Q9Y7U3 (GEP4_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable phosphatidylglycerophosphatase, mitochondrial
EC=3.1.3.27

Alternative name(s):
PGP phosphatase

Gene names

Name:	gep4
ORF Names:	SPCC645.02

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Phosphatidylglycerophosphatase involved in the biosynthesis of cardiolipin (CL), a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes and which has important functions for cellular energy metabolism, mitochondrial dynamics and the initiation of apoptotic pathways By similarity.
Catalytic activity	Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.
Pathway	Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.3.
Sequence similarities	Belongs to the GEP4 family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiolipin biosynthetic process Inferred from sequence orthology. Source: PomBase mitochondrial membrane organization Inferred by curator. Source: PomBase
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial matrix Inferred from sequence orthology. Source: PomBase
Molecular_function	phosphatidylglycerophosphatase activity Inferred from sequence orthology. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 209	209	Probable phosphatidylglycerophosphatase, mitochondrial		PRO_0000351427
Regions
	Motif	57 – 61	5	Phosphoryl acceptor

Sequences

	Sequence		Length	Mass (Da)
	Q9Y7U3 [UniParc]. Last modified July 11, 2012. Version 2. Checksum: DD99C64B73CF1043	FASTA	209	23,992
	10 20 30 40 50 60 MLINIEGIQA FCQTIRNPRR IIPHATFPTF SQIPCNINYF LEQKFQVPVD IRALVLDKDN 70 80 90 100 110 120 CITLPNETTI AEAELKKIRE FQNIYGEKNV ILLSNSIGTR KLDPTGELAA HFQQKWNIPV 130 140 150 160 170 180 VRHSKLKPLC TEELYTYLSN NSHVSSASQI LFIGDRLLTD ITLANIMGSW GVWLTRGVGN 190 200 TTNMMMEVES WLYKRIHTQN PYIPTNRKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Comparative functional genomics of the fission yeasts." Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C. Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVISION OF GENE MODEL.
[3]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAB39898.2.
PIR	T41519.
RefSeq	NP_588111.2. NM_001023101.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPCC645.02-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC645.02.1; SPCC645.02.1:pep; SPCC645.02.
GeneID	2539038.
KEGG	spo:SPCC645.02.
Organism-specific databases
PomBase	SPCC645.02.
Phylogenomic databases
eggNOG	COG1011.
KO	K07025.
OrthoDB	EOG4BGD5F.
Enzyme and pathway databases
UniPathway	UPA00084; UER00504.
Family and domain databases
Gene3D	3.40.50.1000. 1 hit.
InterPro	IPR023214. HAD-like_dom. IPR006549. HAD-SF_hydro_IIIA. IPR010021. HAD-SF_ppase_IIIA. [Graphical view]
Pfam	PF09419. PGP_phosphatase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01662. HAD-SF-IIIA. 1 hit.
ProtoNet	Search...
Other
NextBio	20800212.

Entry information

Entry name

GEP4_SCHPO

Accession

Primary (citable) accession number: Q9Y7U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	July 11, 2012
Last modified:	May 1, 2013
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program