ID AMPD3_HUMAN Reviewed; 767 AA. AC Q01432; A0AUX0; B7Z2S2; B7Z763; B7Z877; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 24-JAN-2024, entry version 203. DE RecName: Full=AMP deaminase 3 {ECO:0000305|PubMed:9291127}; DE EC=3.5.4.6 {ECO:0000269|PubMed:9291127}; DE AltName: Full=AMP deaminase isoform E; DE AltName: Full=Erythrocyte AMP deaminase; GN Name=AMPD3 {ECO:0000312|HGNC:HGNC:470}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1B). RX PubMed=1420359; DOI=10.1016/0167-4781(92)90153-q; RA Yamada Y., Goto H., Ogasawara N.; RT "Cloning and nucleotide sequence of the cDNA encoding human erythrocyte- RT specific AMP deaminase."; RL Biochim. Biophys. Acta 1171:125-128(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C). RC TISSUE=Keratinocyte; RX PubMed=1400401; DOI=10.1016/s0021-9258(19)36768-7; RA Mahnke-Zizelman D.K., Sabina R.L.; RT "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD RT gene exhibiting alternatively spliced 5'-exons."; RL J. Biol. Chem. 267:20866-20877(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1B; 2 AND 3), AND ALTERNATIVE RP SPLICING. RX PubMed=8611627; DOI=10.1016/0167-4781(95)00231-6; RA Mahnke-Zizelman D.K., Eddy R., Shows T.B., Sabina R.L.; RT "Characterization of the human AMPD3 gene reveals that 5' exon useage is RT subject to transcriptional control by three tandem promoters and RT alternative splicing."; RL Biochim. Biophys. Acta 1306:75-92(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1B), AND VARIANT AMPDDE CYS-573. RX PubMed=8004104; DOI=10.1093/hmg/3.2.331; RA Yamada Y., Goto H., Ogasawara N.; RT "A point mutation responsible for human erythrocyte AMP deaminase RT deficiency."; RL Hum. Mol. Genet. 3:331-334(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1B; 2; 3 AND 4). RC TISSUE=Brain, Synovium, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [9] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RC TISSUE=Heart; RX PubMed=9291127; DOI=10.1042/bj3260521; RA Mahnke-Zizelman D.K., D'Cunha J., Wojnar J.M., Brogley M.A., Sabina R.L.; RT "Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal RT muscle fibre type."; RL Biochem. J. 326:521-529(1997). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP VARIANTS AMPDDE LYS-310; VAL-320; THR-324; CYS-331; CYS-402; ARG-450 AND RP LEU-585. RX PubMed=7881427; DOI=10.1093/hmg/3.12.2243; RA Yamada Y., Goto H., Murase T., Ogasawara N.; RT "Molecular basis for human erythrocyte AMP deaminase deficiency: screening RT for the major point mutation and identification of other mutations."; RL Hum. Mol. Genet. 3:2243-2245(1994). RN [13] RP VARIANT AMPDDE LEU-311. RX PubMed=9598089; DOI=10.1007/978-1-4615-5381-6_69; RA Yamada Y., Makarewicz W., Goto H., Nomura N., Kitoh H., Ogasawara N.; RT "Gene mutations responsible for human erythrocyte AMP deaminase deficiency RT in Poles."; RL Adv. Exp. Med. Biol. 431:347-350(1998). RN [14] RP VARIANTS AMPDDE ARG-450 AND PRO-712. RX PubMed=11139257; DOI=10.1002/1098-1004(2001)17:1<78::aid-humu21>3.0.co;2-b; RA Yamada Y., Goto H., Wakamatsu N., Ogasawara N.; RT "A rare case of complete human erythrocyte AMP deaminase deficiency due to RT two novel missense mutations in AMPD3."; RL Hum. Mutat. 17:78-78(2001). CC -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism. CC {ECO:0000305|PubMed:9291127}. 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:0000269|PubMed:9291127}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778; CC Evidence={ECO:0000305|PubMed:9291127}; 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:9291127}. CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC Q01432; P08238: HSP90AB1; NbExp=2; IntAct=EBI-1223554, EBI-352572; CC Q01432-4; P23109: AMPD1; NbExp=3; IntAct=EBI-11955621, EBI-2959675; CC Q01432-4; Q9NZI2-2: KCNIP1; NbExp=3; IntAct=EBI-11955621, EBI-22452746; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1B; CC IsoId=Q01432-1; Sequence=Displayed; CC Name=1A; CC IsoId=Q01432-2; Sequence=VSP_001275, VSP_001277; CC Name=1C; CC IsoId=Q01432-3; Sequence=VSP_001276, VSP_001278; CC Name=2; CC IsoId=Q01432-4; Sequence=VSP_001275; CC Name=3; CC IsoId=Q01432-5; Sequence=VSP_001276; CC Name=4; CC IsoId=Q01432-6; Sequence=VSP_044230; CC -!- DISEASE: Adenosine monophosphate deaminase deficiency erythrocyte type CC (AMPDDE) [MIM:612874]: A metabolic disorder due to lack of activity of CC the erythrocyte isoform of AMP deaminase. It is a clinically CC asymptomatic condition characterized by a 50% increase in steady-state CC levels of ATP in affected cells. Individuals with complete deficiency CC of erythrocyte AMP deaminase are healthy and have no hematologic CC disorders. {ECO:0000269|PubMed:11139257, ECO:0000269|PubMed:7881427, CC ECO:0000269|PubMed:8004104, ECO:0000269|PubMed:9598089}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. 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; D12775; BAA02240.1; -; mRNA. DR EMBL; M84720; AAA58365.1; -; mRNA. DR EMBL; M84721; AAA58366.1; -; mRNA. DR EMBL; M84722; AAA58367.1; -; mRNA. DR EMBL; U29926; AAB60410.1; -; Genomic_DNA. DR EMBL; U29929; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29907; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29909; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29910; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29911; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29916; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29917; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29918; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29922; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29924; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29925; AAB60410.1; JOINED; Genomic_DNA. DR EMBL; U29926; AAB60408.1; -; Genomic_DNA. DR EMBL; U29912; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29929; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29907; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29909; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29910; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29911; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29916; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29917; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29918; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29922; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29924; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29925; AAB60408.1; JOINED; Genomic_DNA. DR EMBL; U29926; AAB60409.1; -; Genomic_DNA. DR EMBL; U29927; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29929; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29907; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29909; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29910; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29911; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29916; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29917; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29918; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29922; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29924; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; U29925; AAB60409.1; JOINED; Genomic_DNA. DR EMBL; D31646; BAA06505.1; -; Genomic_DNA. DR EMBL; AK289998; BAF82687.1; -; mRNA. DR EMBL; AK295046; BAH11958.1; -; mRNA. DR EMBL; AK301507; BAH13499.1; -; mRNA. DR EMBL; AK302970; BAH13863.1; -; mRNA. DR EMBL; AC084117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW68567.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68568.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68569.1; -; Genomic_DNA. DR EMBL; BC126118; AAI26119.1; -; mRNA. DR CCDS; CCDS41617.1; -. [Q01432-1] DR CCDS; CCDS44537.1; -. [Q01432-5] DR CCDS; CCDS53601.1; -. [Q01432-6] DR CCDS; CCDS7802.1; -. [Q01432-4] DR PIR; S68146; S68146. DR PIR; S68147; S68147. DR RefSeq; NP_000471.1; NM_000480.2. [Q01432-4] DR RefSeq; NP_001020560.1; NM_001025389.1. [Q01432-1] DR RefSeq; NP_001020561.1; NM_001025390.1. [Q01432-5] DR RefSeq; NP_001165901.1; NM_001172430.1. [Q01432-1] DR RefSeq; NP_001165902.1; NM_001172431.1. [Q01432-6] DR AlphaFoldDB; Q01432; -. DR SMR; Q01432; -. DR BioGRID; 106769; 15. DR ELM; Q01432; -. DR IntAct; Q01432; 8. DR STRING; 9606.ENSP00000379802; -. DR BindingDB; Q01432; -. DR ChEMBL; CHEMBL2912; -. DR CarbonylDB; Q01432; -. DR iPTMnet; Q01432; -. DR PhosphoSitePlus; Q01432; -. DR BioMuta; AMPD3; -. DR DMDM; 399033; -. DR EPD; Q01432; -. DR jPOST; Q01432; -. DR MassIVE; Q01432; -. DR MaxQB; Q01432; -. DR PaxDb; 9606-ENSP00000379802; -. DR PeptideAtlas; Q01432; -. DR ProteomicsDB; 57945; -. [Q01432-1] DR ProteomicsDB; 57946; -. [Q01432-2] DR ProteomicsDB; 57947; -. [Q01432-3] DR ProteomicsDB; 57948; -. [Q01432-4] DR ProteomicsDB; 57949; -. [Q01432-5] DR Pumba; Q01432; -. DR Antibodypedia; 42354; 343 antibodies from 33 providers. DR DNASU; 272; -. DR Ensembl; ENST00000396553.7; ENSP00000379801.2; ENSG00000133805.16. [Q01432-1] DR Ensembl; ENST00000396554.7; ENSP00000379802.3; ENSG00000133805.16. [Q01432-4] DR Ensembl; ENST00000444303.6; ENSP00000396000.2; ENSG00000133805.16. [Q01432-6] DR Ensembl; ENST00000528723.5; ENSP00000436987.1; ENSG00000133805.16. [Q01432-5] DR Ensembl; ENST00000529507.5; ENSP00000431648.1; ENSG00000133805.16. [Q01432-1] DR GeneID; 272; -. DR KEGG; hsa:272; -. DR MANE-Select; ENST00000396553.7; ENSP00000379801.2; NM_001025389.2; NP_001020560.1. DR UCSC; uc001min.2; human. [Q01432-1] DR AGR; HGNC:470; -. DR CTD; 272; -. DR DisGeNET; 272; -. DR GeneCards; AMPD3; -. DR HGNC; HGNC:470; AMPD3. DR HPA; ENSG00000133805; Tissue enhanced (bone marrow, skeletal muscle). DR MalaCards; AMPD3; -. DR MIM; 102772; gene. DR MIM; 612874; phenotype. DR neXtProt; NX_Q01432; -. DR OpenTargets; ENSG00000133805; -. DR Orphanet; 45; Adenosine monophosphate deaminase deficiency. DR PharmGKB; PA24778; -. DR VEuPathDB; HostDB:ENSG00000133805; -. DR eggNOG; KOG1096; Eukaryota. DR GeneTree; ENSGT00950000183011; -. DR HOGENOM; CLU_003782_4_0_1; -. DR InParanoid; Q01432; -. DR OMA; RKERGMC; -. DR OrthoDB; 20951at2759; -. DR PhylomeDB; Q01432; -. DR TreeFam; TF300439; -. DR BRENDA; 3.5.4.6; 2681. DR PathwayCommons; Q01432; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-74217; Purine salvage. DR SABIO-RK; Q01432; -. DR SignaLink; Q01432; -. DR UniPathway; UPA00591; UER00663. DR BioGRID-ORCS; 272; 14 hits in 1158 CRISPR screens. DR ChiTaRS; AMPD3; human. DR GeneWiki; AMPD3; -. DR GenomeRNAi; 272; -. DR Pharos; Q01432; Tchem. DR PRO; PR:Q01432; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q01432; Protein. DR Bgee; ENSG00000133805; Expressed in gluteal muscle and 196 other cell types or tissues. DR ExpressionAtlas; Q01432; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0003876; F:AMP deaminase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006196; P:AMP catabolic process; TAS:ProtInc. DR GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central. DR GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central. DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway. 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:SF2; AMP DEAMINASE 3; 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; Q01432; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; Hydrolase; Metal-binding; KW Nucleotide metabolism; Phosphoprotein; Reference proteome; Zinc. FT CHAIN 1..767 FT /note="AMP deaminase 3" FT /id="PRO_0000194410" FT REGION 89..111 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 181..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 608 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104" FT BINDING 317 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 319 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 319 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 388..393 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 586 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 589 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 663 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 664..667 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 85 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 107 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT VAR_SEQ 1..159 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044230" FT VAR_SEQ 1 FT /note="M -> MALSSEPAEM (in isoform 1A and isoform 2)" FT /evidence="ECO:0000303|PubMed:1400401, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_001275" FT VAR_SEQ 1 FT /note="M -> MEPGSAEM (in isoform 1C and isoform 3)" FT /evidence="ECO:0000303|PubMed:1400401, FT ECO:0000303|PubMed:14702039" FT /id="VSP_001276" FT VAR_SEQ 208..767 FT /note="Missing (in isoform 1A)" FT /evidence="ECO:0000303|PubMed:1400401" FT /id="VSP_001277" FT VAR_SEQ 652..767 FT /note="Missing (in isoform 1C)" FT /evidence="ECO:0000303|PubMed:1400401" FT /id="VSP_001278" FT VARIANT 185 FT /note="R -> W (in dbSNP:rs11042836)" FT /id="VAR_033499" FT VARIANT 310 FT /note="N -> K (in AMPDDE)" FT /evidence="ECO:0000269|PubMed:7881427" FT /id="VAR_042606" FT VARIANT 311 FT /note="V -> L (in AMPDDE; dbSNP:rs117706710)" FT /evidence="ECO:0000269|PubMed:9598089" FT /id="VAR_042607" FT VARIANT 320 FT /note="A -> V (in AMPDDE; dbSNP:rs147542803)" FT /evidence="ECO:0000269|PubMed:7881427" FT /id="VAR_042608" FT VARIANT 324 FT /note="M -> T (in AMPDDE; dbSNP:rs750004231)" FT /evidence="ECO:0000269|PubMed:7881427" FT /id="VAR_042609" FT VARIANT 331 FT /note="R -> C (in AMPDDE; dbSNP:rs758038726)" FT /evidence="ECO:0000269|PubMed:7881427" FT /id="VAR_042610" FT VARIANT 402 FT /note="R -> C (in AMPDDE; dbSNP:rs766280048)" FT /evidence="ECO:0000269|PubMed:7881427" FT /id="VAR_042611" FT VARIANT 450 FT /note="W -> R (in AMPDDE; dbSNP:rs1273151844)" FT /evidence="ECO:0000269|PubMed:11139257, FT ECO:0000269|PubMed:7881427" FT /id="VAR_042612" FT VARIANT 455 FT /note="Y -> H (in dbSNP:rs36003153)" FT /id="VAR_042613" FT VARIANT 573 FT /note="R -> C (in AMPDDE; enzyme inactive; FT dbSNP:rs3741040)" FT /evidence="ECO:0000269|PubMed:8004104" FT /id="VAR_009881" FT VARIANT 585 FT /note="P -> L (in AMPDDE; dbSNP:rs748852415)" FT /evidence="ECO:0000269|PubMed:7881427" FT /id="VAR_042614" FT VARIANT 712 FT /note="Q -> P (in AMPDDE)" FT /evidence="ECO:0000269|PubMed:11139257" FT /id="VAR_042615" SQ SEQUENCE 767 AA; 88812 MW; 2E0A2C629003B98C CRC64; MPRQFPKLNI SEVDEQVRLL AEKVFAKVLR EEDSKDALSL FTVPEDCPIG QKEAKERELQ KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PPQQDWKGPP AASPAMSPTT PVVTGATSLP TPAPYAMPEF QRVTISGDYC AGITLEDYEQ AAKSLAKALM IREKYARLAY HRFPRITSQY LGHPRADTAP PEEGLPDFHP PPLPQEDPYC LDDAPPNLDY LVHMQGGILF VYDNKKMLEH QEPHSLPYPD LETYTVDMSH ILALITDGPT KTYCHRRLNF LESKFSLHEM LNEMSEFKEL KSNPHRDFYN VRKVDTHIHA AACMNQKHLL RFIKHTYQTE PDRTVAEKRG RKITLRQVFD GLHMDPYDLT VDSLDVHAGR QTFHRFDKFN SKYNPVGASE LRDLYLKTEN YLGGEYFARM VKEVARELEE SKYQYSEPRL SIYGRSPEEW PNLAYWFIQH KVYSPNMRWI IQVPRIYDIF RSKKLLPNFG KMLENIFLPL FKATINPQDH RELHLFLKYV TGFDSVDDES KHSDHMFSDK SPNPDVWTSE QNPPYSYYLY YMYANIMVLN NLRRERGLST FLFRPHCGEA GSITHLVSAF LTADNISHGL LLKKSPVLQY LYYLAQIPIA MSPLSNNSLF LEYSKNPLRE FLHKGLHVSL STDDPMQFHY TKEALMEEYA IAAQVWKLST CDLCEIARNS VLQSGLSHQE KQKFLGQNYY KEGPEGNDIR KTNVAQIRMA FRYETLCNEL SFLSDAMKSE EITALTN //