784.
GeneID30814.
KEGGhsa:30814.
UCSCuc001bct.1. human.

Organism-specific databases

CTD30814.
GeneCardsGC01M020247.
HGNCHGNC:13414. PLA2G2E.
neXtProtNX_Q9NZK7.
PharmGKBPA134889019.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310124.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidQ9NZK7.
KOK01047.
OMAFGVMIER.
OrthoDBEOG7N63PF.
PhylomeDBQ9NZK7.
TreeFamTF319283.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

CleanExHS_PLA2G2E.
GenevestigatorQ9NZK7.

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.
PROSITEPS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi30814.
NextBio52870.
PROQ9NZK7.

Entry information

Entry namePA2GE_HUMAN
AccessionPrimary (citable) accession number: Q9NZK7
Secondary accession number(s): Q5VXJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 112 of the entry and version 1 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

Human chromosome 1

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