UCK2_RAT
ID UCK2_RAT Reviewed; 261 AA.
AC Q9QYG8; B2RZ83;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Uridine-cytidine kinase 2;
DE Short=UCK 2;
DE EC=2.7.1.48 {ECO:0000250|UniProtKB:Q9BZX2};
DE AltName: Full=Cytidine monophosphokinase 2;
DE AltName: Full=Uridine monophosphokinase 2;
GN Name=Uck2 {ECO:0000312|RGD:620742};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3] {ECO:0000305, ECO:0000312|EMBL:BAA83085.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 152-256, AND INDUCTION.
RC STRAIN=Sprague-Dawley {ECO:0000305};
RC TISSUE=Spinal cord {ECO:0000312|EMBL:BAA83085.1};
RX PubMed=10581173; DOI=10.1006/bbrc.1999.1781;
RA Yuh I., Yaoi T., Watanabe S., Okajima S., Hirasawa Y., Fushiki S.;
RT "Up-regulated uridine kinase gene identified by RLCS in the ventral horn
RT after crush injury to rat sciatic nerves.";
RL Biochem. Biophys. Res. Commun. 266:104-109(1999).
CC -!- FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate
CC and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides
CC or purine ribonucleosides. Can use ATP or GTP as a phosphate donor.
CC {ECO:0000250|UniProtKB:Q9BZX2}.
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:0000250|UniProtKB:Q9BZX2};
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:Q9BZX2};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- INDUCTION: Following crush injury to sciatic nerves.
CC {ECO:0000269|PubMed:10581173}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000255}.
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DR EMBL; CH473958; EDM09286.1; -; Genomic_DNA.
DR EMBL; BC167060; AAI67060.1; -; mRNA.
DR EMBL; AB030700; BAA83085.1; -; mRNA.
DR AlphaFoldDB; Q9QYG8; -.
DR SMR; Q9QYG8; -.
DR STRING; 10116.ENSRNOP00000005213; -.
DR jPOST; Q9QYG8; -.
DR PaxDb; Q9QYG8; -.
DR PRIDE; Q9QYG8; -.
DR Ensembl; ENSRNOT00000090668; ENSRNOP00000070085; ENSRNOG00000003917.
DR UCSC; RGD:620742; rat.
DR RGD; 620742; Uck2.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR InParanoid; Q9QYG8; -.
DR Reactome; R-RNO-73614; Pyrimidine salvage.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:Q9QYG8; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043771; F:cytidine kinase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004849; F:uridine kinase activity; ISS:UniProtKB.
DR GO; GO:0071453; P:cellular response to oxygen levels; IEP:RGD.
DR GO; GO:0044211; P:CTP salvage; ISS:UniProtKB.
DR GO; GO:0007631; P:feeding behavior; IEP:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; TAS:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0044206; P:UMP salvage; ISS:UniProtKB.
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; IPR029925; UCK-2.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF131; PTHR10285:SF131; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT CHAIN 2..261
FT /note="Uridine-cytidine kinase 2"
FT /id="PRO_0000164457"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
SQ SEQUENCE 261 AA; 29404 MW; 780AA3CFF5CA8153 CRC64;
MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD YHQKQVVILS
QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELIFKTLKE ITEGKTVQIP VYDFVSHSRK
EETVTIYPAD VVLFEGILAF YSQEVRDLFQ MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ
ILSQYITFVK PAFEEFCLPT KKYADVIIPR GADNLVAINL IVQHIQDILN GGLSKRQTNG
YLNGYTPSRK RQASESSSRP H
