GPC1_YEAST
ID GPC1_YEAST Reviewed; 432 AA.
AC P48236; D6VUT0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glycerophosphocholine acyltransferase 1 {ECO:0000303|PubMed:27758859};
DE Short=GPCAT {ECO:0000303|PubMed:27758859};
DE EC=2.3.1.- {ECO:0000269|PubMed:18430972, ECO:0000269|PubMed:27758859};
GN Name=GPC1 {ECO:0000303|PubMed:27758859}; OrderedLocusNames=YGR149W;
GN ORFNames=G6639;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8585325; DOI=10.1002/yea.320111410;
RA Skala J., Nawrocki A., Goffeau A.;
RT "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT NSR1 genes and ten new open reading frames.";
RL Yeast 11:1421-1427(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=12524434; DOI=10.1074/jbc.m300163200;
RA Kim H., Melen K., von Heijne G.;
RT "Topology models for 37 Saccharomyces cerevisiae membrane proteins based on
RT C-terminal reporter fusions and predictions.";
RL J. Biol. Chem. 278:10208-10213(2003).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=18430972; DOI=10.1194/jlr.m800129-jlr200;
RA Staalberg K., Neal A.C., Ronne H., Staahl U.;
RT "Identification of a novel GPCAT activity and a new pathway for
RT phosphatidylcholine biosynthesis in S. cerevisiae.";
RL J. Lipid Res. 49:1794-1806(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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).
RN [10]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=27758859; DOI=10.1074/jbc.m116.743062;
RA Glab B., Beganovic M., Anaokar S., Hao M.S., Rasmusson A.G.,
RA Patton-Vogt J., Banas A., Stymne S., Lager I.;
RT "Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and
RT plants: a novel enzyme in phosphatidylcholine synthesis.";
RL J. Biol. Chem. 291:25066-25076(2016).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30514764; DOI=10.1074/jbc.ra118.005232;
RA Anaokar S., Kodali R., Jonik B., Renne M.F., Brouwers J.F.H.M., Lager I.,
RA de Kroon A.I.P.M., Patton-Vogt J.;
RT "The glycerophosphocholine acyltransferase Gpc1 is part of a
RT phosphatidylcholine (PC)-remodeling pathway that alters PC species in
RT yeast.";
RL J. Biol. Chem. 294:1189-1201(2019).
CC -!- FUNCTION: Glycerophosphocholine acyltransferase (GPCAT) that utilizes
CC acyl-CoA to acylate glycero-3-phosphocholine (GPC), forming
CC lysophosphatidylcholine (LPC) (PubMed:18430972, PubMed:27758859). Shows
CC broad acyl specificities with a preference for 16:0-CoA,
CC polyunsaturated acyl-CoA, and the hydroxylated ricinoleoyl-CoA
CC (PubMed:18430972, PubMed:27758859). Catalyzes also the acylation of
CC glycero-3-phosphoethanolamine (GPE) with acyl-CoA (PubMed:27758859). In
CC addition to acyl-CoA, GPCAT efficiently utilizes LPC and
CC lysophosphatidylethanolamine (LPE) as acyl donors in the acylation of
CC GPC (PubMed:27758859). Contributes to the maintenance of
CC phosphatidylcholine (PC) homeostasis and might also have specific
CC functions in acyl editing of PC, such as transferring acyl groups
CC modified at the sn-2 position of PC to the sn-1 (PubMed:27758859).
CC Involved in postsynthetic PC remodeling that produces more saturated PC
CC species (PubMed:30514764). {ECO:0000269|PubMed:18430972,
CC ECO:0000269|PubMed:27758859, ECO:0000269|PubMed:30514764}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphocholine = a 1-acyl-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:58476,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:57287, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; Evidence={ECO:0000269|PubMed:18430972,
CC ECO:0000269|PubMed:27758859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycero-3-phosphoethanolamine = a monoacyl-
CC sn-glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:62108,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:67274,
CC ChEBI:CHEBI:143890; Evidence={ECO:0000269|PubMed:27758859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sn-glycero-3-phosphoethanolamine =
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:62104, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:143890, ChEBI:CHEBI:145434;
CC Evidence={ECO:0000269|PubMed:27758859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62105;
CC Evidence={ECO:0000305|PubMed:27758859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphocholine = CoA +
CC hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:56148,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64563; Evidence={ECO:0000269|PubMed:27758859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56149;
CC Evidence={ECO:0000305|PubMed:27758859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphocholine =
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:56152, ChEBI:CHEBI:16870, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:140444;
CC Evidence={ECO:0000269|PubMed:27758859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56153;
CC Evidence={ECO:0000305|PubMed:27758859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12R)-hydroxy-(9Z)-octadecenoyl-CoA + sn-glycerol 3-
CC phosphocholine = (12R-hydroxy-9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:56156, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:139559, ChEBI:CHEBI:140446;
CC Evidence={ECO:0000269|PubMed:27758859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56157;
CC Evidence={ECO:0000305|PubMed:27758859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + sn-glycerol 3-
CC phosphocholine = (9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:56164, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:140445;
CC Evidence={ECO:0000269|PubMed:27758859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56165;
CC Evidence={ECO:0000305|PubMed:27758859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphocholine = (9Z-
CC octadecenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:56168, ChEBI:CHEBI:16870, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:27758859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56169;
CC Evidence={ECO:0000305|PubMed:27758859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + sn-
CC glycerol 3-phosphocholine = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:56236, ChEBI:CHEBI:16870, ChEBI:CHEBI:74971,
CC ChEBI:CHEBI:76083, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000269|PubMed:27758859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56237;
CC Evidence={ECO:0000305|PubMed:27758859};
CC -!- ACTIVITY REGULATION: The GPCAT activity is sensitive to N-
CC ethylmaleimide, phenanthroline, and divalent cations including Ca(2+),
CC Mg(2+), Mn(2+) and Zn(2+) (PubMed:18430972). The activity is also
CC inhibited by glycerol-3-phosphate (G3P) (PubMed:27758859).
CC {ECO:0000269|PubMed:18430972, ECO:0000269|PubMed:27758859}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.45 mM for glycero-3-phosphocholine (GPC)
CC {ECO:0000269|PubMed:27758859};
CC Vmax=87 nmol/min/mg enzyme toward glycero-3-phosphocholine (GPC)
CC {ECO:0000269|PubMed:27758859};
CC pH dependence:
CC Optimum pH is 6.5-8.5. {ECO:0000269|PubMed:18430972};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12524434,
CC ECO:0000269|PubMed:18430972}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12524434}.
CC -!- DISRUPTION PHENOTYPE: Decreases the levels of monounsaturated PC
CC species and increased those of diunsaturated PC species. Does not
CC significantly affect phosphatidylethanolamine, phosphatidylinositol,
CC and phosphatidylserine profiles. {ECO:0000269|PubMed:30514764}.
CC -!- SIMILARITY: Belongs to the GPC1 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; X85807; CAA59807.1; -; Genomic_DNA.
DR EMBL; Z72934; CAA97163.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08241.1; -; Genomic_DNA.
DR PIR; S60440; S60440.
DR RefSeq; NP_011665.1; NM_001181278.1.
DR AlphaFoldDB; P48236; -.
DR BioGRID; 33397; 114.
DR DIP; DIP-4289N; -.
DR IntAct; P48236; 13.
DR STRING; 4932.YGR149W; -.
DR SwissLipids; SLP:000001892; -.
DR iPTMnet; P48236; -.
DR MaxQB; P48236; -.
DR PaxDb; P48236; -.
DR PRIDE; P48236; -.
DR EnsemblFungi; YGR149W_mRNA; YGR149W; YGR149W.
DR GeneID; 853052; -.
DR KEGG; sce:YGR149W; -.
DR SGD; S000003381; GPC1.
DR VEuPathDB; FungiDB:YGR149W; -.
DR eggNOG; KOG2895; Eukaryota.
DR HOGENOM; CLU_018994_1_2_1; -.
DR InParanoid; P48236; -.
DR OMA; YIDYYGK; -.
DR BioCyc; YEAST:G3O-30852-MON; -.
DR BRENDA; 2.3.1.B36; 984.
DR PRO; PR:P48236; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P48236; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106158; F:glycero-3-phosphocholine acyltransferase activity; IDA:SGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:SGD.
DR InterPro; IPR021261; GPCAT.
DR PANTHER; PTHR31201; PTHR31201; 1.
DR Pfam; PF10998; DUF2838; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..432
FT /note="Glycerophosphocholine acyltransferase 1"
FT /id="PRO_0000202829"
FT TOPO_DOM 1..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..187
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..263
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..346
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 347..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:12524434,
FT ECO:0000269|PubMed:16847258"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 432 AA; 51647 MW; 257FB7E828784EAB CRC64;
MYKLDNNDID DETNNSVSLT SLLEFLDPIA SKVVSKYYHG SHLSKAEQKL RNFEGFRRRK
PHHEHDSHHP HHLNRSRSFL QLEDFKVRAL QRIRNLDKPL DSIFFKNSSR LEKAFYPFTL
FNIFFIGFLM GRFPEWFHVY YTILFFVLMP IRFYTYYKTK NHYFLADFCY FVNMLCLLFI
WIFPYSYSLF QSCFAFTFGT LCFAVITWRN SLVIHSIDKT TSCFIHIIPP CVMYVIYHGL
PLEYKIERFP GAIIQSELDI KKNILWTSLY YLVWQSLYHY FITLKKSSKI KSGERMTSFE
YLTTHQFKNF WAVKLRSPWP MIIYTLSQYF YQLFTMLLCG IWIRYKLAAA LFLTIVFLWA
SHNGATYYID HYGKNFEKEV DRLRLEVENL QQKLQPDSDA VISDASVNDK DYLNVNRDED
FDDSSSVSSK SD
