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Reviewed, UniProtKB/Swiss-Prot Q03505 (ADH1_RABIT)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase 1
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase subunit alpha
Gene names
Name: ADH1
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalcohol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 375374Alcohol dehydrogenase 1
PRO_0000160668

Regions

Nucleotide binding200 – 2056NAD By similarity
Nucleotide binding293 – 2953NAD By similarity

Sites

Metal binding471Zinc 1; catalytic By similarity
Metal binding681Zinc 1; catalytic By similarity
Metal binding981Zinc 2 By similarity
Metal binding1011Zinc 2 By similarity
Metal binding1041Zinc 2 By similarity
Metal binding1121Zinc 2 By similarity
Metal binding1751Zinc 1; catalytic By similarity
Binding site2241NAD By similarity
Binding site2291NAD By similarity
Binding site3701NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03505-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 47F03877C54E5B69

FASTA37539,588
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWQLNK PFSIEEVEVA PPKAHEVRIK MVATGICRSD DHAVTGSIAV 

        70         80         90        100        110        120 
PLPVILGHEA AGIVESIGEG VTTVKPGDKV IPLFTPQCGK CRICKHPESN FCLINDLGKP 

       130        140        150        160        170        180 
KGMLLDGTSR FTCKGKPIHH FIGTSTFSQY TVVDEIAVAK IDAAAPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGSAVKVAKV TPGSTCAVFG LGGVGLSVIM GCKAAGASRI IAVDINKDKF PKAKEVGATE 

       250        260        270        280        290        300 
CINPQDYKKP IQEVIQEISD GGVDFSFEVI GRLDTVVAAL LSCHGACGTS VIVGVPPDSQ 

       310        320        330        340        350        360 
SLTVNPMLLL SGRTWKGAIF GGFKSKDSVP KLVADFMAKK FSLDPLITNV LPFEKINEGF 

       370 
DLLRSGKSIR TILTF 

« Hide

References

[1]"Isozyme developments in mammalian class-I alcohol dehydrogenase. cDNA cloning, functional correlations, and lack of evidence for genetic isozymes in rabbit."
Hoeoeg J.-O., Vagelopoulos N., Yip P.-K., Keung W.M., Joernvall H.
Eur. J. Biochem. 213:31-38(1993) [PubMed: 8477702] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.

Cross-references

Sequence databases

X69799 mRNA. Translation: CAA49458.1.
PIRS29343. S30353.
RefSeqNP_001095174.1.
UniGeneOcu.3250

3D structure databases

HSSPHSSP built from PDB template 1HT0 based on UniProtKB P00326.
SMRQ03505. Positions 2-375.
ModBaseSearch...

Genome annotation databases

GeneID100009283.

Phylogenomic databases

HOVERGENQ03505.

Enzyme and pathway databases

BRENDA1.1.1.1. 255.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH1_RABIT
AccessionPrimary (citable) accession number: Q03505
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents