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P00326

- ADH1G_HUMAN

UniProt

P00326 - ADH1G_HUMAN

Protein

Alcohol dehydrogenase 1C

Gene

ADH1C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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 bindingi47 – 471Zinc 1; catalytic
    Metal bindingi68 – 681Zinc 1; catalytic
    Metal bindingi98 – 981Zinc 2
    Metal bindingi101 – 1011Zinc 2
    Metal bindingi104 – 1041Zinc 2
    Metal bindingi112 – 1121Zinc 2
    Metal bindingi175 – 1751Zinc 1; catalytic
    Binding sitei224 – 2241NAD2 Publications
    Binding sitei229 – 2291NAD2 Publications
    Binding sitei370 – 3701NAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi200 – 2056NAD2 Publications
    Nucleotide bindingi293 – 2953NAD2 Publications

    GO - Molecular functioni

    1. alcohol dehydrogenase (NAD) activity Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. ethanol oxidation Source: UniProtKB
    2. small molecule metabolic process Source: Reactome
    3. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_34. Ethanol oxidation.
    SABIO-RKP00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase 1C (EC:1.1.1.1)
    Alternative name(s):
    Alcohol dehydrogenase subunit gamma
    Gene namesi
    Name:ADH1C
    Synonyms:ADH3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:251. ADH1C.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24572.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 375374Alcohol dehydrogenase 1CPRO_0000160664Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP00326.

    PTM databases

    PhosphoSiteiP00326.

    Expressioni

    Gene expression databases

    CleanExiHS_ADH1C.
    GenevestigatoriP00326.

    Interactioni

    Subunit structurei

    Dimer of identical or non-identical chains of three types; alpha, beta and gamma.2 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000209668.

    Structurei

    Secondary structure

    1
    375
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 158
    Beta strandi23 – 297
    Beta strandi36 – 4510
    Helixi48 – 547
    Beta strandi62 – 654
    Beta strandi69 – 779
    Beta strandi89 – 924
    Beta strandi99 – 1013
    Helixi102 – 1054
    Beta strandi117 – 1193
    Beta strandi131 – 1333
    Beta strandi136 – 1394
    Turni142 – 1443
    Beta strandi147 – 1548
    Helixi155 – 1573
    Beta strandi158 – 1603
    Helixi167 – 1704
    Helixi171 – 1744
    Helixi176 – 18510
    Turni186 – 1883
    Beta strandi195 – 1995
    Helixi203 – 21412
    Beta strandi218 – 2236
    Helixi227 – 2293
    Helixi230 – 2356
    Beta strandi239 – 2424
    Helixi244 – 2463
    Helixi251 – 2588
    Turni259 – 2613
    Beta strandi262 – 2687
    Helixi273 – 28210
    Turni285 – 2873
    Beta strandi289 – 2924
    Beta strandi302 – 3043
    Helixi307 – 3104
    Beta strandi314 – 3174
    Helixi320 – 3223
    Helixi325 – 33713
    Helixi344 – 3463
    Beta strandi347 – 3526
    Helixi353 – 3553
    Helixi356 – 3649
    Beta strandi369 – 3746

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DDAmodel-A/B1-375[»]
    1HT0X-ray2.00A/B2-375[»]
    1U3WX-ray1.45A/B2-375[»]
    ProteinModelPortaliP00326.
    SMRiP00326. Positions 2-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00326.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG000195.
    InParanoidiP00326.
    KOiK13951.

    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.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00326-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD    50
    EHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK 100
    CRICKNPESN YCLKNDLGNP RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY 150
    TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG 200
    LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP 250
    IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ 300
    NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI 350
    LPFEKINEGF DLLRSGKSIR TVLTF 375
    Length:375
    Mass (Da):39,868
    Last modified:January 23, 2007 - v2
    Checksum:i414D73CC4C104C84
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301Missing AA sequence (PubMed:6391921)Curated
    Sequence conflicti171 – 1711C → R in AAH67421. (PubMed:15489334)Curated

    Polymorphismi

    Two main alleles are known, ADH3*1 or gamma-1 has Arg-272/Ile-350 while ADH3*2 or gamma-2 has Gln-272/Val-350. ADH3*1 is associated with a fast rate of ethanol oxidation and ADH3*2 with a slow rate.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481R → H.1 Publication
    Corresponds to variant rs35385902 [ dbSNP | Ensembl ].
    VAR_023992
    Natural varianti166 – 1661P → S.1 Publication
    VAR_023993
    Natural varianti272 – 2721R → Q in allele ADH3*2/gamma-2. 3 Publications
    Corresponds to variant rs1693482 [ dbSNP | Ensembl ].
    VAR_000428
    Natural varianti350 – 3501I → V in allele ADH3*2/gamma-2. 3 Publications
    Corresponds to variant rs698 [ dbSNP | Ensembl ].
    VAR_000429
    Natural varianti352 – 3521P → T.1 Publication
    Corresponds to variant rs35719513 [ dbSNP | Ensembl ].
    VAR_023994

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04299 mRNA. Translation: CAA27842.1.
    X04350 mRNA. Translation: CAA27876.1.
    M12272 mRNA. Translation: AAC41757.1.
    D11067 Genomic DNA. Translation: BAC06856.1.
    DQ088981 Genomic DNA. Translation: AAY68222.1.
    AC097530 Genomic DNA. No translation available.
    BC062476 mRNA. Translation: AAH62476.1.
    BC066227 mRNA. Translation: AAH66227.1.
    BC066228 mRNA. Translation: AAH66228.1.
    BC067419 mRNA. Translation: AAH67419.1.
    BC067420 mRNA. Translation: AAH67420.1.
    BC067421 mRNA. Translation: AAH67421.1.
    BC067422 mRNA. Translation: AAH67422.1.
    BC074771 mRNA. Translation: AAH74771.1.
    BC074786 mRNA. Translation: AAH74786.1.
    PIRiC25428. DEHUAG.
    RefSeqiNP_000660.1. NM_000669.4.
    UniGeneiHs.654537.

    Genome annotation databases

    GeneIDi126.
    KEGGihsa:126.
    UCSCiuc031sgp.1. human.

    Polymorphism databases

    DMDMi113398.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04299 mRNA. Translation: CAA27842.1 .
    X04350 mRNA. Translation: CAA27876.1 .
    M12272 mRNA. Translation: AAC41757.1 .
    D11067 Genomic DNA. Translation: BAC06856.1 .
    DQ088981 Genomic DNA. Translation: AAY68222.1 .
    AC097530 Genomic DNA. No translation available.
    BC062476 mRNA. Translation: AAH62476.1 .
    BC066227 mRNA. Translation: AAH66227.1 .
    BC066228 mRNA. Translation: AAH66228.1 .
    BC067419 mRNA. Translation: AAH67419.1 .
    BC067420 mRNA. Translation: AAH67420.1 .
    BC067421 mRNA. Translation: AAH67421.1 .
    BC067422 mRNA. Translation: AAH67422.1 .
    BC074771 mRNA. Translation: AAH74771.1 .
    BC074786 mRNA. Translation: AAH74786.1 .
    PIRi C25428. DEHUAG.
    RefSeqi NP_000660.1. NM_000669.4.
    UniGenei Hs.654537.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DDA model - A/B 1-375 [» ]
    1HT0 X-ray 2.00 A/B 2-375 [» ]
    1U3W X-ray 1.45 A/B 2-375 [» ]
    ProteinModelPortali P00326.
    SMRi P00326. Positions 2-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000209668.

    Chemistry

    BindingDBi P00326.
    ChEMBLi CHEMBL3285.
    DrugBanki DB00898. Ethanol.
    DB01213. Fomepizole.

    PTM databases

    PhosphoSitei P00326.

    Polymorphism databases

    DMDMi 113398.

    Proteomic databases

    PRIDEi P00326.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 126.
    KEGGi hsa:126.
    UCSCi uc031sgp.1. human.

    Organism-specific databases

    CTDi 126.
    GeneCardsi GC04M100257.
    HGNCi HGNC:251. ADH1C.
    MIMi 103730. gene.
    neXtProti NX_P00326.
    PharmGKBi PA24572.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG000195.
    InParanoidi P00326.
    KOi K13951.

    Enzyme and pathway databases

    Reactomei REACT_34. Ethanol oxidation.
    SABIO-RK P00326.

    Miscellaneous databases

    EvolutionaryTracei P00326.
    GeneWikii ADH1C.
    GenomeRNAii 126.
    NextBioi 503.
    PROi P00326.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_ADH1C.
    Genevestigatori P00326.

    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.
    [Graphical view ]
    PANTHERi PTHR11695. PTHR11695. 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. "The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties."
      Hoeoeg J.-O., Heden L.-O., Larsson K., Joernvall H.
      Eur. J. Biochem. 159:215-218(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GAMMA-2 GLN-272 AND VAL-350.
      Tissue: Liver.
    2. "Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence."
      Ikuta T., Szeto S., Yoshida A.
      Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "Molecular structure of the human alcohol dehydrogenase 3 gene."
      Yokoyama S., Matsuo Y., Rajasekharan S., Yokoyama R.
      Jpn. J. Genet. 67:167-171(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. NIEHS SNPs program
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-48; SER-166; GLN-272; VAL-350 AND THR-352.
    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. "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], VARIANTS GAMMA-2 GLN-272 AND VAL-350.
      Tissue: Brain and Femoral artery.
    7. "Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain."
      Buhler R., Hempel J., Kaiser R., de Zalenski C., von Wartburg J.-P., Joernvall H.
      Eur. J. Biochem. 145:447-453(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
      Tissue: Liver.
    8. "Three-dimensional structures of the three human class I alcohol dehydrogenases."
      Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.
      Protein Sci. 10:697-706(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.
    9. "Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors."
      Gibbons B.J., Hurley T.D.
      Biochemistry 43:12555-12562(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.

    Entry informationi

    Entry nameiADH1G_HUMAN
    AccessioniPrimary (citable) accession number: P00326
    Secondary accession number(s): Q4PJ18
    , Q5WRV0, Q6LBW4, Q6NWV0, Q6NZA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 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.

    Caution

    The reference genome assembly, GRCh37, describes a non-functional copy of that gene with a stop codon at position 78. However, this premature stop codon is not present in available mRNAs.Curated

    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