UCK1_MOUSE
ID UCK1_MOUSE Reviewed; 277 AA.
AC P52623;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Uridine-cytidine kinase 1;
DE Short=UCK 1;
DE EC=2.7.1.48 {ECO:0000250|UniProtKB:Q9HA47};
DE AltName: Full=Cytidine monophosphokinase 1;
DE AltName: Full=Uridine monophosphokinase 1;
GN Name=Uck1; Synonyms=Umpk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-277, FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC TISSUE=Brain;
RX PubMed=8951040; DOI=10.1006/abbi.1996.0537;
RA Ropp P.A., Traut T.W.;
RT "Cloning and expression of a cDNA encoding uridine kinase from mouse
RT brain.";
RL Arch. Biochem. Biophys. 336:105-112(1996).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate
CC and cytidine monophosphate (PubMed:8951040). Does not phosphorylate
CC deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a
CC phosphate donor (By similarity). {ECO:0000250|UniProtKB:Q9HA47,
CC ECO:0000269|PubMed:8951040}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000269|PubMed:8951040};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q9HA47};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000250|UniProtKB:Q9HA47}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000269|PubMed:8951040}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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; BC025146; AAH25146.1; -; mRNA.
DR EMBL; L31783; AAB50568.1; -; mRNA.
DR RefSeq; NP_035805.2; NM_011675.2.
DR AlphaFoldDB; P52623; -.
DR SMR; P52623; -.
DR BioGRID; 204440; 8.
DR IntAct; P52623; 1.
DR STRING; 10090.ENSMUSP00000002625; -.
DR BindingDB; P52623; -.
DR ChEMBL; CHEMBL2196; -.
DR iPTMnet; P52623; -.
DR PhosphoSitePlus; P52623; -.
DR EPD; P52623; -.
DR MaxQB; P52623; -.
DR PaxDb; P52623; -.
DR PRIDE; P52623; -.
DR ProteomicsDB; 298191; -.
DR DNASU; 22245; -.
DR GeneID; 22245; -.
DR KEGG; mmu:22245; -.
DR CTD; 83549; -.
DR MGI; MGI:98904; Uck1.
DR eggNOG; KOG4203; Eukaryota.
DR InParanoid; P52623; -.
DR OrthoDB; 929897at2759; -.
DR Reactome; R-MMU-73614; Pyrimidine salvage.
DR SABIO-RK; P52623; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR BioGRID-ORCS; 22245; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Uck1; mouse.
DR PRO; PR:P52623; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P52623; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043771; F:cytidine kinase activity; ISS:UniProtKB.
DR GO; GO:0004849; F:uridine kinase activity; IDA:MGI.
DR GO; GO:0044211; P:CTP salvage; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044206; P:UMP salvage; IDA:MGI.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029920; UCK-1.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF66; PTHR10285:SF66; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..277
FT /note="Uridine-cytidine kinase 1"
FT /id="PRO_0000164454"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA47"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA47"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HA47"
SQ SEQUENCE 277 AA; 31068 MW; 3EBB3C4187FAEB4A CRC64;
MASAGGGGSE SAAPEADRPQ PRPFLIGVSG GTASGKSTVC EKIMELLGQN EVDRRQRKLV
ILSQDCFYKV LTAEQKAKAL KGQYNFDHPD AFDNDLMHKT LKNIVEGKTV EVPTYDFVTH
SRLPETTVVY PADVVLFEGI LVFYTQEIRD MFHLRLFVDT DSDVRLSRRV LRDVQRGRDL
EQILTQYTAF VKPAFEEFCL PTKKYADVII PRGVDNMVAI NLIVQHIQDI LNGDLCKRHR
GGPNGRNHKR TFPEPGDHPG VLATGKRSHL ESSSRPH
