Q9BZM2 (PA2GF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Group IIF secretory phospholipase A2
Short name=GIIF sPLA2
Short name=sPLA2-IIF
EC=3.1.1.4

Alternative name(s):
Phosphatidylcholine 2-acylhydrolase 2F

Gene names

Name:

PLA2G2F

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	168 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. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference. Ref.1
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. Ref.1
Cofactor	Binds 1 calcium ion per subunit. Ref.1
Subcellular location	Secreted Ref.1.
Tissue specificity	Expressed at high levels in placenta, testis, thymus and at lower levels in heart, kidney, liver and prostate. Ref.1
Sequence similarities	Belongs to the phospholipase A2 family.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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	cytosol Traceable author statement. Source: Reactome extracellular region Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phospholipase A2 activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BZM2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9BZM2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADGAKANPKGFKKKVLDRCFSGWRGPRFGASCPSRTSRSSLGM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 168	148	Group IIF secretory phospholipase A2		PRO_0000022759
Sites
	Active site	67	1	By similarity
	Active site	114	1	By similarity
	Metal binding	47	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	49	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	51	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	68	1	Calcium By similarity
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	102	1	N-linked (GlcNAc...) Potential
	Glycosylation	123	1	N-linked (GlcNAc...) Potential
	Glycosylation	144	1	N-linked (GlcNAc...) Potential
	Disulfide bond	46 ↔ 138		By similarity
	Disulfide bond	48 ↔ 64		By similarity
	Disulfide bond	63 ↔ 120		By similarity
	Disulfide bond	69 ↔ 145		By similarity
	Disulfide bond	70 ↔ 113		By similarity
	Disulfide bond	79 ↔ 106		By similarity
	Disulfide bond	98 ↔ 111		By similarity
Natural variations
	Alternative sequence	1	1	M → MADGAKANPKGFKKKVLDRC FSGWRGPRFGASCPSRTSRS SLGM in isoform 2.		VSP_037524
Experimental info
	Sequence conflict	149	1	E → G in BAC04210. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 35B159298246A762	FASTA	168	18,658
	10 20 30 40 50 60 MKKFFTVAIL AGSVLSTAHG SLLNLKAMVE AVTGRSAILS FVGYGCYCGL GGRGQPKDEV 70 80 90 100 110 120 DWCCHAHDCC YQELFDQGCH PYVDHYDHTI ENNTEIVCSD LNKTECDKQT CMCDKNMVLC 130 140 150 160 LMNQTYREEY RGFLNVYCQG PTPNCSIYEP PPEEVTCSHQ SPAPPAPP
	Isoform 2 [UniParc]. Checksum: 483B5E7850CB4248	FASTA	211	23,256
	10 20 30 40 50 60 MADGAKANPK GFKKKVLDRC FSGWRGPRFG ASCPSRTSRS SLGMKKFFTV AILAGSVLST 70 80 90 100 110 120 AHGSLLNLKA MVEAVTGRSA ILSFVGYGCY CGLGGRGQPK DEVDWCCHAH DCCYQELFDQ 130 140 150 160 170 180 GCHPYVDHYD HTIENNTEIV CSDLNKTECD KQTCMCDKNM VLCLMNQTYR EEYRGFLNVY 190 200 210 CQGPTPNCSI YEPPPEEVTC SHQSPAPPAP P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and recombinant expression of human group IIF-secreted phospholipase A(2)." Valentin E., Singer A.G., Ghomashchi F., Lazdunski M., Gelb M.H., Lambeau G. Biochem. Biophys. Res. Commun. 279:223-228(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Fetal lung, Heart and Spleen.
[2]	"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] (ISOFORM 1). Tissue: Thymus.
[3]	"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	AF306566 mRNA. Translation: AAG50242.1. AK093645 mRNA. Translation: BAC04210.1. AL158172, Z98257 Genomic DNA. Translation: CAI19658.1. Z98257, AL158172 Genomic DNA. Translation: CAI20260.1.
IPI	IPI00010184. IPI00930096.
RefSeq	NP_073730.3. NM_022819.3.
UniGene	Hs.302034.
3D structure databases
ProteinModelPortal	Q9BZM2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000364243.
Polymorphism databases
DMDM	20139134.
Proteomic databases
PaxDb	Q9BZM2.
PRIDE	Q9BZM2.
Protocols and materials databases
DNASU	64600.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375102; ENSP00000364243; ENSG00000158786.
GeneID	64600.
KEGG	hsa:64600.
UCSC	uc009vpp.1. human.
Organism-specific databases
CTD	64600.
GeneCards	GC01P020465.
H-InvDB	HIX0000212.
HGNC	HGNC:30040. PLA2G2F.
neXtProt	NX_Q9BZM2.
PharmGKB	PA134931043.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG296589.
HOGENOM	HOG000231749.
HOVERGEN	HBG008137.
InParanoid	Q9BZM2.
KO	K01047.
OMA	LNLKSMV.
OrthoDB	EOG4933JS.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	Q9BZM2.
CleanEx	HS_PLA2G2F.
Genevestigator	Q9BZM2.
GermOnline	ENSG00000158786. 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	Q9BZM2.
ChEMBL	CHEMBL4278.
GenomeRNAi	64600.
NextBio	66565.

Entry information

Entry name

PA2GF_HUMAN

Accession

Primary (citable) accession number: Q9BZM2
Secondary accession number(s): Q5R385, Q8N217, Q9H506

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 11, 2002
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 103 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.