ADK_RAT
ID ADK_RAT Reviewed; 361 AA.
AC Q64640; O09162; Q642G1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Adenosine kinase;
DE Short=AK;
DE EC=2.7.1.20 {ECO:0000250|UniProtKB:P55263};
DE AltName: Full=Adenosine 5'-phosphotransferase;
GN Name=Adk;
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 [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9070863; DOI=10.1006/bbrc.1997.6157;
RA McNally T., Helfrich R.J., Cowart M., Dorwin S.A., Meuth J.L., Idler K.B.,
RA Klute K.A., Simmer R.L., Kowaluk E.A., Halbert D.N.;
RT "Cloning and expression of the adenosine kinase gene from rat and human
RT tissues.";
RL Biochem. Biophys. Res. Commun. 231:645-650(1997).
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-361.
RC TISSUE=Liver;
RX PubMed=8917457; DOI=10.1111/j.1432-1033.1996.00564.x;
RA Singh B., Hao W., Wu Z.-C., Eigl B., Gupta R.S.;
RT "Cloning and characterization of cDNA for adenosine kinase from mammalian
RT (Chinese hamster, mouse, human and rat) species. High frequency mutants of
RT Chinese hamster ovary cells involve structural alterations in the gene.";
RL Eur. J. Biochem. 241:564-571(1996).
RN [4]
RP PROTEIN SEQUENCE OF 88-110 AND 119-148, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
CC -!- FUNCTION: Catalyzes the phosphorylation of the purine nucleoside
CC adenosine at the 5' position in an ATP-dependent manner. Serves as a
CC potential regulator of concentrations of extracellular adenosine and
CC intracellular adenine nucleotides. {ECO:0000250|UniProtKB:P55263}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + ATP = ADP + AMP + H(+); Xref=Rhea:RHEA:20824,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.20;
CC Evidence={ECO:0000250|UniProtKB:P55263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20825;
CC Evidence={ECO:0000250|UniProtKB:P55263};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P55263};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P55263};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenosine: step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55263}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; U90340; AAB50236.1; -; mRNA.
DR EMBL; BC081712; AAH81712.1; -; mRNA.
DR EMBL; U57042; AAB03110.1; -; mRNA.
DR PIR; JC5362; JC5362.
DR RefSeq; NP_037027.2; NM_012895.3.
DR AlphaFoldDB; Q64640; -.
DR SMR; Q64640; -.
DR STRING; 10116.ENSRNOP00000016709; -.
DR BindingDB; Q64640; -.
DR ChEMBL; CHEMBL2384; -.
DR iPTMnet; Q64640; -.
DR PhosphoSitePlus; Q64640; -.
DR jPOST; Q64640; -.
DR PaxDb; Q64640; -.
DR PRIDE; Q64640; -.
DR GeneID; 25368; -.
DR KEGG; rno:25368; -.
DR UCSC; RGD:2046; rat.
DR CTD; 132; -.
DR RGD; 2046; Adk.
DR eggNOG; KOG2854; Eukaryota.
DR InParanoid; Q64640; -.
DR PhylomeDB; Q64640; -.
DR TreeFam; TF300745; -.
DR Reactome; R-RNO-74217; Purine salvage.
DR UniPathway; UPA00588; UER00659.
DR PRO; PR:Q64640; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0004001; F:adenosine kinase activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004136; F:deoxyadenosine kinase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046085; P:adenosine metabolic process; IDA:RGD.
DR GO; GO:0044209; P:AMP salvage; ISO:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEP:RGD.
DR GO; GO:0106383; P:dAMP salvage; ISO:RGD.
DR GO; GO:0006175; P:dATP biosynthetic process; ISO:RGD.
DR GO; GO:0032263; P:GMP salvage; ISO:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:RGD.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR GO; GO:0006166; P:purine ribonucleoside salvage; ISO:RGD.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IMP:RGD.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR001805; Adenokinase.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR45769; PTHR45769; 1.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00989; ADENOKINASE.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Purine salvage;
KW Reference proteome; Transferase.
FT CHAIN 1..361
FT /note="Adenosine kinase"
FT /id="PRO_0000080055"
FT MOTIF 7..15
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P55263"
FT ACT_SITE 316
FT /evidence="ECO:0000250|UniProtKB:P55263"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P55263"
FT BINDING 34
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /evidence="ECO:0000250|UniProtKB:P55263"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55263"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P55263"
FT BINDING 305
FT /ligand="adenosine"
FT /ligand_id="ChEBI:CHEBI:16335"
FT /evidence="ECO:0000250|UniProtKB:P55263"
FT MOD_RES 76
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P55263"
FT CONFLICT 121
FT /note="D -> N (in Ref. 3; AAB03110)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="T -> S (in Ref. 3; AAB03110)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="A -> R (in Ref. 3; AAB03110)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="V -> M (in Ref. 3; AAB03110)"
FT /evidence="ECO:0000305"
FT CONFLICT 217..218
FT /note="FI -> LL (in Ref. 3; AAB03110)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="E -> A (in Ref. 3; AAB03110)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="D -> N (in Ref. 2; AAH81712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 40134 MW; 437B83CC56E7A1C8 CRC64;
MAAADEPKPK KLKVEAPEAL SENVLFGMGN PLLDISAVVD KDFLDKYSLK PNDQILAEDK
HKELFDELVK KFKVEYHAGG STQNSMKVAQ WMIQEPHRAA TFFGCIGIDK FGEILKSKAA
DAHVDAHYYE QNEQPTGTCA ACITGGNRSL VANLAAANCY KKEKHLDLEN NWMLVEKARV
YYIAGFFLTV SPESVLKVAR YAAENNRTFT LNLSAPFISQ FFKEALMEVM PYVDILFGNE
TEAATFAREQ GFETKDIKEI ARKTQALPKV NSKRQRTVIF TQGRDDTIVA TGNDVTAFPV
LDQNQEEIVD TNGAGDAFVG GFLSQLVSNK PLTECIRAGH YAASVIIRRT GCTFPEKPDF
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