ID   AMPD2_MOUSE             Reviewed;         824 AA.
AC   Q9DBT5; A2AE27; A2AE28; Q91YI2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2023, sequence version 2.
DT   02-SEP-2026, entry version 171.
DE   RecName: Full=AMP deaminase 2 {ECO:0000305};
DE            EC=3.5.4.6 {ECO:0000305|PubMed:23911318};
DE   AltName: Full=AMP deaminase isoform L;
GN   Name=Ampd2 {ECO:0000312|MGI:MGI:88016};
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-90, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-135, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-135, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, 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).
RN   [8]
RP   DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=23911318; DOI=10.1016/j.cell.2013.07.005;
RA   Akizu N., Cantagrel V., Schroth J., Cai N., Vaux K., McCloskey D.,
RA   Naviaux R.K., Van Vleet J., Fenstermaker A.G., Silhavy J.L., Scheliga J.S.,
RA   Toyama K., Morisaki H., Sonmez F.M., Celep F., Oraby A., Zaki M.S.,
RA   Al-Baradie R., Faqeih E.A., Saleh M.A., Spencer E., Rosti R.O., Scott E.,
RA   Nickerson E., Gabriel S., Morisaki T., Holmes E.W., Gleeson J.G.;
RT   "AMPD2 regulates GTP synthesis and is mutated in a potentially treatable
RT   neurodegenerative brainstem disorder.";
RL   Cell 154:505-517(2013).
RN   [9]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-44, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism.
CC       Catalyzes the deamination of AMP to IMP and plays an important role in
CC       the purine nucleotide cycle. {ECO:0000269|PubMed:23911318}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + H2O + H(+) = 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:0000305|PubMed:23911318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778;
CC         Evidence={ECO:0000305|PubMed:23911318};
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:0000305|PubMed:23911318}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2;
CC         IsoId=Q9DBT5-2; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q9DBT5-1; Sequence=VSP_061947;
CC   -!- DISRUPTION PHENOTYPE: Mice have normal brain histology.
CC       {ECO:0000269|PubMed:23911318}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16662.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK004759; BAB23540.1; -; mRNA.
DR   EMBL; AK169980; BAE41495.1; -; mRNA.
DR   EMBL; AL671854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016662; AAH16662.2; ALT_INIT; mRNA.
DR   EMBL; BC049119; AAH49119.1; -; mRNA.
DR   CCDS; CCDS17749.1; -. [Q9DBT5-1]
DR   CCDS; CCDS84663.1; -. [Q9DBT5-2]
DR   RefSeq; NP_001276648.1; NM_001289719.1. [Q9DBT5-1]
DR   RefSeq; NP_001276649.1; NM_001289720.1.
DR   RefSeq; NP_001333594.1; NM_001346665.1. [Q9DBT5-2]
DR   RefSeq; NP_083055.1; NM_028779.5. [Q9DBT5-1]
DR   AlphaFoldDB; Q9DBT5; -.
DR   SMR; Q9DBT5; -.
DR   BioGRID; 224949; 9.
DR   FunCoup; Q9DBT5; 2270.
DR   IntAct; Q9DBT5; 3.
DR   MINT; Q9DBT5; -.
DR   STRING; 10090.ENSMUSP00000077946; -.
DR   BindingDB; Q9DBT5; -.
DR   ChEMBL; CHEMBL5291580; -.
DR   iPTMnet; Q9DBT5; -.
DR   PhosphoSitePlus; Q9DBT5; -.
DR   SwissPalm; Q9DBT5; -.
DR   jPOST; Q9DBT5; -.
DR   PaxDb; 10090-ENSMUSP00000077946; -.
DR   PeptideAtlas; Q9DBT5; -.
DR   ProteomicsDB; 296205; -.
DR   ProteomicsDB; 334451; -.
DR   Pumba; Q9DBT5; -.
DR   Antibodypedia; 33766; 225 antibodies from 33 providers.
DR   DNASU; 109674; -.
DR   Ensembl; ENSMUST00000078912.7; ENSMUSP00000077946.6; ENSMUSG00000027889.18. [Q9DBT5-2]
DR   Ensembl; ENSMUST00000102637.8; ENSMUSP00000099697.2; ENSMUSG00000027889.18. [Q9DBT5-1]
DR   Ensembl; ENSMUST00000102638.8; ENSMUSP00000099698.2; ENSMUSG00000027889.18. [Q9DBT5-1]
DR   GeneID; 109674; -.
DR   KEGG; mmu:109674; -.
DR   UCSC; uc008qxz.2; mouse. [Q9DBT5-2]
DR   AGR; MGI:88016; -.
DR   CTD; 271; -.
DR   MGI; MGI:88016; Ampd2.
DR   VEuPathDB; HostDB:ENSMUSG00000027889; -.
DR   eggNOG; KOG1096; Eukaryota.
DR   GeneTree; ENSGT00950000183011; -.
DR   HOGENOM; CLU_003782_4_0_1; -.
DR   InParanoid; Q9DBT5; -.
DR   OMA; FHRKFPY; -.
DR   OrthoDB; 1723809at2759; -.
DR   Reactome; R-MMU-74217; Purine salvage.
DR   UniPathway; UPA00591; UER00663.
DR   BioGRID-ORCS; 109674; 5 hits in 77 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:Q9DBT5; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9DBT5; protein.
DR   Bgee; ENSMUSG00000027889; Expressed in bone fossa and 251 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0003876; F:AMP deaminase activity; IMP:CACAO.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0046033; P:AMP metabolic process; IMP:CACAO.
DR   GO; GO:0046034; P:ATP metabolic process; IMP:CACAO.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR   GO; GO:0052652; P:cyclic purine nucleotide metabolic process; ISS:UniProtKB.
DR   GO; GO:0097009; P:energy homeostasis; IMP:MGI.
DR   GO; GO:0032263; P:GMP salvage; ISO:MGI.
DR   GO; GO:0046039; P:GTP metabolic process; IMP:CACAO.
DR   GO; GO:0006188; P:IMP biosynthetic process; IMP:MGI.
DR   GO; GO:0032264; P:IMP salvage; IMP:MGI.
DR   GO; GO:0009117; P:nucleotide metabolic process; IMP:MGI.
DR   GO; GO:0072015; P:podocyte development; IMP:MGI.
DR   CDD; cd01319; AMPD; 1.
DR   FunFam; 4.10.800.20:FF:000001; AMP deaminase; 1.
DR   FunFam; 3.20.20.140:FF:000035; Probable amp deaminase; 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:SF3; AMP DEAMINASE 2; 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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Metal-binding; Methylation;
KW   Nucleotide metabolism; Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..824
FT                   /note="AMP deaminase 2"
FT                   /id="PRO_0000194408"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..20
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        655
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT   BINDING         364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         435..440
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         633
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         636
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         710
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         711..714
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         44
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01433"
FT   MOD_RES         63
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01433"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01433"
FT   MOD_RES         90
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01433"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         133
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01433"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01433"
FT   VAR_SEQ         1..29
FT                   /note="MASYPGPGKSKAKYPFKKRAGLQASAAAP -> MAS (in isoform 1)"
FT                   /id="VSP_061947"
SQ   SEQUENCE   824 AA;  94696 MW;  1A0FBC58523C42A4 CRC64;
     MASYPGPGKS KAKYPFKKRA GLQASAAAPE ARSGLGASPL QSARSLPGNA PCLKHFPLDL
     RTSMDGKCKE IAEELFSRSL AESELRSAPY EFPEESPIEQ LEERRQRLER QISQDVKLEP
     DILLRAKQDF LKTDSDSDLQ LYKEQGEGQG DRGLWERDVV LEREFQRVII SGEEKCGVPF
     TDLLDAAKSV VRALFIREKY MALSLQSFCP TTRRYLQQLA EKPLETRTYE QSPDTPVSAD
     APVHPPALEQ HPYEHCEPSA MPGDLGLGLR MVRGVVHVYT RRDPDEHCPE VELPYPDLQE
     FVADVNVLMA LIINGPIKSF CYRRLQYLSS KFQMHVLLNE MKELAAQKKV PHRDFYNIRK
     VDTHIHASSC MNQKHLLRFI KRAMKRHLEE IVHVEQGREQ TLREVFESMN LTAYDLSVDT
     LDVHADRNTF HRFDKFNAKY NPIGESVLRE IFIKTDNKIS GKYFAHIIKE VMADLEESKY
     QNAELRLSIY GRSRDEWDKL ARWAVNHKVH SPNVRWLVQV PRLFDVYRTK GQLANFQEML
     ENIFLPLFEA TVHPASHPEL HLFLEHVDGF DSVDDESKPE NHVFNLESPL PEAWVEEDNP
     PYAYYLYYTF ANMAMLNHLR RQRGFHTFVL RPHCGEAGPI HHLVSAFMLA ENISHGLLLR
     KAPVLQYLYY LAQIGIAMSP LSNNSLFLSY HRNPLPEYLS RGLMVSLSTD DPLQFHFTKE
     PLMEEYSIAT QVWKLSSCDM CELARNSVLM SGFSHKVKSH WLGPNYTKEG PEGNDIRRTN
     VPDIRVGYRY ETLCQELALI TQAVQSEMLE TIPEEVGIVM SPGP
//