ID   HPRT_CANFA              Reviewed;         218 AA.
AC   Q6WIT9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-JUL-2012, entry version 55.
DE   RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE            Short=HGPRT;
DE            Short=HGPRTase;
DE            EC=2.4.2.8;
GN   Name=HPRT1; Synonyms=HPRT;
OS   Canis familiaris (Dog) (Canis lupus familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15113653; DOI=10.1016/j.vetimm.2004.01.008;
RA   Johnson C.M., Yang S., Sellins K.S., Frank G.R.;
RT   "Selection of HPRT primers as controls for determination of mRNA
RT   expression in dogs by RT-PCR.";
RL   Vet. Immunol. Immunopathol. 99:47-51(2004).
CC   -!- FUNCTION: Converts guanine to guanosine monophosphate, and
CC       hypoxanthine to inosine monophosphate. Transfers the 5-
CC       phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the
CC       purine. Plays a central role in the generation of purine
CC       nucleotides through the purine salvage pathway (By similarity).
CC   -!- CATALYTIC ACTIVITY: IMP + diphosphate = hypoxanthine + 5-phospho-
CC       alpha-D-ribose 1-diphosphate.
CC   -!- CATALYTIC ACTIVITY: GMP + diphosphate = guanine + 5-phospho-alpha-
CC       D-ribose 1-diphosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit. The magnesium ions
CC       are essentially bound to the substrate and have few direct
CC       interactions with the protein (By similarity).
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC       IMP from hypoxanthine: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family.
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DR   EMBL; AY283372; AAQ21102.1; -; mRNA.
DR   RefSeq; NP_001003357.1; NM_001003357.1.
DR   UniGene; Cfa.4551; -.
DR   ProteinModelPortal; Q6WIT9; -.
DR   SMR; Q6WIT9; 5-218.
DR   STRING; Q6WIT9; -.
DR   GeneID; 442945; -.
DR   KEGG; cfa:442945; -.
DR   CTD; 3251; -.
DR   eggNOG; COG0634; -.
DR   HOGENOM; HOG000236521; -.
DR   HOVERGEN; HBG000242; -.
DR   InParanoid; Q6WIT9; -.
DR   KO; K00760; -.
DR   OrthoDB; EOG4H72CM; -.
DR   NextBio; 20831615; -.
DR   GO; GO:0005829; C:cytosol; IBA:RefGenome.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006168; P:adenine salvage; IBA:RefGenome.
DR   GO; GO:0007610; P:behavior; ISS:UniProtKB.
DR   GO; GO:0021954; P:central nervous system neuron development; IEA:Compara.
DR   GO; GO:0021895; P:cerebral cortex neuron differentiation; IEA:Compara.
DR   GO; GO:0019835; P:cytolysis; IEA:Compara.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:Compara.
DR   GO; GO:0042417; P:dopamine metabolic process; IEA:Compara.
DR   GO; GO:0046038; P:GMP catabolic process; ISS:UniProtKB.
DR   GO; GO:0032263; P:GMP salvage; IBA:RefGenome.
DR   GO; GO:0007625; P:grooming behavior; IEA:Compara.
DR   GO; GO:0006178; P:guanine salvage; ISS:UniProtKB.
DR   GO; GO:0043103; P:hypoxanthine salvage; ISS:UniProtKB.
DR   GO; GO:0032264; P:IMP salvage; IBA:RefGenome.
DR   GO; GO:0046651; P:lymphocyte proliferation; IEA:Compara.
DR   GO; GO:0045964; P:positive regulation of dopamine metabolic process; ISS:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; ISS:UniProtKB.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Compara.
DR   GO; GO:0021756; P:striatum development; IEA:Compara.
DR   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   TIGRFAMs; TIGR01203; HGPRTase; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; Glycosyltransferase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine salvage; Reference proteome;
KW   Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    218       Hypoxanthine-guanine
FT                                phosphoribosyltransferase.
FT                                /FTId=PRO_0000139583.
FT   NP_BIND     134    142       GMP (By similarity).
FT   NP_BIND     186    188       GMP (By similarity).
FT   ACT_SITE    138    138       Proton acceptor (By similarity).
FT   METAL       194    194       Magnesium (By similarity).
FT   BINDING      69     69       GMP (By similarity).
FT   BINDING     166    166       GMP (By similarity).
FT   BINDING     194    194       GMP; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   218 AA;  24438 MW;  E6F1CC8CC6FDF52F CRC64;
     MATRSLGVVI SDDEPGYDLD LFCIPHHYAE DLEKVFIPHG LIMDRTERLA RDVMKEMGGH
     HIVALCVLKG GYKFFADLLD YIKALNRNSD GSIPMTVDFI RLKSYCNDQS TGDIKVIGGD
     DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KEHNPKMVKV ASLLVKRTPR SVGYKPDFVG
     FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA
//