ID   HPRT_RAT                Reviewed;         218 AA.
AC   P27605; P70469; Q4KMC5; Q62926;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   24-JAN-2024, entry version 172.
DE   RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE            Short=HGPRT;
DE            Short=HGPRTase;
DE            EC=2.4.2.8 {ECO:0000250|UniProtKB:P00492};
GN   Name=Hprt1; Synonyms=Hprt;
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].
RX   PubMed=1783384; DOI=10.1016/0888-7543(91)90046-h;
RA   Chiaverotti T.A., Battula N., Monnat R.J. Jr.;
RT   "Rat hypoxanthine phosphoribosyltransferase cDNA cloning and sequence
RT   analysis.";
RL   Genomics 11:1158-1160(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1781355; DOI=10.1007/978-1-4615-7703-4_26;
RA   Chiaverotti T.A., Battula N., Monnat R.J. Jr.;
RT   "Rat hypoxanthine phosphoribosyltransferase cDNA cloning and sequence
RT   analysis.";
RL   Adv. Exp. Med. Biol. 309B:117-120(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1373820; DOI=10.1016/0027-5107(92)90178-5;
RA   Jansen J.G., Vrieling H., van Zeeland A.A., Mohn G.R.;
RT   "The gene encoding hypoxanthine-guanine phosphoribosyltransferase as target
RT   for mutational analysis: PCR cloning and sequencing of the cDNA from the
RT   rat.";
RL   Mutat. Res. 266:105-116(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Fischer 344; TISSUE=Spleen;
RX   PubMed=9691986; DOI=10.1016/s1383-5726(97)00014-9;
RA   Chen T., Mittelstaedt R.A., Heflich R.H.;
RT   "DNA sequence flanking the protein coding regions of the rat Hprt gene.";
RL   Mutat. Res. 382:79-80(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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   [6]
RP   PROTEIN SEQUENCE OF 35-45; 74-83; 92-101; 116-141; 157-166 AND 171-200, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-203.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=7526167; DOI=10.1016/0027-5107(94)90082-5;
RA   Mittelstaedt R.A., Heflich R.H.;
RT   "Analysis of in vivo mutation in exon 8 of the rat hprt gene.";
RL   Mutat. Res. 311:139-148(1994).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; M63983; AAA41350.1; -; mRNA.
DR   EMBL; S79292; AAB21288.1; -; mRNA.
DR   EMBL; X62085; CAA43997.1; -; mRNA.
DR   EMBL; AF001282; AAB65640.1; -; Genomic_DNA.
DR   EMBL; AF001278; AAB65640.1; JOINED; Genomic_DNA.
DR   EMBL; AF009655; AAB65640.1; JOINED; Genomic_DNA.
DR   EMBL; AF009656; AAB65640.1; JOINED; Genomic_DNA.
DR   EMBL; AF001279; AAB65640.1; JOINED; Genomic_DNA.
DR   EMBL; AF001280; AAB65640.1; JOINED; Genomic_DNA.
DR   EMBL; AF001281; AAB65640.1; JOINED; Genomic_DNA.
DR   EMBL; BC098629; AAH98629.1; -; mRNA.
DR   EMBL; U06049; AAA56887.1; -; Genomic_DNA.
DR   PIR; S18140; S18140.
DR   RefSeq; NP_036715.1; NM_012583.2.
DR   RefSeq; XP_008771881.1; XM_008773659.2.
DR   AlphaFoldDB; P27605; -.
DR   SMR; P27605; -.
DR   BioGRID; 246627; 1.
DR   IntAct; P27605; 2.
DR   STRING; 10116.ENSRNOP00000043388; -.
DR   iPTMnet; P27605; -.
DR   PhosphoSitePlus; P27605; -.
DR   SwissPalm; P27605; -.
DR   jPOST; P27605; -.
DR   PaxDb; 10116-ENSRNOP00000043388; -.
DR   Ensembl; ENSRNOT00000109953.1; ENSRNOP00000082017.1; ENSRNOG00000031367.5.
DR   Ensembl; ENSRNOT00055046621; ENSRNOP00055038259; ENSRNOG00055026943.
DR   Ensembl; ENSRNOT00060040585; ENSRNOP00060033544; ENSRNOG00060023239.
DR   Ensembl; ENSRNOT00065050123; ENSRNOP00065041178; ENSRNOG00065028933.
DR   GeneID; 24465; -.
DR   KEGG; rno:24465; -.
DR   AGR; RGD:2826; -.
DR   CTD; 3251; -.
DR   RGD; 2826; Hprt1.
DR   eggNOG; KOG3367; Eukaryota.
DR   GeneTree; ENSGT00940000155028; -.
DR   HOGENOM; CLU_073615_3_0_1; -.
DR   InParanoid; P27605; -.
DR   OrthoDB; 4216383at2759; -.
DR   PhylomeDB; P27605; -.
DR   TreeFam; TF313367; -.
DR   Reactome; R-RNO-74217; Purine salvage.
DR   Reactome; R-RNO-9748787; Azathioprine ADME.
DR   SABIO-RK; P27605; -.
DR   UniPathway; UPA00591; UER00648.
DR   PRO; PR:P27605; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000031367; Expressed in heart and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0046083; P:adenine metabolic process; ISO:RGD.
DR   GO; GO:0044209; P:AMP salvage; ISO:RGD.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR   GO; GO:0021954; P:central nervous system neuron development; ISO:RGD.
DR   GO; GO:0021895; P:cerebral cortex neuron differentiation; ISO:RGD.
DR   GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR   GO; GO:0042417; P:dopamine metabolic process; ISO:RGD.
DR   GO; GO:0071542; P:dopaminergic neuron differentiation; ISO:RGD.
DR   GO; GO:0046038; P:GMP catabolic process; ISS:UniProtKB.
DR   GO; GO:0032263; P:GMP salvage; ISO:RGD.
DR   GO; GO:0007625; P:grooming behavior; ISO:RGD.
DR   GO; GO:0006178; P:guanine salvage; ISS:UniProtKB.
DR   GO; GO:0046100; P:hypoxanthine metabolic process; IDA:RGD.
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; ISO:RGD.
DR   GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR   GO; GO:0046651; P:lymphocyte proliferation; ISO:RGD.
DR   GO; GO:0045964; P:positive regulation of dopamine metabolic process; ISO:RGD.
DR   GO; GO:0051289; P:protein homotetramerization; ISO:RGD.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; ISO:RGD.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; ISO:RGD.
DR   GO; GO:0001975; P:response to amphetamine; ISO:RGD.
DR   GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR   GO; GO:0021756; P:striatum development; ISO:RGD.
DR   GO; GO:0001913; P:T cell mediated cytotoxicity; ISO:RGD.
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   NCBIfam; TIGR01203; HGPRTase; 1.
DR   PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43340:SF6; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
DR   World-2DPAGE; 0004:P27605; -.
DR   Genevisible; P27605; RN.
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_0000139591"
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:0000250|UniProtKB:P00493"
FT   MOD_RES         142
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
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"
SQ   SEQUENCE   218 AA;  24477 MW;  2683FC1444FE0B5E CRC64;
     MSTLSPSVVI SDDEPGYDLD LFCIPNHYAE DLEKVFIPHG LIMDRTERLA RDVMKEMGGH
     HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD
     DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KQYSPKMVKV ASLLVKRTSR SVGYRPDFVG
     FEIPDKFVVG YALDYNEHFR DLNHVCVISE SGKAKYKA
//