PECT1_ARATH
ID PECT1_ARATH Reviewed; 421 AA.
AC Q9ZVI9;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ethanolamine-phosphate cytidylyltransferase {ECO:0000305};
DE EC=2.7.7.14 {ECO:0000269|PubMed:17189343};
DE AltName: Full=CTP:phosphoethanolamine cytidylyltransferase {ECO:0000305};
DE AltName: Full=Phosphorylethanolamine cytidylyltransferase 1 {ECO:0000303|PubMed:17189343};
GN Name=PECT1 {ECO:0000303|PubMed:17189343};
GN OrderedLocusNames=At2g38670 {ECO:0000312|Araport:AT2G38670};
GN ORFNames=T6A23.13 {ECO:0000312|EMBL:AAC67351.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 INDUCTION.
RX PubMed=15147879; DOI=10.1016/j.febslet.2004.04.015;
RA Tasseva G., Richard L., Zachowski A.;
RT "Regulation of phosphatidylcholine biosynthesis under salt stress involves
RT choline kinases in Arabidopsis thaliana.";
RL FEBS Lett. 566:115-120(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-126.
RX PubMed=17189343; DOI=10.1105/tpc.106.040840;
RA Mizoi J., Nakamura M., Nishida I.;
RT "Defects in CTP:PHOSPHORYLETHANOLAMINE CYTIDYLYLTRANSFERASE affect
RT embryonic and postembryonic development in Arabidopsis.";
RL Plant Cell 18:3370-3385(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21896887; DOI=10.1104/pp.111.183160;
RA Duncan O., Taylor N.L., Carrie C., Eubel H., Kubiszewski-Jakubiak S.,
RA Zhang B., Narsai R., Millar A.H., Whelan J.;
RT "Multiple lines of evidence localize signaling, morphology, and lipid
RT biosynthesis machinery to the mitochondrial outer membrane of
RT Arabidopsis.";
RL Plant Physiol. 157:1093-1113(2011).
CC -!- FUNCTION: Plays an important role in the biosynthesis of the
CC phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP-
CC ethanolamine. Essential for early embryonic development.
CC {ECO:0000269|PubMed:17189343}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphoethanolamine = CDP-ethanolamine +
CC diphosphate; Xref=Rhea:RHEA:24592, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:58190; EC=2.7.7.14;
CC Evidence={ECO:0000269|PubMed:17189343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24593;
CC Evidence={ECO:0000269|PubMed:17189343};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:17189343, ECO:0000305|PubMed:21896887}; Single-pass
CC membrane protein {ECO:0000305|PubMed:17189343,
CC ECO:0000305|PubMed:21896887}.
CC -!- TISSUE SPECIFICITY: Expressed in root tip, lateral root primordia,
CC leaves, shoot apex, stem vascular bundles, pollen and embryos.
CC {ECO:0000269|PubMed:17189343}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:17189343}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; AC005499; AAC67351.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09568.1; -; Genomic_DNA.
DR EMBL; AY092984; AAM12983.1; -; mRNA.
DR EMBL; AY128807; AAM91207.1; -; mRNA.
DR PIR; H84807; H84807.
DR RefSeq; NP_181401.1; NM_129424.5.
DR AlphaFoldDB; Q9ZVI9; -.
DR SMR; Q9ZVI9; -.
DR BioGRID; 3791; 1.
DR STRING; 3702.AT2G38670.1; -.
DR iPTMnet; Q9ZVI9; -.
DR SwissPalm; Q9ZVI9; -.
DR PaxDb; Q9ZVI9; -.
DR PRIDE; Q9ZVI9; -.
DR ProteomicsDB; 235114; -.
DR EnsemblPlants; AT2G38670.1; AT2G38670.1; AT2G38670.
DR GeneID; 818449; -.
DR Gramene; AT2G38670.1; AT2G38670.1; AT2G38670.
DR KEGG; ath:AT2G38670; -.
DR Araport; AT2G38670; -.
DR TAIR; locus:2064123; AT2G38670.
DR eggNOG; KOG2803; Eukaryota.
DR HOGENOM; CLU_031246_2_1_1; -.
DR InParanoid; Q9ZVI9; -.
DR OMA; VLQCKYI; -.
DR OrthoDB; 871204at2759; -.
DR PhylomeDB; Q9ZVI9; -.
DR BioCyc; ARA:AT2G38670-MON; -.
DR BioCyc; MetaCyc:AT2G38670-MON; -.
DR BRENDA; 2.7.7.14; 399.
DR UniPathway; UPA00558; UER00742.
DR PRO; PR:Q9ZVI9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVI9; baseline and differential.
DR Genevisible; Q9ZVI9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; IMP:TAIR.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR044608; Ect1/PCYT2.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR45780; PTHR45780; 1.
DR Pfam; PF01467; CTP_transf_like; 2.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 2.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..421
FT /note="Ethanolamine-phosphate cytidylyltransferase"
FT /id="PRO_0000423341"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 203..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 262..263
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q99447"
FT BINDING 270..273
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q99447"
FT BINDING 298
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q99447"
FT BINDING 346..349
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q99447"
FT BINDING 377..381
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q99447"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 126
FT /note="P->S: In pect1-4; delayed embryo maturation and
FT reduced fertility."
FT /evidence="ECO:0000269|PubMed:17189343"
SQ SEQUENCE 421 AA; 46978 MW; B83BB12CDC346504 CRC64;
MVWEKEKIVG SCIVGGAAFA VGASFLHLFL KGELPLGLGL GLSCPWRILR KRKPVRVYMD
GCFDMMHYGH CNALRQARAL GDQLVVGVVS DEEIIANKGP PVTPLHERMT MVKAVKWVDE
VISDAPYAIT EDFMKKLFDE YQIDYIIHGD DPCVLPDGTD AYALAKKAGR YKQIKRTEGV
SSTDIVGRML LCVRERSISD THSRSSLQRQ FSHGHSSPKF EDGASSAGTR VSHFLPTSRR
IVQFSNGKGP GPDARIIYID GAFDLFHAGH VEILRRAREL GDFLLVGIHN DQTVSAKRGA
HRPIMNLHER SLSVLACRYV DEVIIGAPWE VSRDTITTFD ISLVVHGTVA ESDDFRKEED
NPYSVPISMG IFQVLDSPLD ITTSTIIRRI VANHEAYQKR NAKKEASEKK YYEQKSFVSG
D
