PGPS1_MOUSE
ID PGPS1_MOUSE Reviewed; 553 AA.
AC Q8BHF7; Q8QZT9; Q8R4R7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial;
DE EC=2.7.8.5;
DE AltName: Full=Phosphatidylglycerophosphate synthase 1;
DE Short=PGP synthase 1;
DE AltName: Full=Silencer-associated factor;
DE Flags: Precursor;
GN Name=Pgs1; Synonyms=Saf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Embryonic stem cell, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-553.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Siu G., Arsov I.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-553.
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9880566; DOI=10.1074/jbc.274.3.1828;
RA Kawasaki K., Kuge O., Chang S.-C., Heacock P.N., Rho M., Suzuki K.,
RA Nishijima M., Dowhan W.;
RT "Isolation of a chinese hamster ovary (CHO) cDNA encoding
RT phosphatidylglycerophosphate (PGP) synthase, expression of which corrects
RT the mitochondrial abnormalities of a PGP synthase-defective mutant of CHO-
RT K1 cells.";
RL J. Biol. Chem. 274:1828-1834(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC phosphatidylglycerol and cardiolipin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC -!- ACTIVITY REGULATION: Activated by calcium and magnesium and inhibited
CC by other bivalent cations. {ECO:0000250}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in testis,
CC liver and brain. {ECO:0000269|PubMed:9880566}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22918.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL87040.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AK046174; BAC32619.1; -; mRNA.
DR EMBL; AK049359; BAC33708.1; -; mRNA.
DR EMBL; AK053905; BAC35584.1; -; mRNA.
DR EMBL; AL591433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF411101; AAL87040.1; ALT_SEQ; mRNA.
DR EMBL; BC022918; AAH22918.1; ALT_INIT; mRNA.
DR CCDS; CCDS25698.1; -.
DR RefSeq; NP_598518.1; NM_133757.2.
DR AlphaFoldDB; Q8BHF7; -.
DR SMR; Q8BHF7; -.
DR STRING; 10090.ENSMUSP00000121973; -.
DR iPTMnet; Q8BHF7; -.
DR PhosphoSitePlus; Q8BHF7; -.
DR EPD; Q8BHF7; -.
DR MaxQB; Q8BHF7; -.
DR PaxDb; Q8BHF7; -.
DR PRIDE; Q8BHF7; -.
DR ProteomicsDB; 287921; -.
DR Antibodypedia; 9930; 167 antibodies from 23 providers.
DR DNASU; 74451; -.
DR Ensembl; ENSMUST00000132676; ENSMUSP00000121973; ENSMUSG00000017715.
DR GeneID; 74451; -.
DR KEGG; mmu:74451; -.
DR UCSC; uc007moj.1; mouse.
DR CTD; 9489; -.
DR MGI; MGI:1921701; Pgs1.
DR VEuPathDB; HostDB:ENSMUSG00000017715; -.
DR eggNOG; KOG3964; Eukaryota.
DR GeneTree; ENSGT00390000002373; -.
DR HOGENOM; CLU_030471_1_2_1; -.
DR InParanoid; Q8BHF7; -.
DR OMA; YLSTLYI; -.
DR OrthoDB; 1358866at2759; -.
DR PhylomeDB; Q8BHF7; -.
DR TreeFam; TF314768; -.
DR UniPathway; UPA00084; UER00503.
DR BioGRID-ORCS; 74451; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Pgs1; mouse.
DR PRO; PR:Q8BHF7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BHF7; protein.
DR Bgee; ENSMUSG00000017715; Expressed in primary oocyte and 254 other tissues.
DR ExpressionAtlas; Q8BHF7; baseline and differential.
DR Genevisible; Q8BHF7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:BHF-UCL.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS:HGNC-UCL.
DR InterPro; IPR016270; PGS1.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586; PTHR12586; 1.
DR PROSITE; PS50035; PLD; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..553
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase, mitochondrial"
FT /id="PRO_0000337107"
FT DOMAIN 212..238
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 457..490
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 371
FT /note="T -> M (in Ref. 4; AAH22918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 62489 MW; 23373FEE4E47CD46 CRC64;
MAAPAAGPVF WRRLLGLLPG RPGLAALLGR LSDRLGRSRE RRRRRSPWLL LAPLLSPTVP
QVTSPPCCLC PEGVHRFQWI RNLVPEFGVS SSHVRVLSSP AEFFELMKGQ IKIAKRRVVM
ASLYLGTGPL EQELVDCLES SLEKSLQAKF PSDLKVSILL DFTRGSRGRK NSRTMLLPLL
QRFPERVRVS LFHTPNLRGL LRLLIPERFN ETIGLQHIKV YLFDNNVILS GANLSDSYFT
NRQDRYVFLQ DCAEIADFFT ELVDAVGDVS LQLQGDDTVE VVDGMVHPYK GDRAAYCRAA
NKRVMDVIHS ARARQQMLHA QTFHSDSLLS QEEAAAAGDR RPAPDTWIYP LIQMKPFEIQ
IDEIVTETLL TEAERGAKVF LTTGYFNLTQ AYMDLVLGTR AEYQILLASP EVNGFFGAKG
VAGAIPAAYV HIERQFYSEV CSLGQQDRVQ LQEYWRRGWT FHAKGLWLYL AGSSLPCLTL
IGSPNFGYRS VHRDLEAQIA IVTESRSLQQ QLHQEQEQLY LRSGVVTSAT FEQPGRQVKL
WVKMVTPLIK NFF
