SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UNK4

- PA2GD_HUMAN

UniProt

Q9UNK4 - PA2GD_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Group IID secretory phospholipase A2

Gene
PLA2G2D, SPLASH
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. L-alpha-1-palmitoyl-2-linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined.

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactori

Binds 1 calcium ion per subunit.

pH dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Calcium; via carbonyl oxygen By similarity
Metal bindingi49 – 491Calcium; via carbonyl oxygen By similarity
Metal bindingi51 – 511Calcium; via carbonyl oxygen By similarity
Active sitei67 – 671 By similarity
Metal bindingi68 – 681Calcium By similarity
Active sitei112 – 1121 By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. glycerophospholipid biosynthetic process Source: Reactome
  2. inflammatory response Source: ProtInc
  3. lipid catabolic process Source: UniProtKB-KW
  4. phosphatidic acid biosynthetic process Source: Reactome
  5. phosphatidylcholine acyl-chain remodeling Source: Reactome
  6. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
  7. phosphatidylglycerol acyl-chain remodeling Source: Reactome
  8. phosphatidylinositol acyl-chain remodeling Source: Reactome
  9. phosphatidylserine acyl-chain remodeling Source: Reactome
  10. phospholipid metabolic process Source: Reactome
  11. 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 IID secretory phospholipase A2 (EC:3.1.1.4)
Short name:
GIID sPLA2
Short name:
sPLA2-IID
Alternative name(s):
PLA2IID
Phosphatidylcholine 2-acylhydrolase 2D
Secretory-type PLA, stroma-associated homolog
Gene namesi
Name:PLA2G2D
Synonyms:SPLASH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9033. PLA2G2D.

Subcellular locationi

Secreted Reviewed prediction

GO - Cellular componenti

  1. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33363.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed predictionAdd
BLAST
Chaini21 – 145125Group IID secretory phospholipase A2PRO_0000022755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 138 By similarity
Disulfide bondi48 ↔ 64 By similarity
Disulfide bondi63 ↔ 118 By similarity
Disulfide bondi69 ↔ 145 By similarity
Disulfide bondi70 ↔ 111 By similarity
Disulfide bondi79 ↔ 104 By similarity
Glycosylationi89 – 891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi97 ↔ 109 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9UNK4.
PRIDEiQ9UNK4.

PTM databases

PhosphoSiteiQ9UNK4.

Expressioni

Tissue specificityi

Broadly expressed.

Gene expression databases

BgeeiQ9UNK4.
CleanExiHS_PLA2G2D.
GenevestigatoriQ9UNK4.

Organism-specific databases

HPAiHPA046308.

Interactioni

Protein-protein interaction databases

BioGridi117662. 1 interaction.
STRINGi9606.ENSP00000364246.

Structurei

3D structure databases

ProteinModelPortaliQ9UNK4.
SMRiQ9UNK4. Positions 22-126.

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG290941.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiQ9UNK4.
KOiK01047.
OMAiCDKEVAF.
OrthoDBiEOG7N63PF.
PhylomeDBiQ9UNK4.
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.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UNK4-1 [UniParc]FASTAAdd to Basket

« Hide

MELALLCGLV VMAGVIPIQG GILNLNKMVK QVTGKMPILS YWPYGCHCGL    50
GGRGQPKDAT DWCCQTHDCC YDHLKTQGCS IYKDYYRYNF SQGNIHCSDK 100
GSWCEQQLCA CDKEVAFCLK RNLDTYQKRL RFYWRPHCRG QTPGC 145
Length:145
Mass (Da):16,546
Last modified:February 11, 2002 - v2
Checksum:iCF3A49DE516BD1EF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651Q → H.1 Publication
Corresponds to variant rs62541890 [ dbSNP | Ensembl ].
VAR_055387
Natural varianti73 – 731H → R.1 Publication
Corresponds to variant rs62541891 [ dbSNP | Ensembl ].
VAR_055388
Natural varianti80 – 801S → G.3 Publications
Corresponds to variant rs584367 [ dbSNP | Ensembl ].
VAR_012741
Natural varianti96 – 961H → R.1 Publication
Corresponds to variant rs62541892 [ dbSNP | Ensembl ].
VAR_055389
Natural varianti121 – 1211R → C.1 Publication
Corresponds to variant rs62541900 [ dbSNP | Ensembl ].
VAR_055390
Natural varianti121 – 1211R → L.1 Publication
VAR_055391

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS203.1.
RefSeqiNP_001258743.1. NM_001271814.1.
NP_036532.1. NM_012400.3.
UniGeneiHs.189507.

Genome annotation databases

EnsembliENST00000375105; ENSP00000364246; ENSG00000117215.
GeneIDi26279.
KEGGihsa:26279.
UCSCiuc001bcz.4. human.

Polymorphism databases

DMDMi20139286.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS203.1.
RefSeqi NP_001258743.1. NM_001271814.1.
NP_036532.1. NM_012400.3.
UniGenei Hs.189507.

3D structure databases

ProteinModelPortali Q9UNK4.
SMRi Q9UNK4. Positions 22-126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117662. 1 interaction.
STRINGi 9606.ENSP00000364246.

Chemistry

BindingDBi Q9UNK4.
ChEMBLi CHEMBL4281.

PTM databases

PhosphoSitei Q9UNK4.

Polymorphism databases

DMDMi 20139286.

Proteomic databases

PaxDbi Q9UNK4.
PRIDEi Q9UNK4.

Protocols and materials databases

DNASUi 26279.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375105 ; ENSP00000364246 ; ENSG00000117215 .
GeneIDi 26279.
KEGGi hsa:26279.
UCSCi uc001bcz.4. human.

Organism-specific databases

CTDi 26279.
GeneCardsi GC01M020438.
HGNCi HGNC:9033. PLA2G2D.
HPAi HPA046308.
MIMi 605630. gene.
neXtProti NX_Q9UNK4.
PharmGKBi PA33363.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG290941.
HOGENOMi HOG000231749.
HOVERGENi HBG008137.
InParanoidi Q9UNK4.
KOi K01047.
OMAi CDKEVAF.
OrthoDBi EOG7N63PF.
PhylomeDBi Q9UNK4.
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

GeneWikii PLA2G2D.
GenomeRNAii 26279.
NextBioi 48597.
PROi Q9UNK4.
SOURCEi Search...

Gene expression databases

Bgeei Q9UNK4.
CleanExi HS_PLA2G2D.
Genevestigatori Q9UNK4.

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 PS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiPA2GD_HUMAN
AccessioniPrimary (citable) accession number: Q9UNK4
Secondary accession number(s): A8K2Z1, B1AEL9, Q9UK01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: February 11, 2002
Last modified: September 3, 2014
This is version 130 of the entry and version 2 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi