ID   Q7ZYA8_XENLA            Unreviewed;       366 AA.
AC   Q7ZYA8;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   28-JUN-2023, entry version 79.
DE   RecName: Full=choline-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00026101};
DE            EC=2.7.7.15 {ECO:0000256|ARBA:ARBA00026101};
GN   Name=pcyt1b.S {ECO:0000313|RefSeq:NP_001080539.1,
GN   ECO:0000313|Xenbase:XB-GENE-6256564};
GN   Synonyms=cctb {ECO:0000313|RefSeq:NP_001080539.1}, ctb
GN   {ECO:0000313|RefSeq:NP_001080539.1}, pcyt1a
GN   {ECO:0000313|RefSeq:NP_001080539.1}, pcyt1b
GN   {ECO:0000313|RefSeq:NP_001080539.1,
GN   ECO:0000313|Xenbase:XB-GENE-6256564};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH43868.1};
RN   [1] {ECO:0000313|RefSeq:NP_001080539.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH43868.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH43868.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001080539.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAR-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}.
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DR   EMBL; BC043868; AAH43868.1; -; mRNA.
DR   RefSeq; NP_001080539.1; NM_001087070.1.
DR   DNASU; 380231; -.
DR   GeneID; 380231; -.
DR   KEGG; xla:380231; -.
DR   CTD; 380231; -.
DR   Xenbase; XB-GENE-6256564; pcyt1b.S.
DR   OrthoDB; 5474784at2759; -.
DR   UniPathway; UPA00753; UER00739.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 380231; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IEA:InterPro.
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   PANTHER; PTHR10739:SF19; CHOLINE-PHOSPHATE CYTIDYLYLTRANSFERASE A; 1.
DR   PANTHER; PTHR10739; CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotidyltransferase {ECO:0000313|RefSeq:NP_001080539.1};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Transferase {ECO:0000313|RefSeq:NP_001080539.1}.
FT   DOMAIN          80..208
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          239..266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        7..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  41928 MW;  946EA57C6987726D CRC64;
     MEAQSITKSV SRKRRKDDMG PNGTTDEDPV PIKVPRHTMG VREPAPFSDE LKVDRSKPYR
     RVSMEEAKIG TPLERPVRVY ADGIFDLFHS GHARALMQAK TLFPNTHLIV GVCSDELTHN
     LKGFTVMNEA ERYDAVQHCR YVDEVVRNAP WTLTPEFLVK HRIDFVAHDD IPYSSAGSDD
     VYKHIKDAGM FAPTQRTEGI STSDIITRIV RDYDVYVRRN LQRGYTAKEL NVSFINEKRF
     NLQERVDKVK KKVKDVEEKS KEFVQKVEEK SIDMIQKWEE KSREFIGNFL EMFGPEGALK
     HMLKEGKGRM LQAISPKQSP SSSPTRERSP SPSFRWPFSK ISPPASPGRH SRPTAATYDI
     SEDEED
//