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Q9BZM2 (PA2GF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length168 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. 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 processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

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

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functioncalcium 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 168148Group IIF secretory phospholipase A2
PRO_0000022759

Sites

Active site671 By similarity
Active site1141 By similarity
Metal binding471Calcium; via carbonyl oxygen By similarity
Metal binding491Calcium; via carbonyl oxygen By similarity
Metal binding511Calcium; via carbonyl oxygen By similarity
Metal binding681Calcium By similarity

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 138 By similarity
Disulfide bond48 ↔ 64 By similarity
Disulfide bond63 ↔ 120 By similarity
Disulfide bond69 ↔ 145 By similarity
Disulfide bond70 ↔ 113 By similarity
Disulfide bond79 ↔ 106 By similarity
Disulfide bond98 ↔ 111 By similarity

Natural variations

Alternative sequence11M → MADGAKANPKGFKKKVLDRC FSGWRGPRFGASCPSRTSRS SLGM in isoform 2.
VSP_037524

Experimental info

Sequence conflict1491E → G in BAC04210. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 35B159298246A762

FASTA16818,658
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 483B5E7850CB4248
Show »

FASTA21123,256

References

« Hide '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. expand/collapse author list , 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. 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
AF306566 mRNA. Translation: AAG50242.1.
AK093645 mRNA. Translation: BAC04210.1.
AL158172, Z98257 Genomic DNA. Translation: CAI19658.1.
Z98257, AL158172 Genomic DNA. Translation: CAI20260.1.
RefSeqNP_073730.3. NM_022819.3.
UniGeneHs.302034.

3D structure databases

ProteinModelPortalQ9BZM2.
SMRQ9BZM2. Positions 21-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000364243.

Chemistry

BindingDBQ9BZM2.
ChEMBLCHEMBL4278.

Polymorphism databases

DMDM20139134.

Proteomic databases

PaxDbQ9BZM2.
PRIDEQ9BZM2.

Protocols and materials databases

DNASU64600.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375102; ENSP00000364243; ENSG00000158786. [Q9BZM2-2]
GeneID64600.
KEGGhsa:64600.
UCSCuc009vpp.1. human. [Q9BZM2-2]

Organism-specific databases

CTD64600.
GeneCardsGC01P020465.
H-InvDBHIX0000212.
HGNCHGNC:30040. PLA2G2F.
neXtProtNX_Q9BZM2.
PharmGKBPA134931043.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296589.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidQ9BZM2.
KOK01047.
OMALNLKSMV.
OrthoDBEOG7N63PF.
PhylomeDBQ9BZM2.
TreeFamTF319283.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ9BZM2.
CleanExHS_PLA2G2F.
GenevestigatorQ9BZM2.

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

GenomeRNAi64600.
NextBio66565.
PROQ9BZM2.

Entry information

Entry namePA2GF_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 111 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