PGC1_SCHPO
ID PGC1_SCHPO Reviewed; 311 AA.
AC O14169;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Phosphatidylglycerol phospholipase C;
DE EC=3.1.4.-;
GN ORFNames=SPAC4D7.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- FUNCTION: Phosphatidylglycerol phospholipase required for the removal
CC of excess phosphatidylglycerol (PG) via a phospholipase C-type
CC degradation mechanism. {ECO:0000250|UniProtKB:Q08959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = a
CC 1,2-diacyl-sn-glycerol + H(+) + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:32927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57597, ChEBI:CHEBI:64716;
CC Evidence={ECO:0000250|UniProtKB:Q08959};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32928;
CC Evidence={ECO:0000250|UniProtKB:Q08959};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q08959}; Single-pass type IV membrane protein
CC {ECO:0000255}. Lipid droplet {ECO:0000250|UniProtKB:Q08959}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11274.2; -; Genomic_DNA.
DR PIR; T38793; T38793.
DR RefSeq; NP_594955.2; NM_001020386.2.
DR AlphaFoldDB; O14169; -.
DR SMR; O14169; -.
DR BioGRID; 280002; 7.
DR STRING; 4896.SPAC4D7.02c.1; -.
DR MaxQB; O14169; -.
DR PaxDb; O14169; -.
DR EnsemblFungi; SPAC4D7.02c.1; SPAC4D7.02c.1:pep; SPAC4D7.02c.
DR GeneID; 2543587; -.
DR KEGG; spo:SPAC4D7.02c; -.
DR PomBase; SPAC4D7.02c; -.
DR VEuPathDB; FungiDB:SPAC4D7.02c; -.
DR eggNOG; KOG2258; Eukaryota.
DR HOGENOM; CLU_030006_1_2_1; -.
DR InParanoid; O14169; -.
DR OMA; RRAHIGM; -.
DR PRO; PR:O14169; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0034479; F:phosphatidylglycerol phospholipase C activity; ISO:PomBase.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; ISO:PomBase.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Lipid droplet; Lipid metabolism; Membrane; Mitochondrion;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="Phosphatidylglycerol phospholipase C"
FT /id="PRO_0000116698"
FT TRANSMEM 289..310
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 32..272
FT /note="GP-PDE"
SQ SEQUENCE 311 AA; 35585 MW; 7A25079E767DDF6F CRC64;
MAFNYSIANT VDDAAQSIAE NTSSLATFSK PPLVIAHRGY KAKYPENTIL AFQQAVKAGA
DCVETDVRLT KDEVVCILHD RNLNRVFGVD VDVRDLDYEL DNGHFRTIQE PHEPLPTYEQ
FLHELTKHPG VNLLVDIKPV NDLLIIPRMV DAMLRVNSDL DFWKDKVSFC LWSHRFIPAC
DRYAPSIPLY HIGFNFAYAE RHFVMHPRVK GVSMAVALFL LPHSQDFVDL VHAQGKQVFA
WTLNTPSSIY LALIRGCDGL LSDDPVMARA LSQGPIVTKS WHYFHYSEWL HMIYGFLRAQ
FVFFLLRTFV L
