AMPD1_MOUSE
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 03-AUG-2022, entry version 116.
DE RecName: Full=AMP deaminase 1;
DE EC=3.5.4.6;
DE AltName: Full=AMP deaminase isoform M;
DE AltName: Full=Myoadenylate deaminase;
GN Name=Ampd1;
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 -!- 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 -!- 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.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
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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; Q3V1D3; -.
DR PeptideAtlas; Q3V1D3; -.
DR PRIDE; Q3V1D3; -.
DR ProteomicsDB; 296350; -.
DR Antibodypedia; 33863; 268 antibodies from 31 providers.
DR Ensembl; ENSMUST00000090715; ENSMUSP00000088217; ENSMUSG00000070385.
DR GeneID; 229665; -.
DR KEGG; mmu:229665; -.
DR UCSC; uc008qso.1; mouse.
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; MYVYNDA; -.
DR OrthoDB; 49756at2759; -.
DR PhylomeDB; Q3V1D3; -.
DR TreeFam; TF300439; -.
DR Reactome; R-MMU-74217; Purine salvage.
DR UniPathway; UPA00591; UER00663.
DR BioGRID-ORCS; 229665; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q3V1D3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3V1D3; protein.
DR Bgee; ENSMUSG00000070385; Expressed in quadriceps femoris and 36 other tissues.
DR ExpressionAtlas; Q3V1D3; baseline and differential.
DR Genevisible; Q3V1D3; MM.
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 InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR029770; AMPD1.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR PANTHER; PTHR11359:SF1; PTHR11359:SF1; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
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
