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Q9UNK4 (PA2GD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Group IID secretory phospholipase A2

Short name=GIID sPLA2
Short name=sPLA2-IID
EC=3.1.1.4
Alternative name(s):
PLA2IID
Phosphatidylcholine 2-acylhydrolase 2D
Secretory-type PLA, stroma-associated homolog
Gene names
Name:PLA2G2D
Synonyms:SPLASH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length145 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. L-alpha-1-palmitoyl-2-linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit.

Subcellular location

Secreted Potential.

Tissue specificity

Broadly expressed.

Sequence similarities

Belongs to the phospholipase A2 family.

Biophysicochemical properties

pH dependence:

Optimally active at neutral to alkaline pHs with 2 mM Ca2+.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   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

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

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

   Molecular_functioncalcium 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 145125Group IID secretory phospholipase A2
PRO_0000022755

Sites

Active site671 By similarity
Active site1121 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

Glycosylation891N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 138 By similarity
Disulfide bond48 ↔ 64 By similarity
Disulfide bond63 ↔ 118 By similarity
Disulfide bond69 ↔ 145 By similarity
Disulfide bond70 ↔ 111 By similarity
Disulfide bond79 ↔ 104 By similarity
Disulfide bond97 ↔ 109 By similarity

Natural variations

Natural variant651Q → H. Ref.4
Corresponds to variant rs62541890 [ dbSNP | Ensembl ].
VAR_055387
Natural variant731H → R. Ref.4
Corresponds to variant rs62541891 [ dbSNP | Ensembl ].
VAR_055388
Natural variant801S → G. Ref.1 Ref.3 Ref.4
Corresponds to variant rs584367 [ dbSNP | Ensembl ].
VAR_012741
Natural variant961H → R. Ref.4
Corresponds to variant rs62541892 [ dbSNP | Ensembl ].
VAR_055389
Natural variant1211R → C. Ref.4
Corresponds to variant rs62541900 [ dbSNP | Ensembl ].
VAR_055390
Natural variant1211R → L. Ref.4
VAR_055391

Sequences

Sequence LengthMass (Da)Tools
Q9UNK4 [UniParc].

Last modified February 11, 2002. Version 2.
Checksum: CF3A49DE516BD1EF

FASTA14516,546
        10         20         30         40         50         60 
MELALLCGLV VMAGVIPIQG GILNLNKMVK QVTGKMPILS YWPYGCHCGL GGRGQPKDAT 

        70         80         90        100        110        120 
DWCCQTHDCC YDHLKTQGCS IYKDYYRYNF SQGNIHCSDK GSWCEQQLCA CDKEVAFCLK 

       130        140 
RNLDTYQKRL RFYWRPHCRG QTPGC 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of novel mouse and human secretory phospholipase A2s."
Ishizaki J., Suzuki N., Higashino K., Yokota Y., Ono T., Kawamoto K., Fujii N., Arita H., Hanasaki K.
J. Biol. Chem. 274:24973-24979(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-80, CHARACTERIZATION.
[2]"SPLASH (PLA(2)IID), a novel member of phospholipase A2 family, is associated with lymphotoxin-deficiency."
Shakhov A.N., Rubtsov A.V., Lyakhov I.G., Tumanov A.V., Nedospasov S.A.
Genes Immun. 1:191-199(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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], VARIANT GLY-80.
Tissue: Umbilical cord blood.
[4]NIEHS SNPs program
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-65; ARG-73; GLY-80; ARG-96; CYS-121 AND LEU-121.
[5]"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].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas and Spleen.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF112982 mRNA. Translation: AAD51390.1.
AF188625 mRNA. Translation: AAF09020.1.
AK290406 mRNA. Translation: BAF83095.1.
EU447440 Genomic DNA. Translation: ACA06110.1.
AL158172 Genomic DNA. Translation: CAC13159.1.
BC025706 mRNA. Translation: AAH25706.1.
CCDSCCDS203.1.
RefSeqNP_001258743.1. NM_001271814.1.
NP_036532.1. NM_012400.3.
UniGeneHs.189507.

3D structure databases

ProteinModelPortalQ9UNK4.
SMRQ9UNK4. Positions 22-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000364246.

Chemistry

BindingDBQ9UNK4.
ChEMBLCHEMBL4281.

PTM databases

PhosphoSiteQ9UNK4.

Polymorphism databases

DMDM20139286.

Proteomic databases

PaxDbQ9UNK4.
PRIDEQ9UNK4.

Protocols and materials databases

DNASU26279.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375105; ENSP00000364246; ENSG00000117215.
GeneID26279.
KEGGhsa:26279.
UCSCuc001bcz.4. human.

Organism-specific databases

CTD26279.
GeneCardsGC01M020438.
HGNCHGNC:9033. PLA2G2D.
HPAHPA046308.
MIM605630. gene.
neXtProtNX_Q9UNK4.
PharmGKBPA33363.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290941.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidQ9UNK4.
KOK01047.
OMACDKEVAF.
OrthoDBEOG7N63PF.
PhylomeDBQ9UNK4.
TreeFamTF319283.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ9UNK4.
CleanExHS_PLA2G2D.
GenevestigatorQ9UNK4.

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.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPLA2G2D.
GenomeRNAi26279.
NextBio48597.
PROQ9UNK4.
SOURCESearch...

Entry information

Entry namePA2GD_HUMAN
AccessionPrimary (citable) accession number: Q9UNK4
Secondary accession number(s): A8K2Z1, B1AEL9, Q9UK01
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: February 11, 2002
Last modified: July 9, 2014
This is version 129 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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