GPC1_RICCO
ID GPC1_RICCO Reviewed; 391 AA.
AC B9RK42;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 41.
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}; ORFNames=RCOM_1046270;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale;
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
RN [2]
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 monoacyl-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:58460,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:84465; Evidence={ECO:0000269|PubMed:27758859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58461;
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=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:0000269|PubMed:27758859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + sn-glycerol 3-phosphocholine = (9Z-
CC hexadecenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:56228, ChEBI:CHEBI:16870, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:140432;
CC Evidence={ECO:0000269|PubMed:27758859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56229;
CC Evidence={ECO:0000269|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:0000269|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:0000269|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: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; EQ973784; EEF48040.1; -; Genomic_DNA.
DR RefSeq; XP_002514086.1; XM_002514040.2.
DR AlphaFoldDB; B9RK42; -.
DR SMR; B9RK42; -.
DR STRING; 3988.XP_002514086.1; -.
DR SwissLipids; SLP:000001891; -.
DR PRIDE; B9RK42; -.
DR GeneID; 8272523; -.
DR KEGG; rcu:8272523; -.
DR eggNOG; KOG2895; Eukaryota.
DR InParanoid; B9RK42; -.
DR OrthoDB; 1522758at2759; -.
DR BRENDA; 2.3.1.B36; 1204.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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..391
FT /note="Glycerophosphocholine acyltransferase 1"
FT /id="PRO_0000448644"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..92
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..144
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..226
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..318
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 354..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 45744 MW; D2F01CF4112A1699 CRC64;
MSNNEDPINE FVSNGDSFEK VKQRLKDRSK KVAQTKEILS KQANQTKEIL SKQAVKIAKQ
AEEHESFINK VTHLLGVLGF GGFCFLLGAR PQDIPYVYCL FFFIFVPLRW IYYRFKKWHY
FLLDFCYYAN TIFLVDLLLY PKDEKLFMVC FSFAEGPLAW ALIVWRCSLV FSSVDKIVSV
LIHLLPGLVF FTIRWWNPAT FEAMHPEGTS GRASWPYVED KSFLFTWLFL VPLVAYFLWQ
LLYFLIVNVL RRQRLLRDPE VMTSYRELSK KAQKANNVWW RLSGLLGDQN RMLMYILLQA
LFTVATTALT VPIFLSYELH AVFQILKVSA AVWNGGSFLL DVMPRQVILK EKKKSELQPA
HIQQYHSEPK QDQSPNSMEI RMKTIHSAEE Q
