AMPD3_HUMAN
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 03-AUG-2022, entry version 196.
DE RecName: Full=AMP deaminase 3;
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;
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}.
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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; Q01432; -.
DR PeptideAtlas; Q01432; -.
DR PRIDE; 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 Antibodypedia; 42354; 308 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 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; 49756at2759; -.
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 1078 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 194 other tissues.
DR ExpressionAtlas; Q01432; baseline and differential.
DR Genevisible; Q01432; HS.
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; IBA:GO_Central.
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 InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR029771; AMPD3.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR PANTHER; PTHR11359:SF2; PTHR11359:SF2; 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 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
