ID   PCY2_BOVIN              Reviewed;         389 AA.
AC   Q5EA75;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ethanolamine-phosphate cytidylyltransferase;
DE            EC=2.7.7.14 {ECO:0000250|UniProtKB:Q99447};
DE   AltName: Full=CTP:phosphoethanolamine cytidylyltransferase;
DE   AltName: Full=Phosphorylethanolamine transferase;
GN   Name=PCYT2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Ethanolamine-phosphate cytidylyltransferase that catalyzes
CC       the second step in the synthesis of phosphatidylethanolamine (PE) from
CC       ethanolamine via the CDP-ethanolamine pathway. Phosphatidylethanolamine
CC       is a dominant inner-leaflet phospholipid in cell membranes, where it
CC       plays a role in membrane function by structurally stabilizing membrane-
CC       anchored proteins, and participates in important cellular processes
CC       such as cell division, cell fusion, blood coagulation, and apoptosis.
CC       {ECO:0000250|UniProtKB:Q99447}.
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:0000250|UniProtKB:Q99447};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24593;
CC         Evidence={ECO:0000250|UniProtKB:Q99447};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
CC       {ECO:0000250|UniProtKB:Q99447}.
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR   EMBL; BT020694; AAX08711.1; -; mRNA.
DR   RefSeq; NP_001030261.1; NM_001035089.1.
DR   AlphaFoldDB; Q5EA75; -.
DR   SMR; Q5EA75; -.
DR   STRING; 9913.ENSBTAP00000002434; -.
DR   PaxDb; Q5EA75; -.
DR   PRIDE; Q5EA75; -.
DR   GeneID; 510274; -.
DR   KEGG; bta:510274; -.
DR   CTD; 5833; -.
DR   eggNOG; KOG2803; Eukaryota.
DR   HOGENOM; CLU_031246_2_2_1; -.
DR   InParanoid; Q5EA75; -.
DR   OrthoDB; 871204at2759; -.
DR   TreeFam; TF106337; -.
DR   UniPathway; UPA00558; UER00742.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Lipid biosynthesis; Lipid metabolism; Nucleotidyltransferase;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..389
FT                   /note="Ethanolamine-phosphate cytidylyltransferase"
FT                   /id="PRO_0000269914"
FT   BINDING         221..222
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
FT   BINDING         229..232
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
FT   BINDING         307..310
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
FT   BINDING         336..340
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         341
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99447"
FT   MOD_RES         342
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O88637"
SQ   SEQUENCE   389 AA;  44158 MW;  8A6463D3DD6AAA69 CRC64;
     MIRNGHGEAG GAKRPGPRAR RAVRVWCDGC YDMVHYGHSN QLRQARAMGD HLIVGVHTDE
     EIAKHKGPPV FTQEERYKMV QAIKWVDEVV PAAPYVTTLE TLDKYNCDFC VHGNDITLTV
     DGRDTYEEVK QAGRYRECKR TQGVSTTDLV GRMLLVTKAH HSSQEMSSEY REYADSFGKC
     PGGRNPWTGV SQFLQTSQKI IQFASGKEPQ PGETVIYVAG AFDLFHIGHV DFLEKVYGLA
     ERPYVIAGLH FDQEVNHYKG KNYPIMNLHE RTLSVLACRY VSEVVIGAPY SVTAELLDHF
     KVDLVCHGKT EVVPDKDGSD PYEEPKRRGI FCQVDSGNDL TTDLIVQRII KNRLEYEARN
     QKKEAKELAF QEAMRRQEAQ PEREIDCDF