(data stored in ACNUC30567 zone)

HOGENOM: HS1_PE3930

ID   HS1_PE3930                           STANDARD;      PRT;   747 AA.
AC   HS1_PE3930; P23109; Q5TF00;
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 1; EC=3.5.4 6;AltName: Full=AMP deaminase
DE   isoform M;AltName: Full=Myoadenylate deaminase; (HS1.PE3930).
GN   Name=AMPD1;
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 HS1.PE3930.
CC       Homo sapiens chromosome 1 GRCh37  sequence 1..249240621 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:AMPD1_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   -!- 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 AMPD1 are the cause of adenosine monophosphate
CC       deaminase deficiency muscle type (AMPDDM) [MIM:102770]. AMPDDM is
CC       a metabolic disorder resulting in exercise-related myopathy. It is
CC       characterized by exercise-induced muscle aches, cramps, and early
CC       fatigue.
CC   -!- SIMILARITY: Belongs to the adenosine and AMP deaminases family.
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/AMPD1";
CC   -!- GENE_FAMILY: HOG000092200 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000116748;ENST00000353928;ENSP00000316520.
DR   EMBL; AB125879; - ;
DR   EMBL; AB158499; - ;
DR   EMBL; AB158500; - ;
DR   EMBL; AB158502; - ;
DR   EMBL; AB160874; - ;
DR   EMBL; AB160875; - ;
DR   EMBL; AB160876; - ;
DR   EMBL; AB160877; - ;
DR   EMBL; AB160878; - ;
DR   EMBL; AK291349; - ;
DR   EMBL; AK314252; - ;
DR   EMBL; AL096773; - ;
DR   EMBL; BC056678; - ;
DR   EMBL; M37920; - ;
DR   EMBL; M37921; - ;
DR   EMBL; M37922; - ;
DR   EMBL; M37923; - ;
DR   EMBL; M37924; - ;
DR   EMBL; M37927; - ;
DR   EMBL; M37928; - ;
DR   EMBL; M37929; - ;
DR   EMBL; M37930; - ;
DR   EMBL; M37931; - ;
DR   EMBL; M60092; - ;
DR   UniProtKB/Swiss-Prot; P23109; Q5TF00; -.
DR   EMBL; M37931; AAG24258.1; -; Genomic_DNA.
DR   EMBL; M37920; AAG24258.1; JOINED; Genomic_DNA.
DR   EMBL; M37921; AAG24258.1; JOINED; Genomic_DNA.
DR   EMBL; M37922; AAG24258.1; JOINED; Genomic_DNA.
DR   EMBL; M37923; AAG24258.1; JOINED; Genomic_DNA.
DR   EMBL; M37924; AAG24258.1; JOINED; Genomic_DNA.
DR   EMBL; M37927; AAG24258.1; JOINED; Genomic_DNA.
DR   EMBL; M37928; AAG24258.1; JOINED; Genomic_DNA.
DR   EMBL; M37929; AAG24258.1; JOINED; Genomic_DNA.
DR   EMBL; M37930; AAG24258.1; JOINED; Genomic_DNA.
DR   EMBL; M60092; AAA57281.1; -; mRNA.
DR   EMBL; AL096773; CAI18830.1; -; Genomic_DNA.
DR   IPI; IPI00185631; -.
DR   PIR; I39444; I39444.
DR   RefSeq; NP_000027.2; NM_000036.2.
DR   UniGene; Hs.89570; -.
DR   ProteinModelPortal; P23109; -.
DR   SMR; P23109; 103-747.
DR   IntAct; P23109; 4.
DR   STRING; P23109; -.
DR   PRIDE; P23109; -.
DR   Ensembl; ENST00000353928; ENSP00000316520; ENSG00000116748.
DR   GeneID; 270; -.
DR   KEGG; hsa:270; -.
DR   UCSC; uc001efe.1; human.
DR   CTD; 270; -.
DR   GeneCards; GC01M113074; -.
DR   H-InvDB; HIX0199913; -.
DR   HGNC; HGNC:468; AMPD1.
DR   HPA; HPA026478; -.
DR   HPA; HPA028080; -.
DR   MIM; 102770; gene+phenotype.
DR   neXtProt; NX_P23109; -.
DR   Orphanet; 45; Adenosine monophosphate deaminase deficiency.
DR   eggNOG; prNOG13145; -.
DR   OrthoDB; EOG402WRH; -.
DR   PhylomeDB; P23109; -.
DR   Reactome; REACT_1698; Metabolism of nucleotides.
DR   DrugBank; DB00131; Adenosine monophosphate.
DR   NextBio; 1061; -.
DR   ArrayExpress; P23109; -.
DR   Bgee; P23109; -.
DR   CleanEx; HS_AMPD1; -.
DR   Genevestigator; P23109; -.
DR   GermOnline; ENSG00000116748; 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: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; HS1.PE3930; -.
KW   ENSG000001167481755old_1320000031; ENSP000003165207901old_1320000031;
KW   A8K5N4_HUMAN; B2RAM1_HUMAN; Q5W9V2_HUMAN; Q6F4B5_HUMAN; Q6F4B6_HUMAN;
KW   Q6F4B8_HUMAN; Q6F4B9_HUMAN; Q6I6Y1_HUMAN; Q6I6Y2_HUMAN; Q6I6Y3_HUMAN;
KW   AB125879; AB158499; AB158500; AB158502; AB160874; AB160875; AB160876;
KW   AB160878; AK291349; AK314252; AL096773; BC056678; M37920; M37921; M37922;
KW   M37924; M37927; M37928; M37929; M37930; M37931; M60092;
KW   Complete proteome; Disease mutation; Hydrolase; Metal-binding;
KW   Nucleotide metabolism; Polymorphism; Reference proteome; Zinc.
SQ   SEQUENCE   747 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPLFKLPAEE KQIDDAMRNF AEKVFASEVK DEGGRQEISP FDVDEICPIS HHEMQAHIFH
     LETLSTSTEA RRKKRFQGRK TVNLSIPLSE TSSTKLSHID EYISSSPTYQ TVPDFQRVQI
     TGDYASGVTV EDFEIVCKGL YRALCIREKY MQKSFQRFPK TPSKYLRNID GEAWVANESF
     YPVFTPPVKK GEDPFRTDNL PENLGYHLKM KDGVVYVYPN EAAVSKDEPK PLPYPNLDTF
     LDDMNFLLAL IAQGPVKTYT HRRLKFLSSK FQVHQMLNEM DELKELKNNP HRDFYNCRKV
     DTHIHAAACM NQKHLLRFIK KSYQIDADRV VYSTKEKNLT LKELFAKLKM HPYDLTVDSL
     DVHAGRQTFQ RFDKFNDKYN PVGASELRDL YLKTDNYING EYFATIIKEV GADLVEAKYQ
     HAEPRLSIYG RSPDEWSKLS SWFVCNRIHC PNMTWMIQVP RIYDVFRSKN FLPHFGKMLE
     NIFMPVFEAT INPQADPELS VFLKHITGFD SVDDESKHSG HMFSSKSPKP QEWTLEKNPS
     YTYYAYYMYA NIMVLNSLRK ERGMNTFLFR PHCGEAGALT HLMTAFMIAD DISHGLNLKK
     SPVLQYLFFL AQIPIAMSPL SNNSLFLEYA KNPFLDFLQK GLMISLSTDD PMQFHFTKEP
     LMEEYAIAAQ VFKLSTCDMC EVARNSVLQC GISHEEKVKF LGDNYLEEGP AGNDIRRTNV
     AQIRMAYRYE TWCYELNLIA EGLKSTE
//

If you have problems or comments...

PBIL Back to PBIL home page