AMPD2_MOUSE
ID AMPD2_MOUSE Reviewed; 798 AA.
AC Q9DBT5; A2AE28; Q91YI2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=AMP deaminase 2;
DE EC=3.5.4.6 {ECO:0000305|PubMed:23911318};
DE AltName: Full=AMP deaminase isoform L;
GN Name=Ampd2;
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, 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].
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-64, 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-87 AND SER-109, 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-87, 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-87 AND SER-109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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-18, 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 + 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: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 -!- 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; -.
DR RefSeq; NP_001276648.1; NM_001289719.1.
DR RefSeq; NP_001276649.1; NM_001289720.1.
DR RefSeq; NP_083055.1; NM_028779.5.
DR AlphaFoldDB; Q9DBT5; -.
DR SMR; Q9DBT5; -.
DR BioGRID; 224949; 6.
DR IntAct; Q9DBT5; 3.
DR MINT; Q9DBT5; -.
DR STRING; 10090.ENSMUSP00000099698; -.
DR iPTMnet; Q9DBT5; -.
DR PhosphoSitePlus; Q9DBT5; -.
DR SwissPalm; Q9DBT5; -.
DR EPD; Q9DBT5; -.
DR jPOST; Q9DBT5; -.
DR MaxQB; Q9DBT5; -.
DR PaxDb; Q9DBT5; -.
DR PeptideAtlas; Q9DBT5; -.
DR PRIDE; Q9DBT5; -.
DR ProteomicsDB; 296205; -.
DR Antibodypedia; 33766; 229 antibodies from 31 providers.
DR DNASU; 109674; -.
DR Ensembl; ENSMUST00000102637; ENSMUSP00000099697; ENSMUSG00000027889.
DR Ensembl; ENSMUST00000102638; ENSMUSP00000099698; ENSMUSG00000027889.
DR GeneID; 109674; -.
DR KEGG; mmu:109674; -.
DR UCSC; uc008qxz.2; mouse.
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; ESPPYSY; -.
DR OrthoDB; 49756at2759; -.
DR TreeFam; TF300439; -.
DR Reactome; R-MMU-74217; Purine salvage.
DR UniPathway; UPA00591; UER00663.
DR BioGRID-ORCS; 109674; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Ampd2; mouse.
DR PRO; PR:Q9DBT5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9DBT5; protein.
DR Bgee; ENSMUSG00000027889; Expressed in bone fossa and 248 other tissues.
DR ExpressionAtlas; Q9DBT5; baseline and differential.
DR Genevisible; Q9DBT5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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: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 InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR029749; AMPD2.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR PANTHER; PTHR11359:SF3; PTHR11359:SF3; 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; Methylation; Nucleotide metabolism;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..798
FT /note="AMP deaminase 2"
FT /id="PRO_0000194408"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 629
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 409..414
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 610
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 685..688
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 18
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01433"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01433"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01433"
FT MOD_RES 64
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01433"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01433"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01433"
SQ SEQUENCE 798 AA; 92024 MW; 2BC4F37E4006C7D5 CRC64;
MASEARSGLG ASPLQSARSL PGNAPCLKHF PLDLRTSMDG KCKEIAEELF SRSLAESELR
SAPYEFPEES PIEQLEERRQ RLERQISQDV KLEPDILLRA KQDFLKTDSD SDLQLYKEQG
EGQGDRGLWE RDVVLEREFQ RVIISGEEKC GVPFTDLLDA AKSVVRALFI REKYMALSLQ
SFCPTTRRYL QQLAEKPLET RTYEQSPDTP VSADAPVHPP ALEQHPYEHC EPSAMPGDLG
LGLRMVRGVV HVYTRRDPDE HCPEVELPYP DLQEFVADVN VLMALIINGP IKSFCYRRLQ
YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL LRFIKRAMKR
HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD RNTFHRFDKF NAKYNPIGES
VLREIFIKTD NKISGKYFAH IIKEVMADLE ESKYQNAELR LSIYGRSRDE WDKLARWAVN
HKVHSPNVRW LVQVPRLFDV YRTKGQLANF QEMLENIFLP LFEATVHPAS HPELHLFLEH
VDGFDSVDDE SKPENHVFNL ESPLPEAWVE EDNPPYAYYL YYTFANMAML NHLRRQRGFH
TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ YLYYLAQIGI AMSPLSNNSL
FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY SIATQVWKLS SCDMCELARN
SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI RRTNVPDIRV GYRYETLCQE LALITQAVQS
EMLETIPEEV GIVMSPGP
