Q9NZK7 (PA2GE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	142 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inflammatory response Traceable author statement Ref.1. Source: ProtInc lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW 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
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phospholipase A2 activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 142	123	Group IIE secretory phospholipase A2		PRO_0000022757
Sites
	Active site	65	1	By similarity
	Active site	109	1	By similarity
	Metal binding	45	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	47	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	49	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	66	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	44 ↔ 135		By similarity
	Disulfide bond	46 ↔ 62		By similarity
	Disulfide bond	61 ↔ 115		By similarity
	Disulfide bond	67 ↔ 142		By similarity
	Disulfide bond	68 ↔ 108		By similarity
	Disulfide bond	77 ↔ 101		By similarity
	Disulfide bond	95 ↔ 106		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9NZK7 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 3C360EA710E141FB	FASTA	142	15,989
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00005553.
RefSeq	NP_055404.1. NM_014589.2.
UniGene	Hs.272372.
3D structure databases
ProteinModelPortal	Q9NZK7.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000364257.
Polymorphism databases
DMDM	20139240.
Proteomic databases
PaxDb	Q9NZK7.
PRIDE	Q9NZK7.
Protocols and materials databases
DNASU	30814.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375116; ENSP00000364257; ENSG00000188784.
GeneID	30814.
KEGG	hsa:30814.
UCSC	uc001bct.1. human.
Organism-specific databases
CTD	30814.
GeneCards	GC01M020247.
HGNC	HGNC:13414. PLA2G2E.
neXtProt	NX_Q9NZK7.
PharmGKB	PA134889019.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG310124.
HOGENOM	HOG000231749.
HOVERGEN	HBG008137.
InParanoid	Q9NZK7.
KO	K01047.
OMA	NKLCTGP.
OrthoDB	EOG44MXT9.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
CleanEx	HS_PLA2G2E.
Genevestigator	Q9NZK7.
GermOnline	ENSG00000188784. Homo sapiens.
Family and domain databases
Gene3D	1.20.90.10. 1 hit.
InterPro	IPR001211. PLipase_A2. IPR013090. PLipase_A2_AS. IPR016090. PLipase_A2_dom. [Graphical view]
PANTHER	PTHR11716. PTHR11716. 1 hit.
Pfam	PF00068. Phospholip_A2_1. 1 hit. [Graphical view]
PRINTS	PR00389. PHPHLIPASEA2.
SMART	SM00085. PA2c. 1 hit. [Graphical view]
SUPFAM	SSF48619. PhospholipaseA2. 1 hit.
PROSITE	PS00119. PA2_ASP. False negative. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9NZK7.
ChEMBL	CHEMBL2154.
GenomeRNAi	30814.
NextBio	52870.

Entry information

Entry name

PA2GE_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 105 of the entry and version 1 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.