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Q9BZM2

- PA2GF_HUMAN

UniProt

Q9BZM2 - PA2GF_HUMAN

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Protein

Group IIF secretory phospholipase A2

Gene

PLA2G2F

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 PublicationPROSITE-ProRule annotation

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca(2+) 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

  1. calcium ion binding Source: InterPro
  2. phospholipase A2 activity Source: UniProtKB

GO - Biological processi

  1. glycerophospholipid biosynthetic process Source: Reactome
  2. lipid catabolic process Source: UniProtKB-KW
  3. phosphatidic acid biosynthetic process Source: Reactome
  4. phosphatidylcholine acyl-chain remodeling Source: Reactome
  5. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
  6. phosphatidylglycerol acyl-chain remodeling Source: Reactome
  7. phosphatidylinositol acyl-chain remodeling Source: Reactome
  8. phosphatidylserine acyl-chain remodeling Source: Reactome
  9. phospholipid metabolic process Source: Reactome
  10. small molecule metabolic process Source: Reactome
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: Chromosome 1

Organism-specific databases

HGNCiHGNC:30040. PLA2G2F.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134931043.

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.
GenevestigatoriQ9BZM2.

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.
OMAiLPMDEVD.
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. Align

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]
UniGeneiHs.302034.

Genome annotation databases

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

Polymorphism databases

DMDMi20139134.

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 .
CCDSi CCDS204.2. [Q9BZM2-2 ]
RefSeqi NP_073730.3. NM_022819.3. [Q9BZM2-2 ]
UniGenei Hs.302034.

3D structure databases

ProteinModelPortali Q9BZM2.
SMRi Q9BZM2. Positions 21-151.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000364243.

Chemistry

BindingDBi Q9BZM2.
ChEMBLi CHEMBL4278.

Polymorphism databases

DMDMi 20139134.

Proteomic databases

PaxDbi Q9BZM2.
PRIDEi Q9BZM2.

Protocols and materials databases

DNASUi 64600.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375102 ; ENSP00000364243 ; ENSG00000158786 . [Q9BZM2-2 ]
GeneIDi 64600.
KEGGi hsa:64600.
UCSCi uc009vpp.1. human. [Q9BZM2-2 ]

Organism-specific databases

CTDi 64600.
GeneCardsi GC01P020465.
H-InvDB HIX0000212.
HGNCi HGNC:30040. PLA2G2F.
neXtProti NX_Q9BZM2.
PharmGKBi PA134931043.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG296589.
GeneTreei ENSGT00760000119160.
HOGENOMi HOG000231749.
HOVERGENi HBG008137.
InParanoidi Q9BZM2.
KOi K01047.
OMAi LPMDEVD.
OrthoDBi EOG7N63PF.
PhylomeDBi Q9BZM2.
TreeFami TF319283.

Enzyme and pathway databases

Reactomei REACT_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

GenomeRNAii 64600.
NextBioi 66565.
PROi Q9BZM2.

Gene expression databases

Bgeei Q9BZM2.
CleanExi HS_PLA2G2F.
Genevestigatori Q9BZM2.

Family and domain databases

Gene3Di 1.20.90.10. 1 hit.
InterProi IPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view ]
PANTHERi PTHR11716. PTHR11716. 1 hit.
Pfami PF00068. Phospholip_A2_1. 1 hit.
[Graphical view ]
PRINTSi PR00389. PHPHLIPASEA2.
SMARTi SM00085. PA2c. 1 hit.
[Graphical view ]
SUPFAMi SSF48619. SSF48619. 1 hit.
PROSITEi PS00118. PA2_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 117 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