ID   ADH1A_HUMAN             Reviewed;         375 AA.
AC   P07327; A8K3E3; Q17R68;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   19-JAN-2010, entry version 115.
DE   RecName: Full=Alcohol dehydrogenase 1A;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase subunit alpha;
GN   Name=ADH1A; Synonyms=ADH1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-375.
RC   TISSUE=Liver;
RX   MEDLINE=86243367; PubMed=3013304; DOI=10.1021/bi00357a026;
RA   von Bahr-Lindstroem H., Hoeoeg J.-O., Heden L.-O., Kaiser R.,
RA   Fleetwood L., Larsson K., Lake M., Holmquist B., Holmgren A.,
RA   Hempel J., Vallee B.L., Joernvall H.;
RT   "cDNA and protein structure for the alpha subunit of human liver
RT   alcohol dehydrogenase.";
RL   Biochemistry 25:2465-2470(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86120995; PubMed=2935875; DOI=10.1073/pnas.83.3.634;
RA   Ikuta T., Szeto S., Yoshida A.;
RT   "Three human alcohol dehydrogenase subunits: cDNA structure and
RT   molecular and evolutionary divergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89153548; PubMed=2920825; DOI=10.1016/0014-5793(89)81217-7;
RA   Matsuo Y., Yokoyama S.;
RT   "Molecular structure of the human alcohol dehydrogenase 1 gene.";
RL   FEBS Lett. 243:57-60(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX   MEDLINE=90269803; PubMed=2347582; DOI=10.1016/0888-7543(90)90535-3;
RA   Yasunami M., Kikuchi I., Sarapata D., Yoshida A.;
RT   "The human class I alcohol dehydrogenase gene cluster: three genes are
RT   tandemly organized in an 80-kb-long segment of the genome.";
RL   Genomics 7:152-158(1990).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC
RP   IONS.
RX   PubMed=15449945; DOI=10.1021/bi0489107;
RA   Gibbons B.J., Hurley T.D.;
RT   "Structure of three class I human alcohol dehydrogenases complexed
RT   with isoenzyme specific formamide inhibitors.";
RL   Biochemistry 43:12555-12562(2004).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC
RP   IONS.
RX   MEDLINE=21172416; PubMed=11274460; DOI=10.1110/ps.45001;
RA   Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.;
RT   "Three-dimensional structures of the three human class I alcohol
RT   dehydrogenases.";
RL   Protein Sci. 10:697-706(2001).
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit.
CC   -!- SUBUNIT: Dimer of identical or non-identical chains of three
CC       types; alpha, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: There are 7 different ADH's isozymes in human:
CC       three belongs to class-I: alpha, beta, and gamma, one to class-II:
CC       pi, one to class-III: chi, one to class-IV: ADH7 and one to class-
CC       V: ADH6.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/adh1a/";
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DR   EMBL; M12963; AAA51590.1; -; mRNA.
DR   EMBL; M12271; AAA68131.1; -; mRNA.
DR   EMBL; BT019812; AAV38615.1; -; mRNA.
DR   EMBL; AY948115; AAX20115.1; -; Genomic_DNA.
DR   EMBL; AK290558; BAF83247.1; -; mRNA.
DR   EMBL; CH471057; EAX06094.1; -; Genomic_DNA.
DR   EMBL; BC074738; AAH74738.1; -; mRNA.
DR   EMBL; BC117442; AAI17443.1; -; mRNA.
DR   EMBL; BC126306; AAI26307.1; -; mRNA.
DR   EMBL; M37066; AAA51591.1; -; Genomic_DNA.
DR   IPI; IPI00218896; -.
DR   PIR; S02265; DEHUAA.
DR   RefSeq; NP_000658.1; -.
DR   UniGene; Hs.654433; -.
DR   PDB; 1HSO; X-ray; 2.50 A; A/B=2-375.
DR   PDB; 1U3T; X-ray; 2.49 A; A/B=2-375.
DR   PDBsum; 1HSO; -.
DR   PDBsum; 1U3T; -.
DR   STRING; P07327; -.
DR   PRIDE; P07327; -.
DR   Ensembl; ENST00000209668; ENSP00000209668; ENSG00000187758; Homo sapiens.
DR   GeneID; 124; -.
DR   KEGG; hsa:124; -.
DR   UCSC; uc003hur.1; human.
DR   CTD; 124; -.
DR   GeneCards; GC04M100450; -.
DR   H-InvDB; HIX0031477; -.
DR   HGNC; HGNC:249; ADH1A.
DR   HPA; CAB009562; -.
DR   MIM; 103700; gene.
DR   PharmGKB; PA24570; -.
DR   eggNOG; prNOG19139; -.
DR   HOGENOM; HBG753318; -.
DR   HOVERGEN; P07327; -.
DR   InParanoid; P07327; -.
DR   OMA; NPQGTLQ; -.
DR   OrthoDB; EOG9K0T6S; -.
DR   PhylomeDB; P07327; -.
DR   BRENDA; 1.1.1.1; 247.
DR   Reactome; REACT_13433; Biological oxidations.
DR   DrugBank; DB01213; Fomepizole.
DR   DrugBank; DB00157; NADH.
DR   NextBio; 495; -.
DR   ArrayExpress; P07327; -.
DR   Bgee; P07327; -.
DR   CleanEx; HS_ADH1A; -.
DR   Genevestigator; P07327; -.
DR   GermOnline; ENSG00000187758; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0030528; F:transcription regulator activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006066; P:alcohol metabolic process; NAS:UniProtKB.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013154; ADH_GroES-like.
DR   InterPro; IPR002085; ADH_SF_Zn.
DR   InterPro; IPR013149; ADH_Zn-bd.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    375       Alcohol dehydrogenase 1A.
FT                                /FTId=PRO_0000160658.
FT   NP_BIND     200    205       NAD.
FT   NP_BIND     293    295       NAD.
FT   METAL        47     47       Zinc 1; catalytic.
FT   METAL        68     68       Zinc 1; catalytic.
FT   METAL        98     98       Zinc 2.
FT   METAL       101    101       Zinc 2.
FT   METAL       104    104       Zinc 2.
FT   METAL       112    112       Zinc 2.
FT   METAL       175    175       Zinc 1; catalytic.
FT   BINDING     224    224       NAD.
FT   BINDING     229    229       NAD.
FT   BINDING     370    370       NAD.
FT   MOD_RES       2      2       N-acetylserine.
FT   STRAND        8     15
FT   STRAND       23     29
FT   STRAND       36     45
FT   HELIX        48     54
FT   STRAND       62     65
FT   STRAND       69     77
FT   STRAND       89     92
FT   STRAND       99    101
FT   HELIX       102    105
FT   STRAND      116    119
FT   STRAND      131    133
FT   STRAND      136    139
FT   TURN        142    144
FT   STRAND      147    154
FT   HELIX       155    157
FT   STRAND      158    160
FT   HELIX       167    170
FT   HELIX       171    174
FT   HELIX       176    185
FT   TURN        186    188
FT   STRAND      195    199
FT   HELIX       203    214
FT   STRAND      218    223
FT   HELIX       227    229
FT   HELIX       230    235
FT   STRAND      239    242
FT   HELIX       244    246
FT   HELIX       251    258
FT   TURN        259    261
FT   STRAND      263    268
FT   HELIX       273    282
FT   TURN        285    287
FT   STRAND      289    292
FT   STRAND      302    304
FT   HELIX       307    310
FT   STRAND      314    317
FT   HELIX       320    322
FT   HELIX       325    337
FT   HELIX       344    346
FT   STRAND      347    352
FT   HELIX       353    355
FT   HELIX       356    364
FT   STRAND      369    374
SQ   SEQUENCE   375 AA;  39859 MW;  B6DF4D57080D9BC1 CRC64;
     MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT
     PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP
     QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
     YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE
     CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ
     NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV LPFEKINEGF
     DLLHSGKSIR TILMF
//