PSS_YEAST
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 03-AUG-2022, entry version 197.
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}.
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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; 55.
DR DIP; DIP-5331N; -.
DR IntAct; P08456; 7.
DR MINT; P08456; -.
DR STRING; 4932.YER026C; -.
DR CarbonylDB; P08456; -.
DR iPTMnet; P08456; -.
DR PaxDb; P08456; -.
DR PRIDE; P08456; -.
DR DNASU; 856748; -.
DR EnsemblFungi; YER026C_mRNA; YER026C; YER026C.
DR GeneID; 856748; -.
DR KEGG; sce:YER026C; -.
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; CGMISKS; -.
DR BioCyc; YEAST:YER026C-MON; -.
DR BRENDA; 2.7.8.8; 984.
DR UniPathway; UPA00558; UER00615.
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:0016021; C:integral component of 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 Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000852; Phosphatidylserine_synth_fun; 1.
DR TIGRFAMs; TIGR00473; pssA; 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
