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Alcohol dehydrogenase 1C (EC 1.1.1.1) (Alcohol dehydrogenase subunit gamma)

 ADH1G_HUMAN             Reviewed;         375 AA.
P00326; Q4PJ18; Q5WRV0; Q6LBW4; Q6NWV0; Q6NZA7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 184.
RecName: Full=Alcohol dehydrogenase 1C;
EC=1.1.1.1;
AltName: Full=Alcohol dehydrogenase subunit gamma;
Name=ADH1C; Synonyms=ADH3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GAMMA-2 GLN-272 AND VAL-350, AND
POLYMORPHISM.
TISSUE=Liver;
PubMed=3758060; DOI=10.1111/j.1432-1033.1986.tb09855.x;
Hoeoeg J.-O., Heden L.-O., Larsson K., Joernvall H.;
"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.";
Eur. J. Biochem. 159:215-218(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2935875; DOI=10.1073/pnas.83.3.634;
Ikuta T., Szeto S., Yoshida A.;
"Three human alcohol dehydrogenase subunits: cDNA structure and
molecular and evolutionary divergence.";
Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1524834; DOI=10.1266/jjg.67.167;
Yokoyama S., Matsuo Y., Rajasekharan S., Yokoyama R.;
"Molecular structure of the human alcohol dehydrogenase 3 gene.";
Jpn. J. Genet. 67:167-171(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-48; SER-166;
GLN-272; VAL-350 AND THR-352.
NIEHS SNPs program;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GAMMA-2 GLN-272
AND VAL-350.
TISSUE=Brain, and Femoral artery;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, AND
ACETYLATION AT SER-2.
TISSUE=Liver;
PubMed=6391921; DOI=10.1111/j.1432-1033.1984.tb08575.x;
Buhler R., Hempel J., Kaiser R., de Zalenski C., von Wartburg J.-P.,
Joernvall H.;
"Human liver alcohol dehydrogenase. 2. The primary structure of the
gamma 1 protein chain.";
Eur. J. Biochem. 145:447-453(1984).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC
IONS.
PubMed=11274460; DOI=10.1110/ps.45001;
Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.;
"Three-dimensional structures of the three human class I alcohol
dehydrogenases.";
Protein Sci. 10:697-706(2001).
[10]
X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC
IONS.
PubMed=15449945; DOI=10.1021/bi0489107;
Gibbons B.J., Hurley T.D.;
"Structure of three class I human alcohol dehydrogenases complexed
with isoenzyme specific formamide inhibitors.";
Biochemistry 43:12555-12562(2004).
-!- CATALYTIC ACTIVITY: A primary alcohol + NAD(+) = an aldehyde +
NADH.
-!- CATALYTIC ACTIVITY: A secondary alcohol + NAD(+) = a ketone +
NADH.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- SUBUNIT: Dimer of identical or non-identical chains of three
types; alpha, beta and gamma. {ECO:0000269|PubMed:11274460,
ECO:0000269|PubMed:15449945}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- POLYMORPHISM: 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. {ECO:0000269|PubMed:3758060}.
-!- 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.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/adh1c/";
-----------------------------------------------------------------------
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EMBL; X04299; CAA27842.1; -; mRNA.
EMBL; X04350; CAA27876.1; -; mRNA.
EMBL; M12272; AAC41757.1; -; mRNA.
EMBL; D11067; BAC06856.1; -; Genomic_DNA.
EMBL; DQ088981; AAY68222.1; -; Genomic_DNA.
EMBL; AC097530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC062476; AAH62476.1; -; mRNA.
EMBL; BC066227; AAH66227.1; -; mRNA.
EMBL; BC066228; AAH66228.1; -; mRNA.
EMBL; BC067419; AAH67419.1; -; mRNA.
EMBL; BC067420; AAH67420.1; -; mRNA.
EMBL; BC067421; AAH67421.1; -; mRNA.
EMBL; BC067422; AAH67422.1; -; mRNA.
EMBL; BC074771; AAH74771.1; -; mRNA.
EMBL; BC074786; AAH74786.1; -; mRNA.
CCDS; CCDS54780.1; -.
PIR; C25428; DEHUAG.
RefSeq; NP_000660.1; NM_000669.4.
UniGene; Hs.654537; -.
PDB; 1DDA; Model; -; A/B=1-375.
PDB; 1HT0; X-ray; 2.00 A; A/B=2-375.
PDB; 1U3W; X-ray; 1.45 A; A/B=2-375.
PDBsum; 1DDA; -.
PDBsum; 1HT0; -.
PDBsum; 1U3W; -.
ProteinModelPortal; P00326; -.
SMR; P00326; -.
BioGrid; 106638; 2.
BindingDB; P00326; -.
ChEMBL; CHEMBL3285; -.
DrugBank; DB03061; (R)-N-(1-Methyl-Hexyl)-Formamide.
DrugBank; DB02249; 2-Ethoxyethanol.
DrugBank; DB02871; 3-Butylthiolane 1-Oxide.
DrugBank; DB02721; 4-Iodopyrazole.
DrugBank; DB03020; 5-Beta-D-Ribofuranosylnicotinamide Adenine Dinucleotide.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB04071; Cpad.
DrugBank; DB03559; Cyclohexylformamide.
DrugBank; DB00898; Ethanol.
DrugBank; DB01213; Fomepizole.
DrugBank; DB02131; N-1-Methylheptylformamide.
DrugBank; DB04113; N-Formylpiperidine.
DrugBank; DB00157; NADH.
DrugBank; DB02822; Para-Bromobenzyl Alcohol.
DrugBank; DB02757; Pyrazole.
DrugBank; DB03226; Trifluoroethanol.
iPTMnet; P00326; -.
PhosphoSitePlus; P00326; -.
BioMuta; ADH1C; -.
DMDM; 113398; -.
MaxQB; P00326; -.
PeptideAtlas; P00326; -.
PRIDE; P00326; -.
ProteomicsDB; 51229; -.
TopDownProteomics; P00326; -.
Ensembl; ENST00000515683; ENSP00000426083; ENSG00000248144.
GeneID; 126; -.
KEGG; hsa:126; -.
UCSC; uc032trd.2; human.
CTD; 126; -.
DisGeNET; 126; -.
EuPathDB; HostDB:ENSG00000248144.5; -.
GeneCards; ADH1C; -.
HGNC; HGNC:251; ADH1C.
HPA; HPA047814; -.
HPA; HPA060902; -.
MalaCards; ADH1C; -.
MIM; 103730; gene.
neXtProt; NX_P00326; -.
OpenTargets; ENSG00000248144; -.
PharmGKB; PA24572; -.
GeneTree; ENSGT00430000030800; -.
HOVERGEN; HBG000195; -.
InParanoid; P00326; -.
KO; K13951; -.
OMA; CNVCKHP; -.
OrthoDB; EOG091G08N3; -.
BRENDA; 1.1.1.1; 2681.
Reactome; R-HSA-5365859; RA biosynthesis pathway.
Reactome; R-HSA-71384; Ethanol oxidation.
SABIO-RK; P00326; -.
ChiTaRS; ADH1C; human.
EvolutionaryTrace; P00326; -.
GeneWiki; ADH1C; -.
GenomeRNAi; 126; -.
PRO; PR:P00326; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000248144; Expressed in 89 organ(s), highest expression level in liver.
CleanEx; HS_ADH1C; -.
ExpressionAtlas; P00326; baseline and differential.
Genevisible; P00326; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:UniProtKB.
GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; EXP:Reactome.
GO; GO:0004745; F:retinol dehydrogenase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006069; P:ethanol oxidation; IDA:UniProtKB.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR002328; ADH_Zn_CS.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020843; PKS_ER.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SMART; SM00829; PKS_ER; 1.
SUPFAM; SSF50129; SSF50129; 2.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00059; ADH_ZINC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Metal-binding; NAD; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6391921}.
CHAIN 2 375 Alcohol dehydrogenase 1C.
/FTId=PRO_0000160664.
NP_BIND 200 205 NAD. {ECO:0000269|PubMed:11274460,
ECO:0000269|PubMed:15449945}.
NP_BIND 293 295 NAD. {ECO:0000269|PubMed:11274460,
ECO:0000269|PubMed:15449945}.
METAL 47 47 Zinc 1; catalytic.
METAL 68 68 Zinc 1; catalytic.
METAL 98 98 Zinc 2.
METAL 101 101 Zinc 2.
METAL 104 104 Zinc 2.
METAL 112 112 Zinc 2.
METAL 175 175 Zinc 1; catalytic.
BINDING 224 224 NAD. {ECO:0000269|PubMed:11274460,
ECO:0000269|PubMed:15449945}.
BINDING 229 229 NAD. {ECO:0000269|PubMed:11274460,
ECO:0000269|PubMed:15449945}.
BINDING 370 370 NAD. {ECO:0000269|PubMed:11274460,
ECO:0000269|PubMed:15449945}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:6391921}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000250|UniProtKB:P00325}.
VARIANT 48 48 R -> H (in dbSNP:rs35385902).
{ECO:0000269|Ref.4}.
/FTId=VAR_023992.
VARIANT 166 166 P -> S (in dbSNP:rs34195308).
{ECO:0000269|Ref.4}.
/FTId=VAR_023993.
VARIANT 272 272 R -> Q (in allele ADH3*2/gamma-2;
dbSNP:rs1693482).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3758060,
ECO:0000269|Ref.4}.
/FTId=VAR_000428.
VARIANT 350 350 I -> V (in allele ADH3*2/gamma-2;
dbSNP:rs698).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3758060,
ECO:0000269|Ref.4}.
/FTId=VAR_000429.
VARIANT 352 352 P -> T (in dbSNP:rs35719513).
{ECO:0000269|Ref.4}.
/FTId=VAR_023994.
CONFLICT 130 130 Missing (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 171 171 C -> R (in Ref. 6; AAH67421).
{ECO:0000305}.
STRAND 8 15 {ECO:0000244|PDB:1U3W}.
STRAND 23 29 {ECO:0000244|PDB:1U3W}.
STRAND 36 45 {ECO:0000244|PDB:1U3W}.
HELIX 48 54 {ECO:0000244|PDB:1U3W}.
STRAND 62 65 {ECO:0000244|PDB:1U3W}.
STRAND 69 77 {ECO:0000244|PDB:1U3W}.
STRAND 89 92 {ECO:0000244|PDB:1U3W}.
STRAND 99 101 {ECO:0000244|PDB:1U3W}.
HELIX 102 105 {ECO:0000244|PDB:1U3W}.
STRAND 117 119 {ECO:0000244|PDB:1U3W}.
STRAND 131 133 {ECO:0000244|PDB:1U3W}.
STRAND 136 139 {ECO:0000244|PDB:1U3W}.
TURN 142 144 {ECO:0000244|PDB:1U3W}.
STRAND 147 154 {ECO:0000244|PDB:1U3W}.
HELIX 155 157 {ECO:0000244|PDB:1U3W}.
STRAND 158 160 {ECO:0000244|PDB:1U3W}.
HELIX 167 170 {ECO:0000244|PDB:1U3W}.
HELIX 171 174 {ECO:0000244|PDB:1U3W}.
HELIX 176 185 {ECO:0000244|PDB:1U3W}.
TURN 186 188 {ECO:0000244|PDB:1U3W}.
STRAND 195 199 {ECO:0000244|PDB:1U3W}.
HELIX 203 214 {ECO:0000244|PDB:1U3W}.
STRAND 218 223 {ECO:0000244|PDB:1U3W}.
HELIX 227 229 {ECO:0000244|PDB:1U3W}.
HELIX 230 235 {ECO:0000244|PDB:1U3W}.
STRAND 239 242 {ECO:0000244|PDB:1U3W}.
HELIX 244 246 {ECO:0000244|PDB:1U3W}.
HELIX 251 258 {ECO:0000244|PDB:1U3W}.
TURN 259 261 {ECO:0000244|PDB:1U3W}.
STRAND 262 268 {ECO:0000244|PDB:1U3W}.
HELIX 273 282 {ECO:0000244|PDB:1U3W}.
TURN 285 287 {ECO:0000244|PDB:1U3W}.
STRAND 289 292 {ECO:0000244|PDB:1U3W}.
STRAND 302 304 {ECO:0000244|PDB:1U3W}.
HELIX 307 310 {ECO:0000244|PDB:1U3W}.
STRAND 314 317 {ECO:0000244|PDB:1U3W}.
HELIX 320 322 {ECO:0000244|PDB:1U3W}.
HELIX 325 337 {ECO:0000244|PDB:1U3W}.
HELIX 344 346 {ECO:0000244|PDB:1U3W}.
STRAND 347 352 {ECO:0000244|PDB:1U3W}.
HELIX 353 355 {ECO:0000244|PDB:1U3W}.
HELIX 356 364 {ECO:0000244|PDB:1U3W}.
STRAND 369 374 {ECO:0000244|PDB:1U3W}.
SEQUENCE 375 AA; 39868 MW; 414D73CC4C104C84 CRC64;
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT
PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP
RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ
NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF
DLLRSGKSIR TVLTF


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