Full text data of AMPD3
AMPD3
[Confidence: low (only semi-automatic identification from reviews)]
AMP deaminase 3; 3.5.4.6 (AMP deaminase isoform E; Erythrocyte AMP deaminase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
AMP deaminase 3; 3.5.4.6 (AMP deaminase isoform E; Erythrocyte AMP deaminase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q01432
ID AMPD3_HUMAN Reviewed; 767 AA.
AC Q01432; A0AUX0; B7Z2S2; B7Z763; B7Z877;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 1.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=AMP deaminase 3;
DE EC=3.5.4.6;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT erythrocyte-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;
RA Mahnke-Zizelman D.K., Sabina R.L.;
RT "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third
RT AMPD 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
RP ALTERNATIVE 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
RT is 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
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASS
RP SPECTROMETRY.
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 [10]
RP VARIANTS AMPDDE LYS-310; VAL-320; THR-324; CYS-331; CYS-402; ARG-450
RP AND 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:
RT screening for the major point mutation and identification of other
RT mutations.";
RL Hum. Mol. Genet. 3:2243-2245(1994).
RN [11]
RP VARIANT AMPDDE LEU-311.
RX PubMed=9598089;
RA Yamada Y., Makarewicz W., Goto H., Nomura N., Kitoh H., Ogasawara N.;
RT "Gene mutations responsible for human erythrocyte AMP deaminase
RT deficiency in Poles.";
RL Adv. Exp. Med. Biol. 431:347-350(1998).
RN [12]
RP VARIANTS AMPDDE ARG-450 AND PRO-712.
RX PubMed=11139257;
RX DOI=10.1002/1098-1004(2001)17:1<78::AID-HUMU21>3.3.CO;2-2;
RA Yamada Y., Goto H., Wakamatsu N., Ogasawara N.;
RT "A rare case of complete human erythrocyte AMP deaminase deficiency
RT due to two novel missense mutations in AMPD3.";
RL Hum. Mutat. 17:78-78(2001).
CC -!- FUNCTION: AMP deaminase plays a critical role in energy
CC metabolism.
CC -!- CATALYTIC ACTIVITY: AMP + H(2)O = IMP + NH(3).
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC IMP from AMP: step 1/1.
CC -!- SUBUNIT: Homotetramer.
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 -!- TISSUE SPECIFICITY: Isoform 1 is the predominant form in skeletal
CC muscle; Isoform 2 predominates in smooth muscle, non-muscle
CC tissue, embryonic muscle and undifferentiated myoblasts; Isoform 3
CC is found in erythrocytes.
CC -!- DISEASE: Adenosine monophosphate deaminase deficiency erythrocyte
CC type (AMPDDE) [MIM:612874]: A metabolic disorder due to lack of
CC activity of the erythrocyte isoform of AMP deaminase. It is a
CC clinically asymptomatic condition characterized by a 50% increase
CC in steady-state levels of ATP in affected cells. Individuals with
CC complete deficiency of erythrocyte AMP deaminase are healthy and
CC have no hematologic disorders. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the adenosine and AMP deaminases family.
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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 PIR; S68146; S68146.
DR PIR; S68147; S68147.
DR RefSeq; NP_000471.1; NM_000480.2.
DR RefSeq; NP_001020560.1; NM_001025389.1.
DR RefSeq; NP_001020561.1; NM_001025390.1.
DR RefSeq; NP_001165901.1; NM_001172430.1.
DR RefSeq; NP_001165902.1; NM_001172431.1.
DR RefSeq; XP_005252924.1; XM_005252867.1.
DR RefSeq; XP_005252925.1; XM_005252868.1.
DR UniGene; Hs.501890; -.
DR ProteinModelPortal; Q01432; -.
DR SMR; Q01432; 219-762.
DR IntAct; Q01432; 2.
DR STRING; 9606.ENSP00000256183; -.
DR BindingDB; Q01432; -.
DR ChEMBL; CHEMBL2912; -.
DR PhosphoSite; Q01432; -.
DR DMDM; 399033; -.
DR PaxDb; Q01432; -.
DR PRIDE; Q01432; -.
DR DNASU; 272; -.
DR Ensembl; ENST00000396553; ENSP00000379801; ENSG00000133805.
DR Ensembl; ENST00000396554; ENSP00000379802; ENSG00000133805.
DR Ensembl; ENST00000444303; ENSP00000396000; ENSG00000133805.
DR Ensembl; ENST00000528723; ENSP00000436987; ENSG00000133805.
DR Ensembl; ENST00000529507; ENSP00000431648; ENSG00000133805.
DR GeneID; 272; -.
DR KEGG; hsa:272; -.
DR UCSC; uc001mio.1; human.
DR CTD; 272; -.
DR GeneCards; GC11P010329; -.
DR HGNC; HGNC:470; AMPD3.
DR HPA; HPA047408; -.
DR MIM; 102772; gene.
DR MIM; 612874; phenotype.
DR neXtProt; NX_Q01432; -.
DR Orphanet; 45; Adenosine monophosphate deaminase deficiency.
DR PharmGKB; PA24778; -.
DR eggNOG; COG1816; -.
DR HOGENOM; HOG000092200; -.
DR HOVERGEN; HBG050494; -.
DR InParanoid; Q01432; -.
DR KO; K01490; -.
DR OMA; FSLHEML; -.
DR OrthoDB; EOG70ZZMQ; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; Q01432; -.
DR UniPathway; UPA00591; UER00663.
DR ChiTaRS; AMPD3; human.
DR GeneWiki; AMPD3; -.
DR GenomeRNAi; 272; -.
DR NextBio; 1073; -.
DR PRO; PR:Q01432; -.
DR ArrayExpress; Q01432; -.
DR Bgee; Q01432; -.
DR CleanEx; HS_AMPD3; -.
DR Genevestigator; Q01432; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003876; F:AMP deaminase activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006196; P:AMP catabolic process; TAS:ProtInc.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0043101; P:purine-containing compound salvage; TAS:Reactome.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR001365; A/AMP_deaminase_dom.
DR InterPro; IPR006329; AMP_deaminase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Disease mutation; Hydrolase;
KW Metal-binding; Nucleotide metabolism; Phosphoprotein; Polymorphism;
KW Reference proteome; Zinc.
FT CHAIN 1 767 AMP deaminase 3.
FT /FTId=PRO_0000194410.
FT REGION 388 393 Substrate binding (By similarity).
FT REGION 664 667 Substrate binding (By similarity).
FT ACT_SITE 608 608 Proton acceptor (By similarity).
FT METAL 317 317 Zinc; catalytic (By similarity).
FT METAL 319 319 Zinc; catalytic (By similarity).
FT METAL 586 586 Zinc; catalytic (By similarity).
FT METAL 663 663 Zinc; catalytic (By similarity).
FT BINDING 319 319 Substrate (By similarity).
FT BINDING 589 589 Substrate (By similarity).
FT MOD_RES 107 107 Phosphoserine.
FT VAR_SEQ 1 159 Missing (in isoform 4).
FT /FTId=VSP_044230.
FT VAR_SEQ 1 1 M -> MALSSEPAEM (in isoform 1A and
FT isoform 2).
FT /FTId=VSP_001275.
FT VAR_SEQ 1 1 M -> MEPGSAEM (in isoform 1C and isoform
FT 3).
FT /FTId=VSP_001276.
FT VAR_SEQ 208 767 Missing (in isoform 1A).
FT /FTId=VSP_001277.
FT VAR_SEQ 652 767 Missing (in isoform 1C).
FT /FTId=VSP_001278.
FT VARIANT 185 185 R -> W (in dbSNP:rs11042836).
FT /FTId=VAR_033499.
FT VARIANT 310 310 N -> K (in AMPDDE).
FT /FTId=VAR_042606.
FT VARIANT 311 311 V -> L (in AMPDDE; dbSNP:rs117706710).
FT /FTId=VAR_042607.
FT VARIANT 320 320 A -> V (in AMPDDE).
FT /FTId=VAR_042608.
FT VARIANT 324 324 M -> T (in AMPDDE).
FT /FTId=VAR_042609.
FT VARIANT 331 331 R -> C (in AMPDDE).
FT /FTId=VAR_042610.
FT VARIANT 402 402 R -> C (in AMPDDE).
FT /FTId=VAR_042611.
FT VARIANT 450 450 W -> R (in AMPDDE).
FT /FTId=VAR_042612.
FT VARIANT 455 455 Y -> H (in dbSNP:rs36003153).
FT /FTId=VAR_042613.
FT VARIANT 573 573 R -> C (in AMPDDE; enzyme inactive;
FT dbSNP:rs3741040).
FT /FTId=VAR_009881.
FT VARIANT 585 585 P -> L (in AMPDDE).
FT /FTId=VAR_042614.
FT VARIANT 712 712 Q -> P (in AMPDDE).
FT /FTId=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
//
ID AMPD3_HUMAN Reviewed; 767 AA.
AC Q01432; A0AUX0; B7Z2S2; B7Z763; B7Z877;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 1.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=AMP deaminase 3;
DE EC=3.5.4.6;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT erythrocyte-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;
RA Mahnke-Zizelman D.K., Sabina R.L.;
RT "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third
RT AMPD 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
RP ALTERNATIVE 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
RT is 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
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASS
RP SPECTROMETRY.
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 [10]
RP VARIANTS AMPDDE LYS-310; VAL-320; THR-324; CYS-331; CYS-402; ARG-450
RP AND 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:
RT screening for the major point mutation and identification of other
RT mutations.";
RL Hum. Mol. Genet. 3:2243-2245(1994).
RN [11]
RP VARIANT AMPDDE LEU-311.
RX PubMed=9598089;
RA Yamada Y., Makarewicz W., Goto H., Nomura N., Kitoh H., Ogasawara N.;
RT "Gene mutations responsible for human erythrocyte AMP deaminase
RT deficiency in Poles.";
RL Adv. Exp. Med. Biol. 431:347-350(1998).
RN [12]
RP VARIANTS AMPDDE ARG-450 AND PRO-712.
RX PubMed=11139257;
RX DOI=10.1002/1098-1004(2001)17:1<78::AID-HUMU21>3.3.CO;2-2;
RA Yamada Y., Goto H., Wakamatsu N., Ogasawara N.;
RT "A rare case of complete human erythrocyte AMP deaminase deficiency
RT due to two novel missense mutations in AMPD3.";
RL Hum. Mutat. 17:78-78(2001).
CC -!- FUNCTION: AMP deaminase plays a critical role in energy
CC metabolism.
CC -!- CATALYTIC ACTIVITY: AMP + H(2)O = IMP + NH(3).
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC IMP from AMP: step 1/1.
CC -!- SUBUNIT: Homotetramer.
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 -!- TISSUE SPECIFICITY: Isoform 1 is the predominant form in skeletal
CC muscle; Isoform 2 predominates in smooth muscle, non-muscle
CC tissue, embryonic muscle and undifferentiated myoblasts; Isoform 3
CC is found in erythrocytes.
CC -!- DISEASE: Adenosine monophosphate deaminase deficiency erythrocyte
CC type (AMPDDE) [MIM:612874]: A metabolic disorder due to lack of
CC activity of the erythrocyte isoform of AMP deaminase. It is a
CC clinically asymptomatic condition characterized by a 50% increase
CC in steady-state levels of ATP in affected cells. Individuals with
CC complete deficiency of erythrocyte AMP deaminase are healthy and
CC have no hematologic disorders. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the adenosine and AMP deaminases family.
CC -----------------------------------------------------------------------
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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 PIR; S68146; S68146.
DR PIR; S68147; S68147.
DR RefSeq; NP_000471.1; NM_000480.2.
DR RefSeq; NP_001020560.1; NM_001025389.1.
DR RefSeq; NP_001020561.1; NM_001025390.1.
DR RefSeq; NP_001165901.1; NM_001172430.1.
DR RefSeq; NP_001165902.1; NM_001172431.1.
DR RefSeq; XP_005252924.1; XM_005252867.1.
DR RefSeq; XP_005252925.1; XM_005252868.1.
DR UniGene; Hs.501890; -.
DR ProteinModelPortal; Q01432; -.
DR SMR; Q01432; 219-762.
DR IntAct; Q01432; 2.
DR STRING; 9606.ENSP00000256183; -.
DR BindingDB; Q01432; -.
DR ChEMBL; CHEMBL2912; -.
DR PhosphoSite; Q01432; -.
DR DMDM; 399033; -.
DR PaxDb; Q01432; -.
DR PRIDE; Q01432; -.
DR DNASU; 272; -.
DR Ensembl; ENST00000396553; ENSP00000379801; ENSG00000133805.
DR Ensembl; ENST00000396554; ENSP00000379802; ENSG00000133805.
DR Ensembl; ENST00000444303; ENSP00000396000; ENSG00000133805.
DR Ensembl; ENST00000528723; ENSP00000436987; ENSG00000133805.
DR Ensembl; ENST00000529507; ENSP00000431648; ENSG00000133805.
DR GeneID; 272; -.
DR KEGG; hsa:272; -.
DR UCSC; uc001mio.1; human.
DR CTD; 272; -.
DR GeneCards; GC11P010329; -.
DR HGNC; HGNC:470; AMPD3.
DR HPA; HPA047408; -.
DR MIM; 102772; gene.
DR MIM; 612874; phenotype.
DR neXtProt; NX_Q01432; -.
DR Orphanet; 45; Adenosine monophosphate deaminase deficiency.
DR PharmGKB; PA24778; -.
DR eggNOG; COG1816; -.
DR HOGENOM; HOG000092200; -.
DR HOVERGEN; HBG050494; -.
DR InParanoid; Q01432; -.
DR KO; K01490; -.
DR OMA; FSLHEML; -.
DR OrthoDB; EOG70ZZMQ; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; Q01432; -.
DR UniPathway; UPA00591; UER00663.
DR ChiTaRS; AMPD3; human.
DR GeneWiki; AMPD3; -.
DR GenomeRNAi; 272; -.
DR NextBio; 1073; -.
DR PRO; PR:Q01432; -.
DR ArrayExpress; Q01432; -.
DR Bgee; Q01432; -.
DR CleanEx; HS_AMPD3; -.
DR Genevestigator; Q01432; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003876; F:AMP deaminase activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006196; P:AMP catabolic process; TAS:ProtInc.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0043101; P:purine-containing compound salvage; TAS:Reactome.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR001365; A/AMP_deaminase_dom.
DR InterPro; IPR006329; AMP_deaminase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Disease mutation; Hydrolase;
KW Metal-binding; Nucleotide metabolism; Phosphoprotein; Polymorphism;
KW Reference proteome; Zinc.
FT CHAIN 1 767 AMP deaminase 3.
FT /FTId=PRO_0000194410.
FT REGION 388 393 Substrate binding (By similarity).
FT REGION 664 667 Substrate binding (By similarity).
FT ACT_SITE 608 608 Proton acceptor (By similarity).
FT METAL 317 317 Zinc; catalytic (By similarity).
FT METAL 319 319 Zinc; catalytic (By similarity).
FT METAL 586 586 Zinc; catalytic (By similarity).
FT METAL 663 663 Zinc; catalytic (By similarity).
FT BINDING 319 319 Substrate (By similarity).
FT BINDING 589 589 Substrate (By similarity).
FT MOD_RES 107 107 Phosphoserine.
FT VAR_SEQ 1 159 Missing (in isoform 4).
FT /FTId=VSP_044230.
FT VAR_SEQ 1 1 M -> MALSSEPAEM (in isoform 1A and
FT isoform 2).
FT /FTId=VSP_001275.
FT VAR_SEQ 1 1 M -> MEPGSAEM (in isoform 1C and isoform
FT 3).
FT /FTId=VSP_001276.
FT VAR_SEQ 208 767 Missing (in isoform 1A).
FT /FTId=VSP_001277.
FT VAR_SEQ 652 767 Missing (in isoform 1C).
FT /FTId=VSP_001278.
FT VARIANT 185 185 R -> W (in dbSNP:rs11042836).
FT /FTId=VAR_033499.
FT VARIANT 310 310 N -> K (in AMPDDE).
FT /FTId=VAR_042606.
FT VARIANT 311 311 V -> L (in AMPDDE; dbSNP:rs117706710).
FT /FTId=VAR_042607.
FT VARIANT 320 320 A -> V (in AMPDDE).
FT /FTId=VAR_042608.
FT VARIANT 324 324 M -> T (in AMPDDE).
FT /FTId=VAR_042609.
FT VARIANT 331 331 R -> C (in AMPDDE).
FT /FTId=VAR_042610.
FT VARIANT 402 402 R -> C (in AMPDDE).
FT /FTId=VAR_042611.
FT VARIANT 450 450 W -> R (in AMPDDE).
FT /FTId=VAR_042612.
FT VARIANT 455 455 Y -> H (in dbSNP:rs36003153).
FT /FTId=VAR_042613.
FT VARIANT 573 573 R -> C (in AMPDDE; enzyme inactive;
FT dbSNP:rs3741040).
FT /FTId=VAR_009881.
FT VARIANT 585 585 P -> L (in AMPDDE).
FT /FTId=VAR_042614.
FT VARIANT 712 712 Q -> P (in AMPDDE).
FT /FTId=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
//
MIM
102772
*RECORD*
*FIELD* NO
102772
*FIELD* TI
*102772 ADENOSINE MONOPHOSPHATE DEAMINASE 3; AMPD3
*FIELD* TX
DESCRIPTION
Adenosine monophosphate deaminase-3 (EC 3.5.4.6) catalyzes the
read moredeamination of AMP to IMP in red cells and plays an important role in
the purine nucleotide cycle. The AMPD3 gene encodes 2 erythrocyte
isoforms, E1 and E2. An inherited defect in AMPD3 results in combined
deficiency of these isoforms.
Also see AMPD1 (102770) and AMPD2 (102771), which encode the L (liver)
and M (muscle) isoforms of AMP deaminase, respectively.
CLONING
Mahnke-Zizelman and Sabina (1992) isolated several AMPD3 cDNAs from
different human nonskeletal muscle cDNA libraries. The cDNAs differed in
their 5-prime terminal sequences.
Yamada et al. (1992) also cloned a human AMPD3 cDNA. The 3.7-kb cDNA
contains an open reading frame of 2,301 bp that encodes a deduced
767-amino acid protein with a predicted molecular mass of 89 kD.
Mahnke-Zizelman et al. (1996) reported that the AMPD3 gene is widely
expressed in human tissues and cells and that its expression is subject
to transcriptional control by 3 tandem promoters. The AMPD3 transcripts
encode the E isoforms of AMP deaminase.
Mahnke-Zizelman et al. (1997) demonstrated that rat isoform C and human
isoform E are homologous cross-species AMPD3 proteins.
GENE STRUCTURE
Mahnke-Zizelman et al. (1996) demonstrated that the AMPD3 gene contains
17 exons spanning approximately 60 kb. They identified multiple
promoters in proximal flanking sequence 5-prime to exons 1a, 1b, and 1c
that regulate the production of alternative AMPD3 transcripts.
Alternative splicing occurs in exon 1c.
MAPPING
Whereas both the AMPD1 and AMPD2 genes are situated in the 1p21-p13
region of chromosome 1, Eddy et al. (1993) demonstrated that the AMPD3
gene is located on chromosome 11 in the region pter-p13.
Sermsuvitayawong et al. (1997) demonstrated that the Ampd3 gene is
located on mouse chromosome 7 in a region of conserved linkage homology
with human 11p. The mouse homolog, however, has a different gene
structure in the 5-prime region, the gene products are reported to be
immunologically distinct, and Sermsuvitayawong et al. (1997) referred to
the Ampd3 gene as the heart-type AMPD.
MOLECULAR GENETICS
In 2 of the Japanese individuals with erythrocyte AMP deficiency
(612874) reported by Ogasawara et al. (1987), Yamada et al. (1994)
identified a mutation in the AMPD3 gene (102772.0001).
*FIELD* AV
.0001
ERYTHROCYTE AMP DEAMINASE DEFICIENCY
AMPD3, ARG573CYS
In 2 individuals with complete deficiency of erythrocyte AMP deaminase
(612874), Yamada et al. (1994) identified homozygosity for a 1717C-T
transition in the AMPD3 gene, resulting in an amino acid change of arg
to cys at codon 573 (R573C). Two individuals with partial deficiency of
the enzyme were found to be heterozygous for the mutation. The mutation
resulted in a catalytically inactive enzyme.
Among 45 Japanese individuals with partial erythrocyte AMP deaminase
deficiency, Yamada et al. (1994) found that all but 16 were heterozygous
for the R573C mutation; 2 individuals with complete deficiency were
homozygous for the mutation. They concluded that this mutation accounts
for 75% of erythrocyte AMP deaminase deficiency in Japan.
*FIELD* RF
1. Eddy, R. L.; Mahnke-Zizelman, D. K.; Bausch-Jurken, M. T.; Sabina,
R. L.; Shows, T. B.: Distribution of the AMP deaminase multigene
family within the human genome: assignment of the AMPD2 to chromosome
1p21-p34 and AMPD3 to chromosome 11p13-pter. (Abstract) Human Genome
Mapping Workshop 93 24 only, 1993.
2. Mahnke-Zizelman, D. K.; D'Cunha, J.; Wojnar J. M.; Brogley, M.
A.; Sabina, R. L.: Regulation of rat AMP deaminase 3 (isoform C)
by by development and skeletal muscle fibre type. Biochem. J. 326:
521-529, 1997.
3. Mahnke-Zizelman, D. K.; Eddy, R.; Shows, T. B.; Sabina, R. L.:
Characterization of the human AMPD3 gene reveals that 5-prime exon
useage is subject to transcriptional control by three tandem promoters
and alternative splicing. Biochem. Biophys. Acta 1306: 75-92, 1996.
4. Mahnke-Zizelman, D. K.; Sabina, R. L.: Cloning of human AMP deaminase
isoform E cDNAs: evidence for a third AMPD gene exhibiting alternatively
spliced 5-prime exons. J. Biol. Chem. 267: 20866-20877, 1992.
5. Ogasawara, N.; Goto, H.; Yamada, Y.; Nishigaki, I.; Itoh, T.; Hasegawa,
I.; Park, K. S.: Deficiency of AMP deaminase in erythrocytes. Hum.
Genet. 75: 15-18, 1987.
6. Sermsuvitayawong, K.; Wang, X.; Nagabukuro, A.; Matsuda, Y.; Morisaki,
H.; Toyama, K.; Mukai, T.; Morisaki, T.: Genomic organization of
Ampd3, heart-type AMPD gene, located in mouse chromosome 7. Mammalian
Genome 8: 767-769, 1997.
7. Yamada, Y.; Goto, H.; Murase, T.; Ogasawara, N.: Molecular basis
for human erythrocyte AMP deaminase deficiency: screening for the
major point mutation and identification of other mutations. Hum.
Molec. Genet. 3: 2243-2245, 1994.
8. Yamada, Y.; Goto, H.; Ogasawara, N.: Cloning and nucleotide sequence
of the cDNA encoding human erythrocyte-specific AMP deaminase. Biochim.
Biophys. Acta 1171: 125-128, 1992.
9. Yamada, Y.; Goto, H.; Ogasawara, N.: A point mutation responsible
for human erythrocyte AMP deaminase deficiency. Hum. Molec. Genet. 3:
331-334, 1994.
*FIELD* CN
Victor A. McKusick - updated: 10/14/1997
*FIELD* CD
Victor A. McKusick: 12/6/1993
*FIELD* ED
terry: 06/23/2009
carol: 6/23/2009
carol: 12/30/2008
mgross: 3/17/2004
terry: 11/19/1998
dkim: 6/26/1998
mark: 10/17/1997
terry: 10/14/1997
alopez: 7/10/1997
carol: 4/13/1994
carol: 12/6/1993
*RECORD*
*FIELD* NO
102772
*FIELD* TI
*102772 ADENOSINE MONOPHOSPHATE DEAMINASE 3; AMPD3
*FIELD* TX
DESCRIPTION
Adenosine monophosphate deaminase-3 (EC 3.5.4.6) catalyzes the
read moredeamination of AMP to IMP in red cells and plays an important role in
the purine nucleotide cycle. The AMPD3 gene encodes 2 erythrocyte
isoforms, E1 and E2. An inherited defect in AMPD3 results in combined
deficiency of these isoforms.
Also see AMPD1 (102770) and AMPD2 (102771), which encode the L (liver)
and M (muscle) isoforms of AMP deaminase, respectively.
CLONING
Mahnke-Zizelman and Sabina (1992) isolated several AMPD3 cDNAs from
different human nonskeletal muscle cDNA libraries. The cDNAs differed in
their 5-prime terminal sequences.
Yamada et al. (1992) also cloned a human AMPD3 cDNA. The 3.7-kb cDNA
contains an open reading frame of 2,301 bp that encodes a deduced
767-amino acid protein with a predicted molecular mass of 89 kD.
Mahnke-Zizelman et al. (1996) reported that the AMPD3 gene is widely
expressed in human tissues and cells and that its expression is subject
to transcriptional control by 3 tandem promoters. The AMPD3 transcripts
encode the E isoforms of AMP deaminase.
Mahnke-Zizelman et al. (1997) demonstrated that rat isoform C and human
isoform E are homologous cross-species AMPD3 proteins.
GENE STRUCTURE
Mahnke-Zizelman et al. (1996) demonstrated that the AMPD3 gene contains
17 exons spanning approximately 60 kb. They identified multiple
promoters in proximal flanking sequence 5-prime to exons 1a, 1b, and 1c
that regulate the production of alternative AMPD3 transcripts.
Alternative splicing occurs in exon 1c.
MAPPING
Whereas both the AMPD1 and AMPD2 genes are situated in the 1p21-p13
region of chromosome 1, Eddy et al. (1993) demonstrated that the AMPD3
gene is located on chromosome 11 in the region pter-p13.
Sermsuvitayawong et al. (1997) demonstrated that the Ampd3 gene is
located on mouse chromosome 7 in a region of conserved linkage homology
with human 11p. The mouse homolog, however, has a different gene
structure in the 5-prime region, the gene products are reported to be
immunologically distinct, and Sermsuvitayawong et al. (1997) referred to
the Ampd3 gene as the heart-type AMPD.
MOLECULAR GENETICS
In 2 of the Japanese individuals with erythrocyte AMP deficiency
(612874) reported by Ogasawara et al. (1987), Yamada et al. (1994)
identified a mutation in the AMPD3 gene (102772.0001).
*FIELD* AV
.0001
ERYTHROCYTE AMP DEAMINASE DEFICIENCY
AMPD3, ARG573CYS
In 2 individuals with complete deficiency of erythrocyte AMP deaminase
(612874), Yamada et al. (1994) identified homozygosity for a 1717C-T
transition in the AMPD3 gene, resulting in an amino acid change of arg
to cys at codon 573 (R573C). Two individuals with partial deficiency of
the enzyme were found to be heterozygous for the mutation. The mutation
resulted in a catalytically inactive enzyme.
Among 45 Japanese individuals with partial erythrocyte AMP deaminase
deficiency, Yamada et al. (1994) found that all but 16 were heterozygous
for the R573C mutation; 2 individuals with complete deficiency were
homozygous for the mutation. They concluded that this mutation accounts
for 75% of erythrocyte AMP deaminase deficiency in Japan.
*FIELD* RF
1. Eddy, R. L.; Mahnke-Zizelman, D. K.; Bausch-Jurken, M. T.; Sabina,
R. L.; Shows, T. B.: Distribution of the AMP deaminase multigene
family within the human genome: assignment of the AMPD2 to chromosome
1p21-p34 and AMPD3 to chromosome 11p13-pter. (Abstract) Human Genome
Mapping Workshop 93 24 only, 1993.
2. Mahnke-Zizelman, D. K.; D'Cunha, J.; Wojnar J. M.; Brogley, M.
A.; Sabina, R. L.: Regulation of rat AMP deaminase 3 (isoform C)
by by development and skeletal muscle fibre type. Biochem. J. 326:
521-529, 1997.
3. Mahnke-Zizelman, D. K.; Eddy, R.; Shows, T. B.; Sabina, R. L.:
Characterization of the human AMPD3 gene reveals that 5-prime exon
useage is subject to transcriptional control by three tandem promoters
and alternative splicing. Biochem. Biophys. Acta 1306: 75-92, 1996.
4. Mahnke-Zizelman, D. K.; Sabina, R. L.: Cloning of human AMP deaminase
isoform E cDNAs: evidence for a third AMPD gene exhibiting alternatively
spliced 5-prime exons. J. Biol. Chem. 267: 20866-20877, 1992.
5. Ogasawara, N.; Goto, H.; Yamada, Y.; Nishigaki, I.; Itoh, T.; Hasegawa,
I.; Park, K. S.: Deficiency of AMP deaminase in erythrocytes. Hum.
Genet. 75: 15-18, 1987.
6. Sermsuvitayawong, K.; Wang, X.; Nagabukuro, A.; Matsuda, Y.; Morisaki,
H.; Toyama, K.; Mukai, T.; Morisaki, T.: Genomic organization of
Ampd3, heart-type AMPD gene, located in mouse chromosome 7. Mammalian
Genome 8: 767-769, 1997.
7. Yamada, Y.; Goto, H.; Murase, T.; Ogasawara, N.: Molecular basis
for human erythrocyte AMP deaminase deficiency: screening for the
major point mutation and identification of other mutations. Hum.
Molec. Genet. 3: 2243-2245, 1994.
8. Yamada, Y.; Goto, H.; Ogasawara, N.: Cloning and nucleotide sequence
of the cDNA encoding human erythrocyte-specific AMP deaminase. Biochim.
Biophys. Acta 1171: 125-128, 1992.
9. Yamada, Y.; Goto, H.; Ogasawara, N.: A point mutation responsible
for human erythrocyte AMP deaminase deficiency. Hum. Molec. Genet. 3:
331-334, 1994.
*FIELD* CN
Victor A. McKusick - updated: 10/14/1997
*FIELD* CD
Victor A. McKusick: 12/6/1993
*FIELD* ED
terry: 06/23/2009
carol: 6/23/2009
carol: 12/30/2008
mgross: 3/17/2004
terry: 11/19/1998
dkim: 6/26/1998
mark: 10/17/1997
terry: 10/14/1997
alopez: 7/10/1997
carol: 4/13/1994
carol: 12/6/1993
MIM
612874
*RECORD*
*FIELD* NO
612874
*FIELD* TI
#612874 ERYTHROCYTE AMP DEAMINASE DEFICIENCY
*FIELD* TX
A number sign (#) is used with this entry because erythrocyte AMP
read moredeaminase deficiency is caused by mutation in the AMPD3 gene (102772).
DESCRIPTION
Ogasawara et al. (1987) observed 6 related individuals with complete
deficiency of erythrocyte AMP deaminase (isozyme E). All were healthy
and had no hematologic disorders. The ATP level was approximately 150%
higher in AMP-deficient red cells compared to the level in the control
cells. Degradation of adenine nucleotide was slower in the deficient
erythrocytes than in the control erythrocytes.
INHERITANCE
The erythrocyte AMP deaminase deficiency described by Ogasawara et al.
(1987) appeared to be an an autosomal recessive trait because both
parents had partial deficiency in each case in which this could be
studied and all children of completely deficient individuals were
partially deficient.
POPULATION GENETICS
Yamada et al. (1994) stated that AMPD3 deficiency had been found in
Europe and that the frequency in northern Poland was almost the same as
that in east Asia (heterozygote frequency of 1 in 30).
MOLECULAR GENETICS
In 4 Japanese individuals with erythrocyte AMP deficiency Yamada et al.
(1994) identified an R573C mutation in the AMPD3 gene (102772.0001); 2
with complete deficiency, originally reported by Ogasawara et al.
(1987), were homozygous for the mutation and 2 with partial deficiency
were heterozygous.
*FIELD* RF
1. Ogasawara, N.; Goto, H.; Yamada, Y.; Nishigaki, I.; Itoh, T.; Hasegawa,
I.; Park, K. S.: Deficiency of AMP deaminase in erythrocytes. Hum.
Genet. 75: 15-18, 1987.
2. Yamada, Y.; Goto, H.; Ogasawara, N.: A point mutation responsible
for human erythrocyte AMP deaminase deficiency. Hum. Molec. Genet. 3:
331-334, 1994.
*FIELD* CD
Carol A. Bocchini: 6/23/2009
*FIELD* ED
carol: 06/23/2009
carol: 6/23/2009
*RECORD*
*FIELD* NO
612874
*FIELD* TI
#612874 ERYTHROCYTE AMP DEAMINASE DEFICIENCY
*FIELD* TX
A number sign (#) is used with this entry because erythrocyte AMP
read moredeaminase deficiency is caused by mutation in the AMPD3 gene (102772).
DESCRIPTION
Ogasawara et al. (1987) observed 6 related individuals with complete
deficiency of erythrocyte AMP deaminase (isozyme E). All were healthy
and had no hematologic disorders. The ATP level was approximately 150%
higher in AMP-deficient red cells compared to the level in the control
cells. Degradation of adenine nucleotide was slower in the deficient
erythrocytes than in the control erythrocytes.
INHERITANCE
The erythrocyte AMP deaminase deficiency described by Ogasawara et al.
(1987) appeared to be an an autosomal recessive trait because both
parents had partial deficiency in each case in which this could be
studied and all children of completely deficient individuals were
partially deficient.
POPULATION GENETICS
Yamada et al. (1994) stated that AMPD3 deficiency had been found in
Europe and that the frequency in northern Poland was almost the same as
that in east Asia (heterozygote frequency of 1 in 30).
MOLECULAR GENETICS
In 4 Japanese individuals with erythrocyte AMP deficiency Yamada et al.
(1994) identified an R573C mutation in the AMPD3 gene (102772.0001); 2
with complete deficiency, originally reported by Ogasawara et al.
(1987), were homozygous for the mutation and 2 with partial deficiency
were heterozygous.
*FIELD* RF
1. Ogasawara, N.; Goto, H.; Yamada, Y.; Nishigaki, I.; Itoh, T.; Hasegawa,
I.; Park, K. S.: Deficiency of AMP deaminase in erythrocytes. Hum.
Genet. 75: 15-18, 1987.
2. Yamada, Y.; Goto, H.; Ogasawara, N.: A point mutation responsible
for human erythrocyte AMP deaminase deficiency. Hum. Molec. Genet. 3:
331-334, 1994.
*FIELD* CD
Carol A. Bocchini: 6/23/2009
*FIELD* ED
carol: 06/23/2009
carol: 6/23/2009