APT_RAT
ID APT_RAT Reviewed; 180 AA.
AC P36972;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000305};
DE Short=APRT;
DE EC=2.4.2.7 {ECO:0000250|UniProtKB:P07741};
GN Name=Aprt {ECO:0000312|RGD:1307758};
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 [GENOMIC DNA].
RX PubMed=8112572; DOI=10.1139/g93-147;
RA Fieldhouse D., Golding G.B.;
RT "The rat adenine phosphoribosyltransferase sequence shows evolutionary rate
RT variation among exons in rodents.";
RL Genome 36:1107-1110(1993).
RN [2]
RP PROTEIN SEQUENCE OF 15-34; 58-87; 92-107 AND 123-163, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-30 AND SER-66, AND
RP IDENTIFICATION BY 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: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC {ECO:0000250|UniProtKB:P07741}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate +
CC adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7;
CC Evidence={ECO:0000250|UniProtKB:P07741};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000250|UniProtKB:P07741}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; L04970; AAA40757.1; -; Genomic_DNA.
DR RefSeq; NP_001013079.1; NM_001013061.1.
DR AlphaFoldDB; P36972; -.
DR SMR; P36972; -.
DR BioGRID; 253751; 1.
DR IntAct; P36972; 7.
DR MINT; P36972; -.
DR STRING; 10116.ENSRNOP00000061449; -.
DR iPTMnet; P36972; -.
DR PhosphoSitePlus; P36972; -.
DR jPOST; P36972; -.
DR PaxDb; P36972; -.
DR PRIDE; P36972; -.
DR GeneID; 292072; -.
DR KEGG; rno:292072; -.
DR UCSC; RGD:1307758; rat.
DR CTD; 353; -.
DR RGD; 1307758; Aprt.
DR VEuPathDB; HostDB:ENSRNOG00000014405; -.
DR eggNOG; KOG1712; Eukaryota.
DR HOGENOM; CLU_063339_3_2_1; -.
DR InParanoid; P36972; -.
DR OMA; KPGIVFR; -.
DR OrthoDB; 1291050at2759; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-74217; Purine salvage.
DR SABIO-RK; P36972; -.
DR UniPathway; UPA00588; UER00646.
DR PRO; PR:P36972; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000014405; Expressed in duodenum and 18 other tissues.
DR Genevisible; P36972; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0002055; F:adenine binding; ISO:RGD.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016208; F:AMP binding; IDA:RGD.
DR GO; GO:0046083; P:adenine metabolic process; ISO:RGD.
DR GO; GO:0006168; P:adenine salvage; IBA:GO_Central.
DR GO; GO:0044209; P:AMP salvage; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0032263; P:GMP salvage; ISO:RGD.
DR GO; GO:0007625; P:grooming behavior; ISO:RGD.
DR GO; GO:0032264; P:IMP salvage; ISO:RGD.
DR GO; GO:0007595; P:lactation; IDA:RGD.
DR GO; GO:0006166; P:purine ribonucleoside salvage; ISO:RGD.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR InterPro; IPR005764; Ade_phspho_trans.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01090; apt; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Glycosyltransferase;
KW Phosphoprotein; Purine salvage; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..180
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149509"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 60
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
SQ SEQUENCE 180 AA; 19546 MW; D5563374DDEBB3EA CRC64;
MSESELQLVA RRIRSFPDFP IPGVLFRDIS PLLKDPDSFR ASIRLLAGHL KSTHGGKIDY
IAGLDSRGFL FGPSLAQELG VGCVLIRKRG KLPGPTVSAS YSLEYGKAEL EIQKDALEPG
QKVVIVDDLL ATGGTMCAAC ELLSQLRAEV VECVSLVELT SLKGREKLGP VPFFSLLQYE
