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P40394

- ADH7_HUMAN

UniProt

P40394 - ADH7_HUMAN

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
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (23 Mar 2010)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiP40394.
    BgeeiP40394.
    CleanExiHS_ADH7.
    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.
    HOGENOMiHOG000294674.
    HOVERGENiHBG000195.
    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

    MFAEIQIQDK DRMGTAGKVI KCKAAVLWEQ KQPFSIEEIE VAPPKTKEVR    50
    IKILATGICR TDDHVIKGTM VSKFPVIVGH EATGIVESIG EGVTTVKPGD 100
    KVIPLFLPQC RECNACRNPD GNLCIRSDIT GRGVLADGTT RFTCKGKPVH 150
    HFMNTSTFTE YTVVDESSVA KIDDAAPPEK VCLIGCGFST GYGAAVKTGK 200
    VKPGSTCVVF GLGGVGLSVI MGCKSAGASR IIGIDLNKDK FEKAMAVGAT 250
    ECISPKDSTK PISEVLSEMT GNNVGYTFEV IGHLETMIDA LASCHMNYGT 300
    SVVVGVPPSA KMLTYDPMLL FTGRTWKGCV FGGLKSRDDV PKLVTEFLAK 350
    KFDLDQLITH VLPFKKISEG FELLNSGQSI RTVLTF 386
    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.
    HOGENOMi HOG000294674.
    HOVERGENi HBG000195.
    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

    ArrayExpressi P40394.
    Bgeei P40394.
    CleanExi HS_ADH7.
    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

    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 1, 2014
    This is version 144 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