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Protein

Alcohol dehydrogenase class 4 mu/sigma chain

Gene

Adh7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Zinc 1; catalyticBy similarity
Metal bindingi68 – 681Zinc 1; catalyticBy similarity
Metal bindingi98 – 981Zinc 2By similarity
Metal bindingi101 – 1011Zinc 2By similarity
Metal bindingi104 – 1041Zinc 2By similarity
Metal bindingi112 – 1121Zinc 2By similarity
Metal bindingi174 – 1741Zinc 1; catalyticBy similarity
Binding sitei223 – 2231NADBy similarity
Binding sitei228 – 2281NADBy similarity
Binding sitei369 – 3691NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi199 – 2046NADBy similarity
Nucleotide bindingi292 – 2943NADBy similarity

GO - Molecular functioni

  • alcohol dehydrogenase (NAD) activity Source: RGD
  • ethanol binding Source: RGD
  • NAD binding Source: RGD
  • protein homodimerization activity Source: RGD
  • retinol binding Source: RGD
  • zinc ion binding Source: RGD

GO - Biological processi

  • ethanol metabolic process Source: RGD
  • retinoid metabolic process Source: RGD
  • retinol metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class 4 mu/sigma chain (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase class IV mu/sigma chain
Gene namesi
Name:Adh7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621638. Adh7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Alcohol dehydrogenase class 4 mu/sigma chainPRO_0000160696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCurated

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP41682.
PRIDEiP41682.

PTM databases

iPTMnetiP41682.

Expressioni

Tissue specificityi

Preferentially expressed in stomach.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015870.

Structurei

3D structure databases

ProteinModelPortaliP41682.
SMRiP41682. Positions 3-374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP41682.
KOiK13951.
PhylomeDBiP41682.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41682-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTAGKVIKC KAAVLWGTNQ PFSIEDIEVA PPKAKEVRVK ILATGICGTD
60 70 80 90 100
DHVIKGTMVS KFPVIVGHEA VGIVESVGEE VTTVRPGDKV IPLFLPQCRE
110 120 130 140 150
CNPCRNPEGN LCIRSDLTGR GVLADGTTRF TCKGKPVQHF MNTSTFTEYT
160 170 180 190 200
VLDESSVAKI DAEAPPEKAC LIGCGFSTGY GAAVKTAKVS PGSTCAVFGL
210 220 230 240 250
GGVGLSVVMG CKAAGASRII GIDINKDKFQ KALDVGATEC INPRDFTKPI
260 270 280 290 300
SEVLSDMTGN TVQYTFEVIG RLETMVDALS SCHMNYGTSV VVGAPPSAKM
310 320 330 340 350
LSYDPMLLFT GRTWKGCVFG GWKSRDDVPK LVTEFLEKKF DLGQLITHTL
360 370
PFHNISEGFE LLYSGQSIRT VLTF
Length:374
Mass (Da):40,105
Last modified:July 15, 1999 - v2
Checksum:iDD745E7FCB01E452
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 44MDTA → SNRV AA sequence (PubMed:8127901).Curated
Sequence conflicti109 – 1091G → E in CAA67297 (PubMed:10829036).Curated
Sequence conflicti208 – 2081V → I AA sequence (PubMed:8127901).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98746 mRNA. Translation: CAA67297.1.
PIRiA53142.
RefSeqiNP_599156.1. NM_134329.1.
UniGeneiRn.42935.

Genome annotation databases

GeneIDi171178.
KEGGirno:171178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98746 mRNA. Translation: CAA67297.1.
PIRiA53142.
RefSeqiNP_599156.1. NM_134329.1.
UniGeneiRn.42935.

3D structure databases

ProteinModelPortaliP41682.
SMRiP41682. Positions 3-374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015870.

PTM databases

iPTMnetiP41682.

Proteomic databases

PaxDbiP41682.
PRIDEiP41682.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi171178.
KEGGirno:171178.

Organism-specific databases

CTDi131.
RGDi621638. Adh7.

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP41682.
KOiK13951.
PhylomeDBiP41682.

Miscellaneous databases

NextBioi622023.
PROiP41682.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mammalian class IV alcohol dehydrogenase (stomach alcohol dehydrogenase): structure, origin, and correlation with enzymology."
    Pares X., Cederlund E., Moreno A., Hjelmqvist L., Farres J., Joernvall H.
    Proc. Natl. Acad. Sci. U.S.A. 91:1893-1897(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Stomach.
  2. "Molecular basis for differential substrate specificity in class IV alcohol dehydrogenases: a conserved function in retinoid metabolism but not in ethanol oxidation."
    Crosas B., Allali-Hassani A., Martinez S.E., Martras S., Persson B., Jornvall H., Pares X., Farres J.
    J. Biol. Chem. 275:25180-25187(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Lung.

Entry informationi

Entry nameiADH7_RAT
AccessioniPrimary (citable) accession number: P41682
Secondary accession number(s): O55146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 15, 1999
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.