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Database: UniProt
Entry: H2QYF1_PANTR
LinkDB: H2QYF1_PANTR
Original site: H2QYF1_PANTR 
ID   H2QYF1_PANTR            Unreviewed;       334 AA.
AC   H2QYF1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=choline-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00026101};
DE            EC=2.7.7.15 {ECO:0000256|ARBA:ARBA00026101};
GN   Name=PCYT1B {ECO:0000313|Ensembl:ENSPTRP00000037300.5,
GN   ECO:0000313|VGNC:VGNC:14834};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000037300.5, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000037300.5, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000037300.5}
RP   IDENTIFICATION.
RG   Ensembl;
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}.
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DR   EMBL; AACZ04014473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04014474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H2QYF1; -.
DR   Ensembl; ENSPTRT00000040368.5; ENSPTRP00000037300.5; ENSPTRG00000021752.6.
DR   VGNC; VGNC:14834; PCYT1B.
DR   eggNOG; KOG2804; Eukaryota.
DR   GeneTree; ENSGT00940000156040; -.
DR   HOGENOM; CLU_034585_4_2_1; -.
DR   OMA; FEDFSIC; -.
DR   TreeFam; TF106336; -.
DR   UniPathway; UPA00753; UER00739.
DR   Proteomes; UP000002277; Chromosome X.
DR   Bgee; ENSPTRG00000021752; Expressed in testis and 13 other cell types or 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   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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT   DOMAIN          45..173
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          274..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          204..231
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        274..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  38043 MW;  756CC74FF0A10ED3 CRC64;
     IGPVTLTAPA PFADETNCQC QAPHEKLTIA QARLGTPADR PVRVYADGIF DLFHSGHARA
     LMQAKTLFPN SYLLVGVCSD DLTHKFKGFT VMNEAERYEA LRHCRYVDEV IRDAPWTLTP
     EFLEKHKIDF VAHDDIPYSS AGSDDVYKHI KEAGMFVPTQ RTEGISTSDI ITRIVRDYDV
     YARRNLQRGY TAKELNVSFI NEKRYRFQNQ VDKMKEKVKN VEERSKEFVN RVEEKSHDLI
     QKWEEKSREF IGNFLELFGP DGAWKQMFQE RSSRMLQALS PKQSPVSSPT RSRSPSRSPS
     PTFSWLPLKT SPPSSPKAAS ASISSMSEGD EDEK
//
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