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Protein

Alcohol dehydrogenase class 4 mu/sigma chain

Gene

ADH7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Could function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism.

Miscellaneous

There are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.

Caution

It is uncertain whether Met-1 or Met-13 is the initiator.Curated

Catalytic activityi

A primary alcohol + NAD+ = an aldehyde + NADH.
A secondary alcohol + NAD+ = a ketone + NADH.

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Zinc 1; catalytic1
Metal bindingi80Zinc 1; catalytic1
Metal bindingi110Zinc 21
Metal bindingi113Zinc 21
Metal bindingi116Zinc 21
Metal bindingi124Zinc 21
Metal bindingi186Zinc 1; catalytic1
Binding sitei235NAD1 Publication1
Binding sitei240NAD1 Publication1
Binding sitei381NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi211 – 216NAD1 Publication6
Nucleotide bindingi304 – 306NAD1 Publication3

GO - Molecular functioni

  • alcohol dehydrogenase (NAD) activity Source: UniProtKB
  • alcohol dehydrogenase activity, zinc-dependent Source: UniProtKB
  • aldehyde oxidase activity Source: UniProtKB
  • ethanol binding Source: UniProtKB
  • receptor antagonist activity Source: UniProtKB
  • retinol binding Source: UniProtKB
  • retinol dehydrogenase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • ethanol catabolic process Source: Ensembl
  • ethanol oxidation Source: UniProtKB
  • fatty acid omega-oxidation Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • response to bacterium Source: UniProtKB
  • response to ethanol Source: UniProtKB
  • retinoic acid metabolic process Source: Ensembl
  • retinoid metabolic process Source: UniProtKB
  • retinol metabolic process Source: Ensembl

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-71384 Ethanol oxidation

Chemistry databases

SwissLipidsiSLP:000001879

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
Gastric alcohol dehydrogenase
Retinol dehydrogenase
Gene namesi
Name:ADH7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000196344.11
HGNCiHGNC:256 ADH7
MIMi600086 gene
neXtProtiNX_P40394

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi131
OpenTargetsiENSG00000196344
PharmGKBiPA24577

Chemistry databases

ChEMBLiCHEMBL3867
DrugBankiDB00898 Ethanol
DB00157 NADH

Polymorphism and mutation databases

BioMutaiADH7
DMDMi292495000

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001606911 – 386Alcohol dehydrogenase class 4 mu/sigma chainAdd BLAST386

Proteomic databases

PaxDbiP40394
PeptideAtlasiP40394
PRIDEiP40394

PTM databases

iPTMnetiP40394
PhosphoSitePlusiP40394

Expressioni

Tissue specificityi

Preferentially expressed in stomach.

Gene expression databases

BgeeiENSG00000196344
CleanExiHS_ADH7
ExpressionAtlasiP40394 baseline and differential
GenevisibleiP40394 HS

Organism-specific databases

HPAiHPA039695

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • receptor antagonist activity Source: UniProtKB

Protein-protein interaction databases

BioGridi106643, 4 interactors
STRINGi9606.ENSP00000420269

Chemistry databases

BindingDBiP40394

Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 29Combined sources10
Beta strandi35 – 41Combined sources7
Beta strandi48 – 57Combined sources10
Helixi60 – 67Combined sources8
Beta strandi68 – 70Combined sources3
Beta strandi74 – 76Combined sources3
Beta strandi81 – 89Combined sources9
Beta strandi101 – 104Combined sources4
Beta strandi111 – 113Combined sources3
Helixi114 – 117Combined sources4
Beta strandi142 – 150Combined sources9
Turni153 – 155Combined sources3
Beta strandi158 – 165Combined sources8
Helixi166 – 168Combined sources3
Beta strandi169 – 171Combined sources3
Helixi178 – 181Combined sources4
Helixi182 – 185Combined sources4
Helixi187 – 196Combined sources10
Beta strandi206 – 210Combined sources5
Helixi214 – 225Combined sources12
Beta strandi229 – 234Combined sources6
Helixi238 – 240Combined sources3
Helixi241 – 247Combined sources7
Beta strandi250 – 253Combined sources4
Helixi255 – 257Combined sources3
Helixi262 – 270Combined sources9
Beta strandi276 – 279Combined sources4
Helixi284 – 291Combined sources8
Turni296 – 298Combined sources3
Beta strandi300 – 303Combined sources4
Beta strandi313 – 315Combined sources3
Helixi318 – 321Combined sources4
Beta strandi325 – 328Combined sources4
Helixi331 – 333Combined sources3
Helixi336 – 347Combined sources12
Turni348 – 350Combined sources3
Helixi355 – 357Combined sources3
Beta strandi358 – 363Combined sources6
Helixi364 – 366Combined sources3
Helixi367 – 375Combined sources9
Beta strandi380 – 385Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGNX-ray3.00A/B/C/D14-386[»]
1D1SX-ray2.50A/B/C/D14-386[»]
1D1TX-ray2.40A/B/C/D14-386[»]
ProteinModelPortaliP40394
SMRiP40394
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40394

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022 Eukaryota
COG1062 LUCA
GeneTreeiENSGT00430000030800
HOGENOMiHOG000294674
HOVERGENiHBG000195
InParanoidiP40394
KOiK13951
OMAiSNETYNE
OrthoDBiEOG091G08N3
PhylomeDBiP40394
TreeFamiTF300429

Family and domain databases

InterProiView protein in InterPro
IPR013149 ADH_C
IPR013154 ADH_N
IPR002328 ADH_Zn_CS
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf
IPR028635 Zinc_ADH_IV
PANTHERiPTHR43880:SF2 PTHR43880:SF2, 1 hit
PfamiView protein in Pfam
PF08240 ADH_N, 1 hit
PF00107 ADH_zinc_N, 1 hit
SUPFAMiSSF50129 SSF50129, 2 hits
SSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00059 ADH_ZINC, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P40394-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFAEIQIQDK DRMGTAGKVI KCKAAVLWEQ KQPFSIEEIE VAPPKTKEVR
60 70 80 90 100
IKILATGICR TDDHVIKGTM VSKFPVIVGH EATGIVESIG EGVTTVKPGD
110 120 130 140 150
KVIPLFLPQC RECNACRNPD GNLCIRSDIT GRGVLADGTT RFTCKGKPVH
160 170 180 190 200
HFMNTSTFTE YTVVDESSVA KIDDAAPPEK VCLIGCGFST GYGAAVKTGK
210 220 230 240 250
VKPGSTCVVF GLGGVGLSVI MGCKSAGASR IIGIDLNKDK FEKAMAVGAT
260 270 280 290 300
ECISPKDSTK PISEVLSEMT GNNVGYTFEV IGHLETMIDA LASCHMNYGT
310 320 330 340 350
SVVVGVPPSA KMLTYDPMLL FTGRTWKGCV FGGLKSRDDV PKLVTEFLAK
360 370 380
KFDLDQLITH VLPFKKISEG FELLNSGQSI RTVLTF
Length:386
Mass (Da):41,481
Last modified:March 23, 2010 - v2
Checksum:iE34C959778ED6817
GO
Isoform 2 (identifier: P40394-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MFAEIQIQDKDRMGTAGK → MKCLVSRHTVRETLDMVFQRMSVEAG

Note: No experimental confirmation available.
Show »
Length:394
Mass (Da):42,467
Checksum:i2EBC96FC412B6729
GO

Sequence cautioni

The sequence AAA19002 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAC51351 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAG35707 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA53960 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA53961 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9D → E in AAA19002 (PubMed:8195208).Curated1
Sequence conflicti32Q → R AA sequence (PubMed:1592118).Curated1
Sequence conflicti83T → R AA sequence (PubMed:1592118).Curated1
Sequence conflicti110C → V in AAB38424 (PubMed:8824810).Curated1
Sequence conflicti150 – 151HH → GR AA sequence (PubMed:1592118).Curated2
Sequence conflicti160 – 161EY → VI in AAB38424 (PubMed:8824810).Curated2
Sequence conflicti169V → E in AAB38424 (PubMed:8824810).Curated1
Sequence conflicti175A → T in BAG35707 (PubMed:14702039).Curated1
Sequence conflicti217L → V in AAB38424 (PubMed:8824810).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02436492G → A. Corresponds to variant dbSNP:rs1573496Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0430931 – 18MFAEI…GTAGK → MKCLVSRHTVRETLDMVFQR MSVEAG in isoform 2. 1 PublicationAdd BLAST18

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76342 mRNA Translation: CAA53961.1 Different initiation.
X76342 mRNA Translation: CAA53960.1 Different initiation.
U07821 mRNA Translation: AAA19002.1 Different initiation.
U16293
, U16286, U16287, U16288, U16289, U16290, U16291, U16292 Genomic DNA Translation: AAC51351.1 Different initiation.
AK301696 mRNA Translation: BAG63168.1
AK312854 mRNA Translation: BAG35707.1 Different initiation.
AP001960 Genomic DNA No translation available.
CH471057 Genomic DNA Translation: EAX06101.1
BC131512 mRNA Translation: AAI31513.1
L33179 mRNA Translation: AAA59211.1
U09623 mRNA Translation: AAA82165.1
L47166 Genomic DNA Translation: AAB38424.1
S77168 mRNA Translation: AAB34478.1
CCDSiCCDS34034.1 [P40394-1]
CCDS54781.1 [P40394-2]
PIRiA55878 DEHUAS
RefSeqiNP_000664.2, NM_000673.4 [P40394-1]
NP_001159976.1, NM_001166504.1 [P40394-2]
UniGeneiHs.389

Genome annotation databases

EnsembliENST00000209665; ENSP00000209665; ENSG00000196344 [P40394-1]
ENST00000476959; ENSP00000420269; ENSG00000196344 [P40394-2]
GeneIDi131
KEGGihsa:131
UCSCiuc003huv.2 human [P40394-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiADH7_HUMAN
AccessioniPrimary (citable) accession number: P40394
Secondary accession number(s): A2RRB6
, A8MVN9, B2R760, B4DWV6, Q13713
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: March 23, 2010
Last modified: March 28, 2018
This is version 172 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health