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UniProtKB/Swiss-Prot entry P07327


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADH1A_HUMAN
Primary accession number P07327
Secondary accession number Q17R68
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 98)
Name and origin of the protein
Protein name Alcohol dehydrogenase 1A
Synonyms EC 1.1.1.1
Alcohol dehydrogenase subunit alpha
Gene name
Name: ADH1A
Synonyms: ADH1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-375.
TISSUE=Liver;
DOI=10.1021/bi00357a026; PubMed=3013304 [NCBI, ExPASy, EBI, Israel, Japan]
von Bahr-Lindstroem H., Hoeoeg J.-O., Heden L.-O., Kaiser R., Fleetwood L., Larsson K., Lake M., Holmquist B., Holmgren A., Hempel J., Vallee B.L., Joernvall H.;
"cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase.";
Biochemistry 25:2465-2470(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2935875 [NCBI, ExPASy, EBI, Israel, Japan]
Ikuta T., Szeto S., Yoshida A.;
"Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence.";
Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986).
[3]
NUCLEOTIDE SEQUENCE.
DOI=10.1016/0014-5793(89)81217-7; PubMed=2920825 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuo Y., Yokoyama S.;
"Molecular structure of the human alcohol dehydrogenase 1 gene.";
FEBS Lett. 243:57-60(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Rieder M.J., Rajkumar N., Downing T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
DOI=10.1016/0888-7543(90)90535-3; PubMed=2347582 [NCBI, ExPASy, EBI, Israel, Japan]
Yasunami M., Kikuchi I., Sarapata D., Yoshida A.;
"The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome.";
Genomics 7:152-158(1990).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M12271; AAA68131.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12963; AAA51590.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019812; AAV38615.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY948115; AAX20115.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074738; AAH74738.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117442; AAI17443.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126306; AAI26307.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M37066; AAA51591.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S02265; DEHUAA.
RefSeq NP_000658.1; -.
UniGene Hs.654433
3D structure databases
PDB
1HSO; X-ray; 2.50 A; A/B=1-375.[ExPASy / RCSB / EBI]
1U3T; X-ray; 2.49 A; A/B=1-375.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HSO; -.
1U3T; -.
ModBase P07327.
Enzyme and pathway databases
Reactome REACT_2063; Metabolism of xenobiotics.
Polymorphism databases
NIEHS-SNPs ADH1A.
Organism-specific databases
H-InvDB HIX0031477; -.
HGNC HGNC:249; ADH1A.
GenAtlas ADH1A.
HPA CAB009562; -.
MIM 103700; gene. [NCBI / EBI]
PharmGKB PA24570; -.
GeneCards P07327.
Gene expression databases
ArrayExpress P07327; -.
CleanEx HS_ADH1A; -.
GermOnline ENSG00000187758; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0004024; Molecular function: alcohol dehydrogenase activity, zinc-dependent (non-traceable author statement from UniProtKB).
GO:0006066; Biological process: cellular alcohol metabolic process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00059; ADH_ZINC; 1.
BLOCKS P07327.
ProtoNet P07327.
Genome annotation databases
Ensembl ENSG00000187758; Homo sapiens. [Contig view]
GeneID 124; -.
KEGG hsa:124; -.
Phylogenomic databases
HOGENOM P07327; -.
HOVERGEN P07327; -.
Other
DrugBank DB01213; Fomepizole.
DB00157; NADH.
NextBio 495; -.
SOURCE ADH1A; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   375  374     Alcohol dehydrogenase 1A. PRO_0000160658
METAL   47    47        Zinc 1; catalytic. 
METAL   68    68        Zinc 1; catalytic. 
METAL   98    98        Zinc 2. 
METAL   101   101        Zinc 2. 
METAL   104   104        Zinc 2. 
METAL   112   112        Zinc 2. 
METAL   175   175        Zinc 1; catalytic. 
MOD_RES   2     2        N-acetylserine. 
STRAND   8    15  8      
STRAND   23    29  7      
STRAND   36    45  10      
HELIX   48    54  7      
STRAND   62    65  4      
STRAND   69    77  9      
STRAND   89    92  4      
STRAND   99   101  3      
HELIX   102   105  4      
STRAND   116   119  4      
STRAND   131   133  3      
STRAND   136   139  4      
TURN   142   144  3      
STRAND   147   154  8      
HELIX   155   157  3      
STRAND   158   160  3      
HELIX   167   170  4      
HELIX   171   174  4      
HELIX   176   185  10      
TURN   186   188  3      
STRAND   195   199  5      
HELIX   203   214  12      
STRAND   218   223  6      
HELIX   227   229  3      
HELIX   230   235  6      
STRAND   239   242  4      
HELIX   244   246  3      
HELIX   251   258  8      
TURN   259   261  3      
STRAND   263   268  6      
HELIX   273   282  10      
TURN   285   287  3      
STRAND   289   292  4      
STRAND   302   304  3      
HELIX   307   310  4      
STRAND   314   317  4      
HELIX   320   322  3      
HELIX   325   337  13      
HELIX   344   346  3      
STRAND   347   352  6      
HELIX   353   355  3      
HELIX   356   364  9      
STRAND   369   374  6      
Sequence information
Length: 375 AA [This is the length of the unprocessed precursor] Molecular weight: 39859 Da [This is the MW of the unprocessed precursor] CRC64: B6DF4D57080D9BC1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT 

        70         80         90        100        110        120 
PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP 

       130        140        150        160        170        180 
QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE 

       250        260        270        280        290        300 
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ 

       310        320        330        340        350        360 
NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV LPFEKINEGF 

       370 
DLLHSGKSIR TILMF 

P07327 in FASTA format

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