GPC1_ARATH
ID GPC1_ARATH Reviewed; 381 AA.
AC Q9FJB4;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 OrderedLocusNames=At5g35460 {ECO:0000312|Araport:AT5G35460};
GN ORFNames=MOK9.4 {ECO:0000312|EMBL:BAB08704.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION, FUNCTION, AND CATALYTIC ACTIVITY.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58477;
CC 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62109;
CC Evidence={ECO:0000269|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: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; AB015477; BAB08704.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93969.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69377.1; -; Genomic_DNA.
DR EMBL; AY037213; AAK59798.1; -; mRNA.
DR EMBL; BT003018; AAO23583.1; -; mRNA.
DR RefSeq; NP_001318675.1; NM_001344105.1.
DR RefSeq; NP_198396.1; NM_122937.3.
DR AlphaFoldDB; Q9FJB4; -.
DR SMR; Q9FJB4; -.
DR IntAct; Q9FJB4; 51.
DR STRING; 3702.AT5G35460.1; -.
DR SwissLipids; SLP:000001896; -.
DR iPTMnet; Q9FJB4; -.
DR PaxDb; Q9FJB4; -.
DR PRIDE; Q9FJB4; -.
DR ProteomicsDB; 181606; -.
DR EnsemblPlants; AT5G35460.1; AT5G35460.1; AT5G35460.
DR EnsemblPlants; AT5G35460.2; AT5G35460.2; AT5G35460.
DR GeneID; 833509; -.
DR Gramene; AT5G35460.1; AT5G35460.1; AT5G35460.
DR Gramene; AT5G35460.2; AT5G35460.2; AT5G35460.
DR KEGG; ath:AT5G35460; -.
DR Araport; AT5G35460; -.
DR TAIR; locus:2169533; AT5G35460.
DR eggNOG; KOG2895; Eukaryota.
DR HOGENOM; CLU_018994_3_1_1; -.
DR InParanoid; Q9FJB4; -.
DR OMA; GYLIGAY; -.
DR OrthoDB; 1522758at2759; -.
DR PhylomeDB; Q9FJB4; -.
DR BRENDA; 2.3.1.B36; 399.
DR PRO; PR:Q9FJB4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJB4; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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..381
FT /note="Glycerophosphocholine acyltransferase 1"
FT /id="PRO_0000448643"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..89
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..141
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..223
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..315
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 44697 MW; 52A6FD1ED941D1AF CRC64;
MANNEDSNSN GLDSFDAVKQ RFKDRSKKVV QTRELLSKQA VQTREILSKQ AVKIAKQAEE
HERFINKVTH LVGVLGFGGF CFLLGARPQD IPLVYCFFYV IFVPLRWIYY RFKKWHYYLL
DFCYYANTIF LVDLLLYPKN EKLFMVCFSF AEGPLAWAII VWRCSLVFSS PDKIVSVLIH
LLPGLVFFTI RWWNPATFAA MHPVGTDRRV SWPYVEDKAY LFTWLFLVPL VVYTLWQVLY
FLIVNVLRRQ RLLRDPEVMT SYRELSKKAE KANNKLWQLS GLLGDQNRIW MYILFQAIFT
VATMALTVPI FLSYRLHVIF QILKISAAVW NGGSFLLEVM PRQVIQKEKK KKAEMQPIEE
QILHHEAVSH PTENEPKSTE T
