HPRT_MOUSE
ID HPRT_MOUSE Reviewed; 218 AA.
AC P00493; Q545Y2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE Short=HGPRT;
DE Short=HGPRTase;
DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P00492};
DE AltName: Full=HPRT B;
GN Name=Hprt1; Synonyms=Hprt;
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 [MRNA].
RX PubMed=6294614; DOI=10.1093/nar/10.21.6763;
RA Konecki D.S., Brennand J., Fuscoe J.C., Caskey C.T., Chinault A.C.;
RT "Hypoxanthine-guanine phosphoribosyltransferase genes of mouse and Chinese
RT hamster: construction and sequence analysis of cDNA recombinants.";
RL Nucleic Acids Res. 10:6763-6775(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Myeloma;
RX PubMed=6326107; DOI=10.1073/pnas.81.7.2147;
RA Melton D.W., Konecki D.S., Brennand J., Caskey C.T.;
RT "Structure, expression, and mutation of the hypoxanthine
RT phosphoribosyltransferase gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2147-2151(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP PROTEIN SEQUENCE OF 74-83 AND 171-200, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine
CC to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-
CC phosphoribosylpyrophosphate onto the purine. Plays a central role in
CC the generation of purine nucleotides through the purine salvage pathway
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8;
CC Evidence={ECO:0000250|UniProtKB:P00492};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC Evidence={ECO:0000250|UniProtKB:P00492};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8;
CC Evidence={ECO:0000250|UniProtKB:P00492};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC Evidence={ECO:0000250|UniProtKB:P00492};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. The magnesium ions are
CC essentially bound to the substrate and have few direct interactions
CC with the protein. {ECO:0000250};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from hypoxanthine: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; J00423; AAA96232.1; -; mRNA.
DR EMBL; K01515; AAA96271.1; -; Genomic_DNA.
DR EMBL; K01507; AAA96271.1; JOINED; Genomic_DNA.
DR EMBL; K01508; AAA96271.1; JOINED; Genomic_DNA.
DR EMBL; K01509; AAA96271.1; JOINED; Genomic_DNA.
DR EMBL; K01510; AAA96271.1; JOINED; Genomic_DNA.
DR EMBL; K01511; AAA96271.1; JOINED; Genomic_DNA.
DR EMBL; K01512; AAA96271.1; JOINED; Genomic_DNA.
DR EMBL; K01513; AAA96271.1; JOINED; Genomic_DNA.
DR EMBL; K01514; AAA96271.1; JOINED; Genomic_DNA.
DR EMBL; AK002286; BAB21989.1; -; mRNA.
DR EMBL; AK088114; BAC40153.1; -; mRNA.
DR EMBL; AK146626; BAE27315.1; -; mRNA.
DR EMBL; BC083145; AAH83145.1; -; mRNA.
DR CCDS; CCDS40972.1; -.
DR PIR; I49756; RTMSG.
DR RefSeq; NP_038584.2; NM_013556.2.
DR AlphaFoldDB; P00493; -.
DR SMR; P00493; -.
DR BioGRID; 200411; 12.
DR DIP; DIP-6034N; -.
DR MINT; P00493; -.
DR STRING; 10090.ENSMUSP00000026723; -.
DR ChEMBL; CHEMBL3243916; -.
DR iPTMnet; P00493; -.
DR PhosphoSitePlus; P00493; -.
DR SwissPalm; P00493; -.
DR EPD; P00493; -.
DR jPOST; P00493; -.
DR MaxQB; P00493; -.
DR PaxDb; P00493; -.
DR PeptideAtlas; P00493; -.
DR PRIDE; P00493; -.
DR ProteomicsDB; 267060; -.
DR Antibodypedia; 1912; 613 antibodies from 37 providers.
DR DNASU; 15452; -.
DR Ensembl; ENSMUST00000026723; ENSMUSP00000026723; ENSMUSG00000025630.
DR GeneID; 15452; -.
DR KEGG; mmu:15452; -.
DR UCSC; uc009ter.1; mouse.
DR CTD; 15452; -.
DR MGI; MGI:96217; Hprt.
DR VEuPathDB; HostDB:ENSMUSG00000025630; -.
DR eggNOG; KOG3367; Eukaryota.
DR GeneTree; ENSGT00940000155028; -.
DR HOGENOM; CLU_073615_3_0_1; -.
DR InParanoid; P00493; -.
DR OMA; TMDWMAV; -.
DR OrthoDB; 1537610at2759; -.
DR PhylomeDB; P00493; -.
DR TreeFam; TF313367; -.
DR Reactome; R-MMU-74217; Purine salvage.
DR Reactome; R-MMU-9748787; Azathioprine ADME.
DR UniPathway; UPA00591; UER00648.
DR BioGRID-ORCS; 15452; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Hprt; mouse.
DR PRO; PR:P00493; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P00493; protein.
DR Bgee; ENSMUSG00000025630; Expressed in cleaving embryo and 285 other tissues.
DR Genevisible; P00493; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IMP:MGI.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0046083; P:adenine metabolic process; IGI:MGI.
DR GO; GO:0044209; P:AMP salvage; IDA:MGI.
DR GO; GO:0021954; P:central nervous system neuron development; IMP:MGI.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:MGI.
DR GO; GO:0046038; P:GMP catabolic process; ISS:UniProtKB.
DR GO; GO:0032263; P:GMP salvage; IMP:MGI.
DR GO; GO:0007625; P:grooming behavior; IGI:MGI.
DR GO; GO:0006178; P:guanine salvage; ISO:MGI.
DR GO; GO:0046100; P:hypoxanthine metabolic process; IMP:MGI.
DR GO; GO:0043103; P:hypoxanthine salvage; ISS:UniProtKB.
DR GO; GO:0046040; P:IMP metabolic process; ISS:UniProtKB.
DR GO; GO:0032264; P:IMP salvage; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0046651; P:lymphocyte proliferation; IMP:MGI.
DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; ISO:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; ISO:MGI.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IMP:MGI.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0021756; P:striatum development; IMP:MGI.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IMP:MGI.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR InterPro; IPR005904; Hxn_phspho_trans.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01203; HGPRTase; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Glycosyltransferase;
KW Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Purine salvage; Reference proteome; Transferase;
KW Ubl conjugation.
FT CHAIN 1..218
FT /note="Hypoxanthine-guanine phosphoribosyltransferase"
FT /id="PRO_0000139588"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 134..142
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 103
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27605"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P00492"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P00492"
FT CONFLICT 201
FT /note="D -> N (in Ref. 1; AAA96232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 24570 MW; 925CC0D4A6626E05 CRC64;
MPTRSPSVVI SDDEPGYDLD LFCIPNHYAE DLEKVFIPHG LIMDRTERLA RDVMKEMGGH
HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD
DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KQYSPKMVKV ASLLVKRTSR SVGYRPDFVG
FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA
