(data stored in ACNUC30567 zone)

HOGENOM: HS11_PE658

ID   HS11_PE658                           STANDARD;      PRT;   767 AA.
AC   HS11_PE658; Q01432; B7Z877;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=AMP deaminase 3; EC=3.5.4 6;AltName: Full=AMP deaminase
DE   isoform E;AltName: Full=Erythrocyte AMP deaminase; (HS11.PE658).
GN   Name=AMPD3;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS11.PE658.
CC       Homo sapiens chromosome 11 GRCh37  sequence 1..134946516 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:AMPD3_HUMAN
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=3;
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   -!- TISSUE SPECIFICITY: Three isoforms are present in mammals: AMP
CC       deaminase 1 is the predominant form in skeletal muscle; AMP
CC       deaminase 2 predominates in smooth muscle, non-muscle tissue,
CC       embryonic muscle and undifferentiated myoblasts; AMP deaminase 3
CC       is found in erythrocytes.
CC   -!- DISEASE: Defects in AMPD3 are the cause of adenosine monophosphate
CC       deaminase deficiency erythrocyte type (AMPDDE) [MIM:612874]; also
CC       known as erythrocyte AMP deaminase deficiency. AMPDDE is a
CC       metabolic disorder due to lack of activity of the erythrocyte
CC       isoform of AMP deaminase. It is a clinically asymptomatic
CC       condition characterized by a 50% increase in steady-state levels
CC       of ATP in affected cells. Individuals with complete deficiency of
CC       erythrocyte AMP deaminase are healthy and have no hematologic
CC       disorders.
CC   -!- SIMILARITY: Belongs to the adenosine and AMP deaminases family.
CC   -!- GENE_FAMILY: HOG000092200 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000133805;ENST00000444303;ENSP00000396000.
DR   EMBL; AK294444; - ;
DR   EMBL; AK295046; - ;
DR   EMBL; AK299113; - ;
DR   EMBL; AK302970; - ;
DR   EMBL; CH471064; - ;
DR   EMBL; D12775; - ;
DR   EMBL; D31646; - ;
DR   EMBL; M84720; - ;
DR   EMBL; M84721; - ;
DR   EMBL; M84722; - ;
DR   EMBL; U29907; - ;
DR   EMBL; U29909; - ;
DR   EMBL; U29910; - ;
DR   EMBL; U29911; - ;
DR   EMBL; U29912; - ;
DR   EMBL; U29916; - ;
DR   EMBL; U29917; - ;
DR   EMBL; U29918; - ;
DR   EMBL; U29922; - ;
DR   EMBL; U29924; - ;
DR   EMBL; U29925; - ;
DR   EMBL; U29926; - ;
DR   EMBL; U29927; - ;
DR   EMBL; U29929; - ;
DR   UniProtKB/Swiss-Prot; Q01432; B7Z877; -.
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; AK302970; BAH13863.1; -; mRNA.
DR   EMBL; CH471064; EAW68569.1; -; Genomic_DNA.
DR   IPI; IPI00300573; -.
DR   IPI; IPI00619970; -.
DR   IPI; IPI01010843; -.
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   UniGene; Hs.501890; -.
DR   ProteinModelPortal; Q01432; -.
DR   SMR; Q01432; 128-763.
DR   IntAct; Q01432; 2.
DR   STRING; Q01432; -.
DR   PhosphoSite; Q01432; -.
DR   PRIDE; Q01432; -.
DR   Ensembl; ENST00000256183; ENSP00000256183; ENSG00000133805.
DR   Ensembl; ENST00000396553; ENSP00000379801; ENSG00000133805.
DR   Ensembl; ENST00000431080; ENSP00000389509; ENSG00000133805.
DR   Ensembl; ENST00000444303; ENSP00000396000; ENSG00000133805.
DR   GeneID; 272; -.
DR   KEGG; hsa:272; -.
DR   UCSC; uc001min.1; human.
DR   UCSC; uc009yfx.1; human.
DR   CTD; 272; -.
DR   GeneCards; GC11P010144; -.
DR   H-InvDB; HIX0036031; -.
DR   HGNC; HGNC:470; AMPD3.
DR   MIM; 102772; gene.
DR   MIM; 612874; phenotype.
DR   neXtProt; NX_Q01432; -.
DR   Orphanet; 45; Adenosine monophosphate deaminase deficiency.
DR   GeneTree; ENSGT00390000008190; -.
DR   InParanoid; Q01432; -.
DR   OrthoDB; EOG4J9MZC; -.
DR   PhylomeDB; Q01432; -.
DR   Reactome; REACT_1698; Metabolism of nucleotides.
DR   NextBio; 1073; -.
DR   ArrayExpress; Q01432; -.
DR   Bgee; Q01432; -.
DR   CleanEx; HS_AMPD3; -.
DR   Genevestigator; Q01432; -.
DR   GermOnline; ENSG00000133805; Homo sapiens.
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:0006144; P:purine base metabolic process; TAS:Reactome.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0043101; P:purine-containing compound salvage; TAS:Reactome.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A/AMP_deaminase.
DR   InterPro; IPR006329; AMP_deaminase.
DR   InterPro; IPR016297; AMP_deaminase_met.
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.
DR   HOGENOMDNA; HS11.PE658; -.
KW   ENSG000001338051755old_1320000031; ENSP000003960007901old_1320000031;
KW   B7Z282_HUMAN; B7Z2S2_HUMAN; B7Z5L7_HUMAN; AK294444; AK295046; AK299113;
KW   CH471064; D12775; D31646; M84720; M84721; M84722; U29907; U29909; U29910;
KW   U29912; U29916; U29917; U29918; U29922; U29924; U29925; U29926; U29927;
KW   U29929;
KW   Alternative splicing; Complete proteome; Disease mutation; Hydrolase;
KW   Metal-binding; Nucleotide metabolism; Phosphoprotein; Polymorphism;
KW   Reference proteome; Zinc.
SQ   SEQUENCE   767 AA;  UNKNOWN MW;  UNKNOWN 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
//

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