GPC1_BRANA
ID GPC1_BRANA Reviewed; 387 AA.
AC A0A078H868;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 25-MAY-2022, entry version 23.
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:27758859};
GN Name=GPC1 {ECO:0000303|PubMed:27758859};
GN ORFNames=BnaC04g29620D, GSBRNA2T00055068001;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh;
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Glycerophosphocholine acyltransferase (GPCAT) that utilizes
CC acyl-CoA to acylate glycero-3-phosphocholine (GPC), forming
CC lysophosphatidylcholine (LPC) (PubMed:27758859). Shows broad acyl
CC specificities with a preference for 16:0-CoA, polyunsaturated acyl-CoA,
CC and the hydroxylated ricinoleoyl-CoA (PubMed:27758859). Catalyzes also
CC the acylation of glycero-3-phosphoethanolamine (GPE) with acyl-CoA
CC (PubMed:27758859). In addition to acyl-CoA, GPCAT efficiently utilizes
CC LPC and lysophosphatidylethanolamine (LPE) as acyl donors in the
CC acylation of 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 {ECO:0000269|PubMed:27758859}.
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: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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the GPC1 family. {ECO:0000305}.
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DR EMBL; LK032320; CDY33689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078H868; -.
DR SMR; A0A078H868; -.
DR STRING; 3708.A0A078H868; -.
DR EnsemblPlants; CDY33689; CDY33689; GSBRNA2T00055068001.
DR Gramene; CDY33689; CDY33689; GSBRNA2T00055068001.
DR OMA; YIDYYGK; -.
DR BRENDA; 2.3.1.B36; 944.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106158; F:glycero-3-phosphocholine acyltransferase activity; IEA:RHEA.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..387
FT /note="Glycerophosphocholine acyltransferase 1"
FT /id="PRO_0000448645"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..93
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..145
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..227
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..319
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 352..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 45457 MW; 399724EEE128C19B CRC64;
MANNEDHSED SNLNGEDSFE TVKQRLKDRS KKVVQTRDLL SKQAVQTREI LSKQAVKIAK
QAEEHERFIN KVTHLVGVLG FGGFCFLLGA RPQDIPLVYC FFYVIFVPLR WIYYRFKKWH
YYLLDFCYYA NTIFLVDLLL YPKNEKLFMV CFSFAEGPLA WALIVWRCSL VFSSVDKIVS
VLIHLLPGLV FFTIRWWNPE TFAAMHPVGT ARRVSWPYVD DKPYLFTWLF LIPLVVYTLW
QVLYFLIVNV LRRQRLLRDP EVMTSYRELS KKAQKANNKL WQLSGILGDQ NRMWMYILFQ
AIFTVATMAL TVPIFLSYRL HVIFQILKIS AAVWNGGSFL LEVMPRQVIQ KEKKKKTEMQ
PIEEQLPAQH EPVSPPTHYE AESTTET
