GPC1_SCHPO
ID GPC1_SCHPO Reviewed; 403 AA.
AC O94673;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Glycerophosphocholine acyltransferase 1 {ECO:0000250|UniProtKB:P48236};
DE Short=GPCAT {ECO:0000250|UniProtKB:P48236};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P48236};
GN Name=gpc1 {ECO:0000250|UniProtKB:P48236}; ORFNames=SPBC776.05;
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).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Glycerophosphocholine acyltransferase (GPCAT) that utilizes
CC acyl-CoA to acylate glycero-3-phosphocholine (GPC), forming
CC lysophosphatidylcholine (LPC) (By similarity). Shows broad acyl
CC specificities with a preference for 16:0-CoA, polyunsaturated acyl-CoA,
CC and the hydroxylated ricinoleoyl-CoA (By similarity). Catalyzes also
CC the acylation of glycero-3-phosphoethanolamine (GPE) with acyl-CoA (By
CC similarity). In addition to acyl-CoA, GPCAT efficiently utilizes LPC
CC and lysophosphatidylethanolamine (LPE) as acyl donors in the acylation
CC of GPC (By similarity). 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 (By similarity).
CC {ECO:0000250|UniProtKB:P48236}.
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:0000250|UniProtKB:P48236};
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:0000250|UniProtKB:P48236};
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:0000250|UniProtKB:P48236};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the GPC1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22878.2; -; Genomic_DNA.
DR PIR; T40675; T40675.
DR RefSeq; NP_596320.2; NM_001022242.2.
DR AlphaFoldDB; O94673; -.
DR SMR; O94673; -.
DR BioGRID; 277694; 5.
DR STRING; 4896.SPBC776.05.1; -.
DR iPTMnet; O94673; -.
DR MaxQB; O94673; -.
DR PaxDb; O94673; -.
DR EnsemblFungi; SPBC776.05.1; SPBC776.05.1:pep; SPBC776.05.
DR GeneID; 2541180; -.
DR KEGG; spo:SPBC776.05; -.
DR PomBase; SPBC776.05; -.
DR VEuPathDB; FungiDB:SPBC776.05; -.
DR eggNOG; KOG2895; Eukaryota.
DR HOGENOM; CLU_018994_1_2_1; -.
DR InParanoid; O94673; -.
DR OMA; GYLIGAY; -.
DR PRO; PR:O94673; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISM:PomBase.
DR GO; GO:0106158; F:glycero-3-phosphocholine acyltransferase activity; ISO:PomBase.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:PomBase.
DR InterPro; IPR021261; GPCAT.
DR PANTHER; PTHR31201; PTHR31201; 1.
DR Pfam; PF10998; DUF2838; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..403
FT /note="Glycerophosphocholine acyltransferase 1"
FT /id="PRO_0000343219"
FT TOPO_DOM 1..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..137
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..186
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..262
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..352
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 403 AA; 47491 MW; 00A9BDBFD67B8411 CRC64;
MDHLEFDENT DSEYSIFEED NDYGLHGLDD SVGFTDLFDA PNIYRVYSWL HKHYNQKKGQ
LKHGVSRQKN KLQPIHKQIN YETDKLKERL GKSIDKFQEQ WNSGKVVRFR DKLSFALGVS
TCILTALLVG MAPESMHLWY TIQLFVYLPL RYYTYQRKGY EYFIADFCYW GNILLLVYIW
IFPESRRLFI LSYSISYGTL AWSVVAWRNS LLFHSIDKIT SLFIHFFPPL VLHTIVHLTN
KSYLKDRFPA VLKVKKIDLL SSVEIASFFY ALWQIWYYFF IQVGKQKQIQ EGRPTSFTWL
SKAYSKTKLG RAVAKLPQNL QPFVFMIIQY LYSITTMLPC SLWYNNKLYS TAFLALIFGW
SVWNGASYYI DVFGRRFQKE LEALRQQLAE TPTNSGSSSA LSR
