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Database: UniProt
Entry: I1LC79_SOYBN
LinkDB: I1LC79_SOYBN
Original site: I1LC79_SOYBN 
ID   I1LC79_SOYBN            Unreviewed;       424 AA.
AC   I1LC79;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
DE            EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
GN   Name=100794043 {ECO:0000313|EnsemblPlants:KRH34428};
GN   ORFNames=GLYMA_10G183200 {ECO:0000313|EMBL:KRH34428.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH34428};
RN   [1] {ECO:0000313|EMBL:KRH34428.1, ECO:0000313|EnsemblPlants:KRH34428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH34428};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH34428.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH34428}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH34428};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH34428.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH34428.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the synthesis of minor phospholipids and
CC       in modulation of IP3-mediated signal transduction.
CC       {ECO:0000256|PIRNR:PIRNR018269}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC         diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC         Evidence={ECO:0000256|PIRNR:PIRNR018269,
CC         ECO:0000256|RuleBase:RU003938};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR018269};
CC       Note=Requires a divalent cation for activity.
CC       {ECO:0000256|PIRNR:PIRNR018269};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005119, ECO:0000256|PIRNR:PIRNR018269,
CC       ECO:0000256|RuleBase:RU003938}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185,
CC       ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}.
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DR   EMBL; CM000843; KRH34428.1; -; Genomic_DNA.
DR   RefSeq; XP_003536226.1; XM_003536178.3.
DR   RefSeq; XP_014618749.1; XM_014763263.1.
DR   AlphaFoldDB; I1LC79; -.
DR   EnsemblPlants; KRH34428; KRH34428; GLYMA_10G183200.
DR   GeneID; 100794043; -.
DR   Gramene; KRH34428; KRH34428; GLYMA_10G183200.
DR   KEGG; gmx:100794043; -.
DR   HOGENOM; CLU_023471_2_0_1; -.
DR   OMA; VFTAAPW; -.
DR   OrthoDB; 5481516at2759; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000008827; Chromosome 10.
DR   ExpressionAtlas; I1LC79; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR000374; PC_trans.
DR   InterPro; IPR016720; PC_Trfase_euk.
DR   PANTHER; PTHR13773; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR13773:SF31; PHOSPHATIDATE CYTIDYLYLTRANSFERASE 2; 1.
DR   Pfam; PF01148; CTP_transf_1; 1.
DR   PIRSF; PIRSF018269; PC_trans_euk; 1.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018269};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018269};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|PIRNR:PIRNR018269}.
FT   TRANSMEM        57..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        107..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        146..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        181..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        209..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        243..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        316..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  48715 MW;  22A5053CEF79DFFD CRC64;
     MQKDTSTTAP STTSGRVRHR KRSNEVIPEV SKANGTKLLV NDKSKYKSML IRAYSSVWMI
     GGFVLIIYMG HLYITAMVVV IQIFMARELF NLLRRAHEDR QLPGFRLLNW HFFFTAMLFV
     YGRILSQCLV NTVTSDMVLY WLVSNLIKYH MVICYSLYIA GFMWFILTLK KKMYKYQFGQ
     YAWTHMILIV VFGQSSFTVA SIFEGIFWFL LPATLIVIND IAAYIFGFFF GRTPLIKLSP
     KKTWEGFIGA SVTTIISAFM LANIMGRSQW LTCPRKDLST GWLHCDPGPL FKPESYPLPG
     CISHWFSWKE ISILPIQWHS LCLGLFASII APFGGFFASG FKRAFKIKDF GDSIPGHGGI
     TDRMDCQMVM AVFAYIYHQS FVVPQTLSVE MILDQISMNL TFDEQQALYW RLGEILQQGF
     ARMS
//
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