ID A3KNL3_DANRE Unreviewed; 343 AA.
AC A3KNL3; A0A8M1NDJ0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=choline-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00026101};
DE EC=2.7.7.15 {ECO:0000256|ARBA:ARBA00026101};
GN Name=pcyt1ba {ECO:0000313|Ensembl:ENSDARP00000065287,
GN ECO:0000313|RefSeq:NP_001076415.1,
GN ECO:0000313|ZFIN:ZDB-GENE-061220-4};
GN Synonyms=pcyt1b {ECO:0000313|RefSeq:NP_001076415.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI33903.1};
RN [1] {ECO:0000313|RefSeq:NP_001076415.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16517001;
RA Kohn M., Hogel J., Vogel W., Minich P., Kehrer-Sawatzki H., Graves J.A.,
RA Hameister H.;
RT "Reconstruction of a 450-My-old ancestral vertebrate protokaryotype.";
RL Trends Genet. 22:203-210(2006).
RN [2] {ECO:0000313|EMBL:AAI33903.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole {ECO:0000313|EMBL:AAI33903.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSDARP00000065287}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000065287};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSDARP00000065287, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000065287};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [5] {ECO:0000313|RefSeq:NP_001076415.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [6] {ECO:0000313|RefSeq:NP_001076415.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [7] {ECO:0000313|RefSeq:NP_001076415.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [8] {ECO:0000313|RefSeq:NP_001076415.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline
CC pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00025501}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate;
CC Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975;
CC EC=2.7.7.15; Evidence={ECO:0000256|ARBA:ARBA00024554};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000256|ARBA:ARBA00024554};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC {ECO:0000256|ARBA:ARBA00025706}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010101}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR354424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC133902; AAI33903.1; -; mRNA.
DR RefSeq; NP_001076415.1; NM_001082946.1.
DR STRING; 7955.ENSDARP00000065287; -.
DR PaxDb; 7955-ENSDARP00000065287; -.
DR Ensembl; ENSDART00000065288.7; ENSDARP00000065287.6; ENSDARG00000058162.7.
DR GeneID; 100001552; -.
DR KEGG; dre:100001552; -.
DR AGR; ZFIN:ZDB-GENE-061220-4; -.
DR CTD; 100001552; -.
DR ZFIN; ZDB-GENE-061220-4; pcyt1ba.
DR eggNOG; KOG2804; Eukaryota.
DR HOGENOM; CLU_034585_4_2_1; -.
DR OMA; FEDFSIC; -.
DR OrthoDB; 5474784at2759; -.
DR TreeFam; TF106336; -.
DR Reactome; R-DRE-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00739.
DR Proteomes; UP000000437; Chromosome 24.
DR Bgee; ENSDARG00000058162; Expressed in testis and 12 other cell types or tissues.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045049; Pcy1-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR10739:SF20; CHOLINE-PHOSPHATE CYTIDYLYLTRANSFERASE B; 1.
DR PANTHER; PTHR10739; CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotidyltransferase {ECO:0000313|RefSeq:NP_001076415.1};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A3KNL3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transferase {ECO:0000313|RefSeq:NP_001076415.1}.
FT DOMAIN 54..182
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT REGION 287..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 39461 MW; B53F1AE9AB15C96F CRC64;
MEELEHTCPL PRTTLIEPAI FTPETSCECR APHEKLTVDQ ASHGTPVDRP VRVYADGIFD
LFHSGHARAL MQAKNLFPNT YLIVGVCSDE LTHKYKGFTV MTEDERYEAL RHCRYVDEVL
RDAPWTLTQD FLEKHKIDFV AHDDIPYSSA GSEDVYKHIK EAGMFVPTKR TEGISTSDLI
TRIVRDYDVY ARRNLQRGYT AKELNVSYIN EKKYRLQNQV DRMKEKVRTV EEKSKHFVYR
VEEKSHDLIQ KWEEKSREFI GNFLELFGPD GTWKQMFQER SGRMIQAFSP RGSPSSSPPR
DFSPSRSPSP PSRWAMPRTS PPSSPKGASA SISSMSEGDE DEK
//
