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Reviewed, UniProtKB/Swiss-Prot P06757 (ADH1_RAT)

Last modified June 16, 2009. Version 85. 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 A subunit
Gene names
Name: Adh1
Synonyms: Adh-1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length376 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.

Subunit structure

Dimer of identical or non-identical chains of three types (A, B, C), which are coded by 3 separate genes at different loci.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 376375Alcohol dehydrogenase 1
PRO_0000160669

Regions

Nucleotide binding201 – 2066NAD By similarity
Nucleotide binding294 – 2963NAD By similarity

Sites

Metal binding471Zinc 1; catalytic
Metal binding681Zinc 1; catalytic
Metal binding981Zinc 2
Metal binding1011Zinc 2
Metal binding1041Zinc 2
Metal binding1121Zinc 2
Metal binding1761Zinc 1; catalytic
Binding site2251NAD By similarity
Binding site2301NAD By similarity
Binding site3711NAD By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.4

Experimental info

Sequence conflict1431I → L in AAA40681. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P06757-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3C7026C6D7C0ED76

FASTA37639,645
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWEPHK PFTIEDIEVA PPKAHEVRIK MVATGVCRSD DHAVSGSLFT 

        70         80         90        100        110        120 
PLPAVLGHEG AGIVESIGEG VTCVKPGDKV IPLFSPQCGK CRICKHPESN LCCQTKNLTQ 

       130        140        150        160        170        180 
PKGALLDGTS RFSCRGKPIH HFISTSTFSQ YTVVDDIAVA KIDAAAPLDK VCLIGCGFST 

       190        200        210        220        230        240 
GYGSAVQVAK VTPGSTCAVF GLGGVGLSVV IGCKTAGAAK IIAVDINKDK FAKAKELGAT 

       250        260        270        280        290        300 
DCINPQDYTK PIQEVLQEMT DGGVDFSFEV IGRLDTMTSA LLSCHSACGV SVIVGVPPSA 

       310        320        330        340        350        360 
QSLSVNPMSL LLGRTWKGAI FGGFKSKDAV PKLVADFMAK KFPLEPLITH VLPFEKINEA 

       370 
FDLLRAGKSI RTVLTF 

« Hide

References

« Hide 'large scale' references
[1]"Complete amino acid sequence of rat liver alcohol dehydrogenase deduced from the cDNA sequence."
Crabb D.W., Edenberg H.J.
Gene 48:287-291(1986) [PubMed: 2881847] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Structure and expression of the rat class I alcohol dehydrogenase gene."
Crabb D.W., Stein P.M., Dipple K.M., Hittle J.B., Sidhu R., Qulali M., Zhang K., Edenberg H.J.
Genomics 5:906-914(1989) [PubMed: 2591969] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[4]"Structural studies of alcohol dehydrogenase from rat liver."
Joernvall H., Markovic O.
Eur. J. Biochem. 29:167-174(1972) [PubMed: 4673366] [Abstract]
Cited for: ACETYLATION AT SER-2.
+Additional computationally mapped references.

Cross-references

Sequence databases

M29523 expand/collapse EMBL AC list , M29516, M29517, M29518, M29519, M29520, M29521, M29522 Genomic DNA. Translation: AAA85462.1.
M15327 mRNA. Translation: AAA40681.1.
BC062403 mRNA. Translation: AAH62403.1.
IPIIPI00331983.
PIRA26468.
RefSeqNP_062159.3.
UniGeneRn.40222

3D structure databases

HSSPHSSP built from PDB template 1HT0 based on UniProtKB P00326.
SMRP06757. Positions 2-376.
ModBaseSearch...

Proteomic databases

PRIDEP06757.

Genome annotation databases

EnsemblENSRNOG00000012464. Rattus norvegicus. [Contig view]
GeneID24172.
KEGGrno:24172.

Organism-specific databases

RGD2044. Adh1.

Phylogenomic databases

HOVERGENP06757.

Enzyme and pathway databases

BRENDA1.1.1.1. 248.

Gene expression databases

ArrayExpressP06757.
GermOnlineENSRNOG00000012464. Rattus norvegicus.

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...

Other Resources

NextBio602493.

Entry information

Entry nameADH1_RAT
AccessionPrimary (citable) accession number: P06757
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 85 of the entry and version 3 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