HPRT_RAT
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 03-AUG-2022, entry version 164.
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 World-2DPAGE; 0004:P27605; -.
DR jPOST; P27605; -.
DR PaxDb; P27605; -.
DR PRIDE; P27605; -.
DR Ensembl; ENSRNOT00000109953; ENSRNOP00000082017; ENSRNOG00000031367.
DR GeneID; 24465; -.
DR KEGG; rno:24465; -.
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 OMA; TMDWMAV; -.
DR OrthoDB; 1537610at2759; -.
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 tissues.
DR Genevisible; P27605; RN.
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:0007420; P:brain development; IEP: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: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 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_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
