ID PSS_YEAST Reviewed; 276 AA. AC P08456; D3DLS5; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 204. DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase; DE EC=2.7.8.8; DE AltName: Full=Phosphatidylserine synthase; GN Name=CHO1; Synonyms=PSS, PSS1; OrderedLocusNames=YER026C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3040403; DOI=10.1111/j.1432-1033.1987.tb13297.x; RA Nikawa J., Tsukagoschi Y., Kodaki T., Yamashita S.; RT "Nucleotide sequence and characterization of the yeast PSS gene encoding RT phosphatidylserine synthase."; RL Eur. J. Biochem. 167:7-12(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15. RX PubMed=2830250; DOI=10.1093/oxfordjournals.jbchem.a122147; RA Kiyono K., Miura K., Kushima Y., Hikiji T., Fukushima M., Shibuya I., RA Ohta A.; RT "Primary structure and product characterization of the Saccharomyces RT cerevisiae CHO1 gene that encodes phosphatidylserine synthase."; RL J. Biochem. 102:1089-1100(1987). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-34; SER-42; SER-46; RP SER-47 AND SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-34, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-34; SER-42; SER-46; RP SER-47 AND SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn- CC glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262, CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step CC 1/2. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. CC Endoplasmic reticulum membrane; Multi-pass membrane protein. CC Mitochondrion outer membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X05944; CAA29376.1; -; Genomic_DNA. DR EMBL; D00171; BAA00121.1; -; Genomic_DNA. DR EMBL; U18778; AAB64559.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07679.1; -; Genomic_DNA. DR PIR; S00080; S00080. DR RefSeq; NP_010943.3; NM_001178917.3. DR AlphaFoldDB; P08456; -. DR SMR; P08456; -. DR BioGRID; 36761; 58. DR DIP; DIP-5331N; -. DR IntAct; P08456; 7. DR MINT; P08456; -. DR STRING; 4932.YER026C; -. DR CarbonylDB; P08456; -. DR iPTMnet; P08456; -. DR PaxDb; 4932-YER026C; -. DR PeptideAtlas; P08456; -. DR DNASU; 856748; -. DR EnsemblFungi; YER026C_mRNA; YER026C; YER026C. DR GeneID; 856748; -. DR KEGG; sce:YER026C; -. DR AGR; SGD:S000000828; -. DR SGD; S000000828; CHO1. DR VEuPathDB; FungiDB:YER026C; -. DR eggNOG; ENOG502QPJG; Eukaryota. DR GeneTree; ENSGT00940000154169; -. DR HOGENOM; CLU_049944_5_0_1; -. DR InParanoid; P08456; -. DR OMA; HGCGMIS; -. DR OrthoDB; 1332156at2759; -. DR BioCyc; YEAST:YER026C-MONOMER; -. DR BRENDA; 2.7.8.8; 984. DR UniPathway; UPA00558; UER00615. DR BioGRID-ORCS; 856748; 8 hits in 10 CRISPR screens. DR PRO; PR:P08456; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P08456; Protein. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:SGD. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD. DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IDA:SGD. DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IDA:SGD. DR Gene3D; 1.20.120.1760; -; 1. DR InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase. DR InterPro; IPR016271; CDP-diaglyc--ser_O-PTrfase_fun. DR InterPro; IPR000462; CDP-OH_P_trans. DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom. DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS. DR NCBIfam; TIGR00473; pssA; 1. DR PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1. DR PANTHER; PTHR14269:SF61; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1. DR Pfam; PF01066; CDP-OH_P_transf; 1. DR PIRSF; PIRSF000852; Phosphatidylserine_synth_fun; 1. DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Endoplasmic reticulum; Lipid biosynthesis; KW Lipid metabolism; Membrane; Microsome; Mitochondrion; KW Mitochondrion outer membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2830250" FT CHAIN 2..276 FT /note="CDP-diacylglycerol--serine O- FT phosphatidyltransferase" FT /id="PRO_0000056801" FT TRANSMEM 82..102 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 163..183 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 210..230 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 248..268 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 42 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT CONFLICT 123 FT /note="G -> A (in Ref. 2; BAA00121)" FT /evidence="ECO:0000305" FT CONFLICT 191 FT /note="R -> T (in Ref. 2; BAA00121)" FT /evidence="ECO:0000305" FT CONFLICT 276 FT /note="P -> A (in Ref. 2; BAA00121)" FT /evidence="ECO:0000305" SQ SEQUENCE 276 AA; 30805 MW; E52B1FC836B67D24 CRC64; MVESDEDFAP QEFPHTDTDV IVNEHRDEND GYASDEVGGT LSRRASSIFS INTTPLAPPN ATDIQKFTSD EHHFSMMRNL HMADYITMLN GFSGFYSIVS CLRFTLTGKP HYVQRAHFFI LLGMCFDFLD GRVARLRNRS SLMGQELDSL ADLVSFGVAP AAIAFAIGFQ TTFDVMILSF FVLCGLARLA RFNVTVAQLP KDSSTGKSKY FEGLPMPTTL ALVLGMAYCV RKGLIFDNIP FGIFREDQIL EFHPIILVFF IHGCGMISKS LKIPKP //