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P40394

- ADH7_HUMAN

UniProt

P40394 - ADH7_HUMAN

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Protein

Alcohol dehydrogenase class 4 mu/sigma chain

Gene

ADH7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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.

Catalytic activityi

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

Cofactori

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Zinc 1; catalytic
Metal bindingi80 – 801Zinc 1; catalytic
Metal bindingi110 – 1101Zinc 2
Metal bindingi113 – 1131Zinc 2
Metal bindingi116 – 1161Zinc 2
Metal bindingi124 – 1241Zinc 2
Metal bindingi186 – 1861Zinc 1; catalytic
Binding sitei235 – 2351NAD1 Publication
Binding sitei240 – 2401NAD1 Publication
Binding sitei381 – 3811NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi211 – 2166NAD1 Publication
Nucleotide bindingi304 – 3063NAD1 Publication

GO - Molecular functioni

  1. alcohol dehydrogenase (NAD) activity Source: UniProtKB
  2. alcohol dehydrogenase activity, zinc-dependent Source: UniProtKB
  3. aldehyde oxidase activity Source: UniProtKB
  4. ethanol binding Source: UniProtKB
  5. receptor antagonist activity Source: UniProtKB
  6. retinol binding Source: UniProtKB
  7. retinol dehydrogenase activity Source: UniProtKB
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. ethanol catabolic process Source: Ensembl
  2. ethanol oxidation Source: UniProtKB
  3. extracellular negative regulation of signal transduction Source: GOC
  4. fatty acid omega-oxidation Source: UniProtKB
  5. oxidation-reduction process Source: UniProtKB
  6. response to bacterium Source: UniProtKB
  7. response to ethanol Source: UniProtKB
  8. retinoic acid metabolic process Source: Ensembl
  9. retinoid metabolic process Source: UniProtKB
  10. retinol metabolic process Source: Ensembl
  11. small molecule metabolic process Source: Reactome
  12. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiREACT_34. Ethanol oxidation.

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
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:256. ADH7.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular region Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24577.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Alcohol dehydrogenase class 4 mu/sigma chainPRO_0000160691Add
BLAST

Proteomic databases

PaxDbiP40394.
PRIDEiP40394.

PTM databases

PhosphoSiteiP40394.

Expressioni

Tissue specificityi

Preferentially expressed in stomach.

Gene expression databases

BgeeiP40394.
CleanExiHS_ADH7.
ExpressionAtlasiP40394. baseline and differential.
GenevestigatoriP40394.

Organism-specific databases

HPAiHPA039695.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi106643. 3 interactions.
STRINGi9606.ENSP00000209665.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 2910
Beta strandi35 – 417
Beta strandi48 – 5710
Helixi60 – 678
Beta strandi68 – 703
Beta strandi74 – 763
Beta strandi81 – 899
Beta strandi101 – 1044
Beta strandi111 – 1133
Helixi114 – 1174
Beta strandi142 – 1509
Turni153 – 1553
Beta strandi158 – 1658
Helixi166 – 1683
Beta strandi169 – 1713
Helixi178 – 1814
Helixi182 – 1854
Helixi187 – 19610
Beta strandi206 – 2105
Helixi214 – 22512
Beta strandi229 – 2346
Helixi238 – 2403
Helixi241 – 2477
Beta strandi250 – 2534
Helixi255 – 2573
Helixi262 – 2709
Beta strandi276 – 2794
Helixi284 – 2918
Turni296 – 2983
Beta strandi300 – 3034
Beta strandi313 – 3153
Helixi318 – 3214
Beta strandi325 – 3284
Helixi331 – 3333
Helixi336 – 34712
Turni348 – 3503
Helixi355 – 3573
Beta strandi358 – 3636
Helixi364 – 3663
Helixi367 – 3759
Beta strandi380 – 3856

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 14-386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40394.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1062.
GeneTreeiENSGT00430000030800.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP40394.
KOiK13951.
OMAiPFKQINE.
OrthoDBiEOG72NRQ6.
PhylomeDBiP40394.
TreeFamiTF300429.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR028635. Zinc_ADH_IV.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PTHR11695:SF406. PTHR11695:SF406. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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 AAA19002.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAC51351.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAG35707.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA53960.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA53961.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91D → E in AAA19002. (PubMed:8195208)Curated
Sequence conflicti32 – 321Q → R AA sequence (PubMed:1592118)Curated
Sequence conflicti83 – 831T → R AA sequence (PubMed:1592118)Curated
Sequence conflicti110 – 1101C → V in AAB38424. (PubMed:8824810)Curated
Sequence conflicti150 – 1512HH → GR AA sequence (PubMed:1592118)Curated
Sequence conflicti160 – 1612EY → VI in AAB38424. (PubMed:8824810)Curated
Sequence conflicti169 – 1691V → E in AAB38424. (PubMed:8824810)Curated
Sequence conflicti175 – 1751A → T in BAG35707. (PubMed:14702039)Curated
Sequence conflicti217 – 2171L → V in AAB38424. (PubMed:8824810)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921G → A.
Corresponds to variant rs1573496 [ dbSNP | Ensembl ].
VAR_024364

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1818MFAEI…GTAGK → MKCLVSRHTVRETLDMVFQR MSVEAG in isoform 2. 1 PublicationVSP_043093Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000437033; ENSP00000414254; ENSG00000196344.
ENST00000476959; ENSP00000420269; ENSG00000196344. [P40394-2]
GeneIDi131.
KEGGihsa:131.
UCSCiuc003huv.2. human. [P40394-1]
uc021xqj.1. human. [P40394-2]

Polymorphism databases

DMDMi292495000.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS34034.1. [P40394-1 ]
CCDS54781.1. [P40394-2 ]
PIRi A55878. DEHUAS.
RefSeqi NP_000664.2. NM_000673.4. [P40394-1 ]
NP_001159976.1. NM_001166504.1. [P40394-2 ]
UniGenei Hs.389.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AGN X-ray 3.00 A/B/C/D 14-386 [» ]
1D1S X-ray 2.50 A/B/C/D 14-386 [» ]
1D1T X-ray 2.40 A/B/C/D 14-386 [» ]
ProteinModelPortali P40394.
SMRi P40394. Positions 14-386.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106643. 3 interactions.
STRINGi 9606.ENSP00000209665.

Chemistry

BindingDBi P40394.
ChEMBLi CHEMBL3867.

PTM databases

PhosphoSitei P40394.

Polymorphism databases

DMDMi 292495000.

Proteomic databases

PaxDbi P40394.
PRIDEi P40394.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000209665 ; ENSP00000209665 ; ENSG00000196344 . [P40394-1 ]
ENST00000437033 ; ENSP00000414254 ; ENSG00000196344 .
ENST00000476959 ; ENSP00000420269 ; ENSG00000196344 . [P40394-2 ]
GeneIDi 131.
KEGGi hsa:131.
UCSCi uc003huv.2. human. [P40394-1 ]
uc021xqj.1. human. [P40394-2 ]

Organism-specific databases

CTDi 131.
GeneCardsi GC04M100333.
HGNCi HGNC:256. ADH7.
HPAi HPA039695.
MIMi 600086. gene.
neXtProti NX_P40394.
PharmGKBi PA24577.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1062.
GeneTreei ENSGT00430000030800.
HOGENOMi HOG000294674.
HOVERGENi HBG000195.
InParanoidi P40394.
KOi K13951.
OMAi PFKQINE.
OrthoDBi EOG72NRQ6.
PhylomeDBi P40394.
TreeFami TF300429.

Enzyme and pathway databases

Reactomei REACT_34. Ethanol oxidation.

Miscellaneous databases

EvolutionaryTracei P40394.
GeneWikii ADH7.
GenomeRNAii 131.
NextBioi 523.
PROi P40394.
SOURCEi Search...

Gene expression databases

Bgeei P40394.
CleanExi HS_ADH7.
ExpressionAtlasi P40394. baseline and differential.
Genevestigatori P40394.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProi IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR028635. Zinc_ADH_IV.
[Graphical view ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
PTHR11695:SF406. PTHR11695:SF406. 1 hit.
Pfami PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 2 hits.
PROSITEi PS00059. ADH_ZINC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships."
    Farres J., Moreno A., Crosas B., Peralba J.M., Allali-Hassani A., Hjelmqvist L., Joernvall H., Pares X.
    Eur. J. Biochem. 224:549-557(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Stomach.
  2. "The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene."
    Satre M.A., Zgombic-Knight M., Duester G.
    J. Biol. Chem. 269:15606-15612(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Stomach.
  3. "Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro."
    Zgombic-Knight M., Foglio M.H., Duester G.
    J. Biol. Chem. 270:4305-4311(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Esophagus and Trachea.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7)."
    Yokoyama S., Matsuo Y., Ramsbotham R., Yokoyama R.
    FEBS Lett. 351:411-415(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-386 (ISOFORM 1), ZINC-BINDING SITES.
    Tissue: Stomach.
  9. "Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes."
    Kedishvili N.Y., Bosron W.F., Stone C.L., Hurley T.D., Peggs C.F., Thomasson H.R., Popov K.M., Carr L.G., Edenberg H.J., Li T.K.
    J. Biol. Chem. 270:3625-3630(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-386 (ISOFORM 1).
    Tissue: Stomach.
  10. "Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH."
    Yokoyama H., Baraona E., Lieber C.S.
    Genomics 31:243-245(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-386.
    Tissue: Foreskin.
  11. "Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class."
    Pares X., Cederlund E., Moreno A., Saubi N., Hoeoeg J.-O., Joernvall H.
    FEBS Lett. 303:69-72(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-33; 53-58; 74-92; 97-123; 147-154 AND 181-186.
  12. "Human stomach class IV alcohol dehydrogenase: molecular genetic analysis."
    Cheung B., Anderson J.K., Holmes R.S., Beacham I.R.
    Alcohol. Clin. Exp. Res. 19:185-186(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 239-311 (ISOFORM 1).
    Tissue: Stomach.
  13. "X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity."
    Xie P., Parsons S.H., Speckhard D.C., Bosron W.F., Hurley T.D.
    J. Biol. Chem. 272:18558-18563(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 14-386.
  14. "Methionine-141 directly influences the binding of 4-methylpyrazole in human sigma sigma alcohol dehydrogenase."
    Xie P.T., Hurley T.D.
    Protein Sci. 8:2639-2644(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-386 IN COMPLEX WITH NAD AND ZINC IONS.

Entry informationi

Entry nameiADH7_HUMAN
AccessioniPrimary (citable) accession number: P40394
Secondary accession number(s): A2RRB6
, A8MVN9, B2R760, B4DWV6, Q13713
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: March 23, 2010
Last modified: October 29, 2014
This is version 145 of the entry and version 2 of the sequence. [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

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3