ID A0A2I4GCG9_JUGRE Unreviewed; 226 AA.
AC A0A2I4GCG9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00013212, ECO:0000256|PIRNR:PIRNR000848};
DE EC=2.7.8.11 {ECO:0000256|ARBA:ARBA00013212, ECO:0000256|PIRNR:PIRNR000848};
GN Name=LOC109006694 {ECO:0000313|RefSeq:XP_018841606.1};
GN ORFNames=F2P56_036204 {ECO:0000313|EMBL:KAF5443666.1};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018841606.1};
RN [1] {ECO:0000313|EMBL:KAF5443666.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5443666.1};
RA Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA Stevens K., Paul R., Butterfield T., Britton M., Reagan R., Chakraborty S.,
RA Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R., Pratt K.,
RA Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M., Salzberg S.L.,
RA Wegrzyn J.L., Langley C.H., Neale D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF5443666.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5443666.1};
RA Marrano A., Britton M., Zimin A.V., Zaini P.A., Workman R., Puiu D.,
RA Bianco L., Allen B.J., Troggio M., Leslie C.A., Timp W., Dendekar A.,
RA Salzberg S.L., Neale D.B.;
RT "Walnut 2.0.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_018841606.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018841606.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) + CMP + H(+);
CC Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11;
CC Evidence={ECO:0000256|PIRNR:PIRNR000848};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|PIRNR:PIRNR000848,
CC ECO:0000256|RuleBase:RU003750}.
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DR EMBL; LIHL02000016; KAF5443666.1; -; Genomic_DNA.
DR RefSeq; XP_018841606.1; XM_018986061.2.
DR STRING; 51240.A0A2I4GCG9; -.
DR EnsemblPlants; Jr16_15170_p1; cds.Jr16_15170_p1; Jr16_15170.
DR GeneID; 109006694; -.
DR Gramene; Jr16_15170_p1; cds.Jr16_15170_p1; Jr16_15170.
DR KEGG; jre:109006694; -.
DR OrthoDB; 5472855at2759; -.
DR Proteomes; UP000235220; Chromosome 16.
DR Proteomes; UP000619265; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR014387; CDP_diag_ino_3_P_euk.
DR PANTHER; PTHR15362:SF4; CDP-DIACYLGLYCEROL--INOSITOL 3-PHOSPHATIDYLTRANSFERASE; 1.
DR PANTHER; PTHR15362; PHOSPHATIDYLINOSITOL SYNTHASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000848; CDP_diag_ino_3_P; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000848};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR000848};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000848};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR000848};
KW Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR000848};
KW Reference proteome {ECO:0000313|Proteomes:UP000235220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000848};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 226 AA; 25687 MW; 63B4FB4AC8A6D764 CRC64;
MMDTKLPRSK LSVYLYIPNI IGYIRILMNC LAFGVCFSNK KLFSILYLIS FVCDALDGYF
ARKLNQVSTF GAVLDMVTDR ISTACLLVIL SQVYRPGLIF LSLLALDIAS HWLQMYSTFL
FGRASHKDVK DSTNWLFKAY YGNRIFMAYC CVSCEVLYII LFLVAKNQTN DVIDVLVYTA
KQNSLLSLLV ALALFGWAIK QAINIIQMKT AADLCVLYDI NKKQRP
//
