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Protein

Group IIF secretory phospholipase A2

Gene

PLA2G2F

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference.1 Publication

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation1 Publication

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Calcium; via carbonyl oxygenBy similarity
Metal bindingi49 – 491Calcium; via carbonyl oxygenBy similarity
Metal bindingi51 – 511Calcium; via carbonyl oxygenBy similarity
Active sitei67 – 671PROSITE-ProRule annotation
Metal bindingi68 – 681CalciumBy similarity
Active sitei114 – 1141PROSITE-ProRule annotation

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • phospholipase A2 activity Source: UniProtKB

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

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:
Group IIF secretory phospholipase A2 (EC:3.1.1.4)
Short name:
GIIF sPLA2
Short name:
sPLA2-IIF
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase 2F
Gene namesi
Name:PLA2G2F
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30040. PLA2G2F.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134931043.

Polymorphism and mutation databases

BioMutaiPLA2G2F.
DMDMi20139134.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 168148Group IIF secretory phospholipase A2PRO_0000022759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 138By similarity
Disulfide bondi48 ↔ 64By similarity
Disulfide bondi63 ↔ 120By similarity
Disulfide bondi69 ↔ 145By similarity
Disulfide bondi70 ↔ 113By similarity
Disulfide bondi79 ↔ 106By similarity
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi98 ↔ 111By similarity
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9BZM2.
PRIDEiQ9BZM2.

Expressioni

Tissue specificityi

Expressed at high levels in placenta, testis, thymus and at lower levels in heart, kidney, liver and prostate.1 Publication

Gene expression databases

BgeeiQ9BZM2.
CleanExiHS_PLA2G2F.
GenevisibleiQ9BZM2. HS.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000364243.

Structurei

3D structure databases

ProteinModelPortaliQ9BZM2.
SMRiQ9BZM2. Positions 21-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG296589.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiQ9BZM2.
KOiK01047.
OMAiLNETECD.
OrthoDBiEOG7N63PF.
PhylomeDBiQ9BZM2.
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.
PROSITEiPS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZM2-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKKFFTVAIL AGSVLSTAHG SLLNLKAMVE AVTGRSAILS FVGYGCYCGL
60 70 80 90 100
GGRGQPKDEV DWCCHAHDCC YQELFDQGCH PYVDHYDHTI ENNTEIVCSD
110 120 130 140 150
LNKTECDKQT CMCDKNMVLC LMNQTYREEY RGFLNVYCQG PTPNCSIYEP
160
PPEEVTCSHQ SPAPPAPP
Length:168
Mass (Da):18,658
Last modified:June 1, 2001 - v1
Checksum:i35B159298246A762
GO
Isoform 2 (identifier: Q9BZM2-2) [UniParc]FASTAAdd to basket

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

Show »
Length:211
Mass (Da):23,256
Checksum:i483B5E7850CB4248
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491E → G in BAC04210 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MADGAKANPKGFKKKVLDRC FSGWRGPRFGASCPSRTSRS SLGM in isoform 2. CuratedVSP_037524

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF306566 mRNA. Translation: AAG50242.1.
AK093645 mRNA. Translation: BAC04210.1.
AL158172, Z98257 Genomic DNA. Translation: CAI19658.1.
Z98257, AL158172 Genomic DNA. Translation: CAI20260.1.
CCDSiCCDS204.2. [Q9BZM2-2]
RefSeqiNP_073730.3. NM_022819.3. [Q9BZM2-2]
XP_011540258.1. XM_011541956.1. [Q9BZM2-2]
UniGeneiHs.302034.

Genome annotation databases

EnsembliENST00000375102; ENSP00000364243; ENSG00000158786. [Q9BZM2-2]
GeneIDi64600.
KEGGihsa:64600.
UCSCiuc009vpp.1. human. [Q9BZM2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF306566 mRNA. Translation: AAG50242.1.
AK093645 mRNA. Translation: BAC04210.1.
AL158172, Z98257 Genomic DNA. Translation: CAI19658.1.
Z98257, AL158172 Genomic DNA. Translation: CAI20260.1.
CCDSiCCDS204.2. [Q9BZM2-2]
RefSeqiNP_073730.3. NM_022819.3. [Q9BZM2-2]
XP_011540258.1. XM_011541956.1. [Q9BZM2-2]
UniGeneiHs.302034.

3D structure databases

ProteinModelPortaliQ9BZM2.
SMRiQ9BZM2. Positions 21-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000364243.

Chemistry

BindingDBiQ9BZM2.
ChEMBLiCHEMBL4278.

Polymorphism and mutation databases

BioMutaiPLA2G2F.
DMDMi20139134.

Proteomic databases

PaxDbiQ9BZM2.
PRIDEiQ9BZM2.

Protocols and materials databases

DNASUi64600.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375102; ENSP00000364243; ENSG00000158786. [Q9BZM2-2]
GeneIDi64600.
KEGGihsa:64600.
UCSCiuc009vpp.1. human. [Q9BZM2-2]

Organism-specific databases

CTDi64600.
GeneCardsiGC01P020465.
H-InvDBHIX0000212.
HGNCiHGNC:30040. PLA2G2F.
neXtProtiNX_Q9BZM2.
PharmGKBiPA134931043.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG296589.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiQ9BZM2.
KOiK01047.
OMAiLNETECD.
OrthoDBiEOG7N63PF.
PhylomeDBiQ9BZM2.
TreeFamiTF319283.

Enzyme and pathway databases

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

GenomeRNAii64600.
NextBioi66565.
PROiQ9BZM2.

Gene expression databases

BgeeiQ9BZM2.
CleanExiHS_PLA2G2F.
GenevisibleiQ9BZM2. 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.
PROSITEiPS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].

Entry informationi

Entry nameiPA2GF_HUMAN
AccessioniPrimary (citable) accession number: Q9BZM2
Secondary accession number(s): Q5R385, Q8N217, Q9H506
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 121 of the entry and version 1 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. 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.