ID   AMPD1_MOUSE             Reviewed;         745 AA.
AC   Q3V1D3; F8VPY9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 2.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=AMP deaminase 1 {ECO:0000305};
DE            EC=3.5.4.6 {ECO:0000250|UniProtKB:P23109};
DE   AltName: Full=AMP deaminase isoform M;
DE   AltName: Full=Myoadenylate deaminase;
GN   Name=Ampd1 {ECO:0000312|MGI:MGI:88015};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
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   [2]
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue;
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: AMP deaminase plays a critical role in energy metabolism.
CC       {ECO:0000250|UniProtKB:P23109}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6;
CC         Evidence={ECO:0000250|UniProtKB:P23109};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778;
CC         Evidence={ECO:0000250|UniProtKB:P23109};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from AMP: step 1/1. {ECO:0000250|UniProtKB:P23109}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK132524; BAE21218.1; -; mRNA.
DR   EMBL; AC150894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC163297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS38571.1; -.
DR   RefSeq; NP_001028475.2; NM_001033303.2.
DR   AlphaFoldDB; Q3V1D3; -.
DR   SMR; Q3V1D3; -.
DR   BioGRID; 230879; 3.
DR   IntAct; Q3V1D3; 1.
DR   STRING; 10090.ENSMUSP00000088217; -.
DR   BindingDB; Q3V1D3; -.
DR   iPTMnet; Q3V1D3; -.
DR   PhosphoSitePlus; Q3V1D3; -.
DR   MaxQB; Q3V1D3; -.
DR   PaxDb; 10090-ENSMUSP00000088217; -.
DR   PeptideAtlas; Q3V1D3; -.
DR   ProteomicsDB; 296350; -.
DR   Antibodypedia; 33863; 311 antibodies from 31 providers.
DR   Ensembl; ENSMUST00000090715.13; ENSMUSP00000088217.7; ENSMUSG00000070385.13.
DR   GeneID; 229665; -.
DR   KEGG; mmu:229665; -.
DR   UCSC; uc008qso.1; mouse.
DR   AGR; MGI:88015; -.
DR   CTD; 270; -.
DR   MGI; MGI:88015; Ampd1.
DR   VEuPathDB; HostDB:ENSMUSG00000070385; -.
DR   eggNOG; KOG1096; Eukaryota.
DR   GeneTree; ENSGT00950000183011; -.
DR   HOGENOM; CLU_003782_4_0_1; -.
DR   InParanoid; Q3V1D3; -.
DR   OMA; HHEMQEH; -.
DR   OrthoDB; 20951at2759; -.
DR   PhylomeDB; Q3V1D3; -.
DR   TreeFam; TF300439; -.
DR   Reactome; R-MMU-74217; Purine salvage.
DR   UniPathway; UPA00591; UER00663.
DR   BioGRID-ORCS; 229665; 4 hits in 76 CRISPR screens.
DR   PRO; PR:Q3V1D3; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q3V1D3; Protein.
DR   Bgee; ENSMUSG00000070385; Expressed in quadriceps femoris and 37 other cell types or tissues.
DR   ExpressionAtlas; Q3V1D3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003876; F:AMP deaminase activity; IMP:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032036; F:myosin heavy chain binding; ISO:MGI.
DR   GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR   GO; GO:0032263; P:GMP salvage; ISO:MGI.
DR   GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032264; P:IMP salvage; IMP:MGI.
DR   GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR   CDD; cd01319; AMPD; 1.
DR   Gene3D; 4.10.800.20; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR006329; AMPD.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01429; AMP_deaminase; 1.
DR   PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR   PANTHER; PTHR11359:SF1; AMP DEAMINASE 1; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
DR   Genevisible; Q3V1D3; MM.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Nucleotide metabolism; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   CHAIN           1..745
FT                   /note="AMP deaminase 1"
FT                   /id="PRO_0000269718"
FT   ACT_SITE        592
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         570
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         573
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         647
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         648..651
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         79
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10759"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10759"
FT   MOD_RES         214
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P10759"
FT   MOD_RES         439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10759"
FT   CONFLICT        226
FT                   /note="E -> D (in Ref. 1; BAE21218)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        534
FT                   /note="E -> G (in Ref. 1; BAE21218)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   745 AA;  86105 MW;  4595A57908A13239 CRC64;
     MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS LHEMQAHIFH
     MENLSMDGRR KRRFQGRKTV NLSIPQSETS STKLSHIEEF ISSSPTYESV PDFQRVQITG
     DYASGVTVED FEVVCKGLYR ALCIREKYMQ KSFQRFPKTP SKYLRNIDGE ALVGNESFYP
     VFTPPPKKGE DPFRTEDLPA NLGYHLKMKA GVIYIYPDEA AANRDEPKPY PYPNLDDFLD
     DMNFLLALIA QGPVKTYAHR RLKFLSSKFQ VHQMLNEMDE LKELKNNPHR DFYNCRKVDT
     HIHAAACMNQ KHLLRFIKKS YHIDADRVVY STKEKSLTLK ELFAKLNMHP YDLTVDSLDV
     HAGRQTFQRF DKFNDKYNPV GASELRDLYL KTDNYINGEY FATIIKEVGA DLVEAKYQHA
     EPRLSIYGRS PDEWNKLSSW FVCNRIYCPN MTWMIQVPRI YDVFRSKNFL PHFGKMLENI
     FLPVFEATIN PQAHPDLSVF LKHITGFDSV DDESKHSGHM FSSKSPKPEE WTMENNPSYT
     YYAYYMYANI TVLNSLRKER GMNTFLFRPH CGEAGALTHL MTAFMIADNI SHGLNLKKSP
     VLQYLFFLAQ IPIAMSPLSN NSLFLEYAKN PFLDFLQKGL MISLSTDDPM QFHFTKEPLM
     EEYAIAAQVF KLSTCDMCEV ARNSVLQCGI SHEEKAKFLG NNYLEEGPVG NDIRRTNVAQ
     IRMAYRYETW CYELNLIAEG LKATE
//