APT_MOUSE
ID APT_MOUSE Reviewed; 180 AA.
AC P08030; Q564P4; Q61319; Q6PK77; Q9DCY3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 2.
DT 03-AUG-2022, entry version 164.
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|MGI:MGI:88061};
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=3921964; DOI=10.1073/pnas.82.9.2731;
RA Dush M.K., Sikela J.M., Khan S.A., Tischfield J.A., Stambrook P.J.;
RT "Nucleotide sequence and organization of the mouse adenine
RT phosphoribosyltransferase gene: presence of a coding region common to
RT animal and bacterial phosphoribosyltransferases that has a variable
RT intron/exon arrangement.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2731-2735(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Carcinoma;
RA Fujimori A.;
RT "mRNA aprt (wild-type allele) in murine SR-1 cell line.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-133.
RX PubMed=8433377; DOI=10.1007/bf02407304;
RA Turker M.S., Cooper G.E., Bishop P.L.;
RT "Region-specific rates of molecular evolution: a fourfold reduction in the
RT rate of accumulation of 'silent' mutations in transcribed versus
RT nontranscribed regions of homologous DNA fragments derived from two closely
RT related mouse species.";
RL J. Mol. Evol. 36:31-40(1993).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
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).
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; M11310; AAA37255.1; -; mRNA.
DR EMBL; AB033539; BAD95571.1; -; mRNA.
DR EMBL; AB033540; BAD95572.1; -; mRNA.
DR EMBL; AK002350; BAB22029.1; -; mRNA.
DR EMBL; AK153201; BAE31801.1; -; mRNA.
DR EMBL; AC114917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11692.1; -; Genomic_DNA.
DR EMBL; BC005667; AAH05667.1; -; mRNA.
DR EMBL; M86439; AAA37256.1; -; Genomic_DNA.
DR CCDS; CCDS40503.1; -.
DR PIR; A22670; RTMSA.
DR RefSeq; NP_033828.2; NM_009698.2.
DR AlphaFoldDB; P08030; -.
DR SMR; P08030; -.
DR BioGRID; 198168; 3.
DR IntAct; P08030; 2.
DR STRING; 10090.ENSMUSP00000006764; -.
DR iPTMnet; P08030; -.
DR PhosphoSitePlus; P08030; -.
DR SwissPalm; P08030; -.
DR EPD; P08030; -.
DR jPOST; P08030; -.
DR PaxDb; P08030; -.
DR PeptideAtlas; P08030; -.
DR PRIDE; P08030; -.
DR ProteomicsDB; 283170; -.
DR Antibodypedia; 17347; 353 antibodies from 32 providers.
DR DNASU; 11821; -.
DR Ensembl; ENSMUST00000006764; ENSMUSP00000006764; ENSMUSG00000006589.
DR GeneID; 11821; -.
DR KEGG; mmu:11821; -.
DR UCSC; uc009ntf.1; mouse.
DR CTD; 353; -.
DR MGI; MGI:88061; Aprt.
DR VEuPathDB; HostDB:ENSMUSG00000006589; -.
DR eggNOG; KOG1712; Eukaryota.
DR GeneTree; ENSGT00390000017259; -.
DR HOGENOM; CLU_063339_3_2_1; -.
DR InParanoid; P08030; -.
DR OMA; KPGIVFR; -.
DR OrthoDB; 1291050at2759; -.
DR PhylomeDB; P08030; -.
DR TreeFam; TF300227; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-74217; Purine salvage.
DR UniPathway; UPA00588; UER00646.
DR BioGRID-ORCS; 11821; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Aprt; mouse.
DR PRO; PR:P08030; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P08030; protein.
DR Bgee; ENSMUSG00000006589; Expressed in ectoplacental cone and 267 other tissues.
DR ExpressionAtlas; P08030; baseline and differential.
DR Genevisible; P08030; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0002055; F:adenine binding; IDA:MGI.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IDA:MGI.
DR GO; GO:0016208; F:AMP binding; ISO:MGI.
DR GO; GO:0046083; P:adenine metabolic process; IMP:MGI.
DR GO; GO:0006168; P:adenine salvage; IBA:GO_Central.
DR GO; GO:0044209; P:AMP salvage; IDA:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0032263; P:GMP salvage; IDA:MGI.
DR GO; GO:0007625; P:grooming behavior; IGI:MGI.
DR GO; GO:0032264; P:IMP salvage; IMP:MGI.
DR GO; GO:0007595; P:lactation; ISO:MGI.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IMP:MGI.
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; Glycosyltransferase; Phosphoprotein;
KW Purine salvage; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P36972"
FT CHAIN 2..180
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149506"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P36972"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 60
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07741"
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"
FT CONFLICT 6..7
FT /note="LK -> FE (in Ref. 3; BAB22029)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="S -> V (in Ref. 1; AAA37255)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="V -> A (in Ref. 3; BAB22029)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="L -> S (in Ref. 3; BAB22029)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="G -> A (in Ref. 3; BAB22029)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="K -> KVR (in Ref. 7; AAA37256)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="T -> I (in Ref. 2; BAD95572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 19724 MW; A6AE4DBE0B456E42 CRC64;
MSEPELKLVA RRIRSFPDFP IPGVLFRDIS PLLKDPDSFR ASIRLLASHL KSTHSGKIDY
IAGLDSRGFL FGPSLAQELG VGCVLIRKQG KLPGPTVSAS YSLEYGKAEL EIQKDALEPG
QRVVIVDDLL ATGGTMFAAC DLLHQLRAEV VECVSLVELT SLKGRERLGP IPFFSLLQYD
