Q9UNK4 (PA2GD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	145 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Molecular_function	calcium 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 145	125	Group IID secretory phospholipase A2		PRO_0000022755
Sites
	Active site	67	1	By similarity
	Active site	112	1	By similarity
	Metal binding	47	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	49	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	51	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	68	1	Calcium By similarity
Amino acid modifications
	Glycosylation	89	1	N-linked (GlcNAc...) Potential
	Disulfide bond	46 ↔ 138		By similarity
	Disulfide bond	48 ↔ 64		By similarity
	Disulfide bond	63 ↔ 118		By similarity
	Disulfide bond	69 ↔ 145		By similarity
	Disulfide bond	70 ↔ 111		By similarity
	Disulfide bond	79 ↔ 104		By similarity
	Disulfide bond	97 ↔ 109		By similarity
Natural variations
	Natural variant	65	1	Q → H. Ref.4		VAR_055387
	Natural variant	73	1	H → R. Ref.4		VAR_055388
	Natural variant	80	1	S → G. Ref.1 Ref.3 Ref.4 Corresponds to variant rs584367 [ dbSNP | Ensembl ].		VAR_012741
	Natural variant	96	1	H → R. Ref.4		VAR_055389
	Natural variant	121	1	R → C. Ref.4		VAR_055390
	Natural variant	121	1	R → L. Ref.4		VAR_055391

Sequences

	Sequence		Length	Mass (Da)
	Q9UNK4 [UniParc]. Last modified February 11, 2002. Version 2. Checksum: CF3A49DE516BD1EF	FASTA	145	16,546
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.
IPI	IPI00018259.
RefSeq	NP_001258743.1. NM_001271814.1. NP_036532.1. NM_012400.3.
UniGene	Hs.189507.
3D structure databases
ProteinModelPortal	Q9UNK4.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000364246.
PTM databases
PhosphoSite	Q9UNK4.
Polymorphism databases
DMDM	20139286.
Proteomic databases
PaxDb	Q9UNK4.
PRIDE	Q9UNK4.
Protocols and materials databases
DNASU	26279.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375105; ENSP00000364246; ENSG00000117215.
GeneID	26279.
KEGG	hsa:26279.
UCSC	uc001bcz.3. human.
Organism-specific databases
CTD	26279.
GeneCards	GC01M020438.
HGNC	HGNC:9033. PLA2G2D.
HPA	HPA046308.
MIM	605630. gene.
neXtProt	NX_Q9UNK4.
PharmGKB	PA33363.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG290941.
HOGENOM	HOG000231749.
HOVERGEN	HBG008137.
InParanoid	Q9UNK4.
KO	K01047.
OMA	CACDKEV.
OrthoDB	EOG4N04G9.
PhylomeDB	Q9UNK4.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	Q9UNK4.
CleanEx	HS_PLA2G2D.
Genevestigator	Q9UNK4.
GermOnline	ENSG00000117215. Homo sapiens.
Family and domain databases
Gene3D	1.20.90.10. 1 hit.
InterPro	IPR001211. PLipase_A2. IPR013090. PLipase_A2_AS. IPR016090. PLipase_A2_dom. [Graphical view]
PANTHER	PTHR11716. PTHR11716. 1 hit.
Pfam	PF00068. Phospholip_A2_1. 1 hit. [Graphical view]
PRINTS	PR00389. PHPHLIPASEA2.
SMART	SM00085. PA2c. 1 hit. [Graphical view]
SUPFAM	SSF48619. PhospholipaseA2. 1 hit.
PROSITE	PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UNK4.
ChEMBL	CHEMBL4281.
GenomeRNAi	26279.
NextBio	48597.
SOURCE	Search...

Entry information

Entry name

PA2GD_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.