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Alcohol dehydrogenase 4 (EC 1.1.1.1) (Alcohol dehydrogenase class II pi chain)

 ADH4_HUMAN              Reviewed;         380 AA.
P08319; A8K470; B4DIE7; C9J4A9; Q8TCD7;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 5.
22-NOV-2017, entry version 185.
RecName: Full=Alcohol dehydrogenase 4;
EC=1.1.1.1;
AltName: Full=Alcohol dehydrogenase class II pi chain;
Name=ADH4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
PubMed=3036213; DOI=10.1021/bi00381a021;
Hoeoeg J.-O., von Bahr-Lindstroem H., Heden L.-O., Holmquist B.,
Larsson K., Hempel J., Vallee B.L., Joernvall H.;
"Structure of the class II enzyme of human liver alcohol
dehydrogenase: combined cDNA and protein sequence determination of the
pi subunit.";
Biochemistry 26:1926-1932(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Fetal liver;
PubMed=1889753; DOI=10.1016/0378-1119(91)90285-J;
von Bahr-Lindstroem H., Joernvall H., Hoeoeg J.-O.;
"Cloning and characterization of the human ADH4 gene.";
Gene 103:269-274(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS VAL-309 AND ILE-374.
TISSUE=Hippocampus, and Liver;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-318.
NIEHS SNPs program;
Submitted (MAR-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] (ISOFORM 1), AND VARIANTS
VAL-309 AND ILE-374.
TISSUE=Liver;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-278, AND
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).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC
IONS.
Structural genomics consortium (SGC);
"Crystal structure of human class II alcohol dehydrogenase (ADH4) in
complex with NAD and Zn.";
Submitted (APR-2008) to the PDB data bank.
-!- 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: Homodimer. {ECO:0000269|Ref.8}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P08319-1; Sequence=Displayed;
Name=2;
IsoId=P08319-2; Sequence=VSP_036788;
-!- 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. Class-II subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/adh4/";
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EMBL; M15943; AAA51595.1; -; mRNA.
EMBL; X56411; CAA39813.1; -; Genomic_DNA.
EMBL; X56412; CAA39813.1; JOINED; Genomic_DNA.
EMBL; X56413; CAA39813.1; JOINED; Genomic_DNA.
EMBL; X56414; CAA39813.1; JOINED; Genomic_DNA.
EMBL; X56415; CAA39813.1; JOINED; Genomic_DNA.
EMBL; X56416; CAA39813.1; JOINED; Genomic_DNA.
EMBL; X56417; CAA39813.1; JOINED; Genomic_DNA.
EMBL; X56418; CAA39813.1; JOINED; Genomic_DNA.
EMBL; X56419; CAA39813.1; JOINED; Genomic_DNA.
EMBL; AK290835; BAF83524.1; -; mRNA.
EMBL; AK295556; BAG58459.1; -; mRNA.
EMBL; AY974245; AAX59034.1; -; Genomic_DNA.
EMBL; AC019131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC022319; AAH22319.1; -; mRNA.
CCDS; CCDS34032.1; -. [P08319-1]
CCDS; CCDS77942.1; -. [P08319-2]
PIR; A27109; DEHUAP.
RefSeq; NP_000661.2; NM_000670.4. [P08319-1]
RefSeq; NP_001293100.1; NM_001306171.1. [P08319-2]
RefSeq; NP_001293101.1; NM_001306172.1. [P08319-2]
UniGene; Hs.1219; -.
PDB; 3COS; X-ray; 2.10 A; A/B/C/D=1-380.
PDBsum; 3COS; -.
ProteinModelPortal; P08319; -.
SMR; P08319; -.
BioGrid; 106639; 3.
IntAct; P08319; 1.
STRING; 9606.ENSP00000265512; -.
BindingDB; P08319; -.
ChEMBL; CHEMBL2990; -.
DrugBank; DB03559; Cyclohexylformamide.
DrugBank; DB00898; Ethanol.
DrugBank; DB00157; NADH.
SwissLipids; SLP:000000499; -.
iPTMnet; P08319; -.
PhosphoSitePlus; P08319; -.
BioMuta; ADH4; -.
DMDM; 308153684; -.
EPD; P08319; -.
MaxQB; P08319; -.
PaxDb; P08319; -.
PeptideAtlas; P08319; -.
PRIDE; P08319; -.
DNASU; 127; -.
Ensembl; ENST00000265512; ENSP00000265512; ENSG00000198099. [P08319-1]
Ensembl; ENST00000505590; ENSP00000425416; ENSG00000198099. [P08319-2]
Ensembl; ENST00000508393; ENSP00000424630; ENSG00000198099. [P08319-2]
GeneID; 127; -.
KEGG; hsa:127; -.
UCSC; uc003hun.4; human. [P08319-1]
CTD; 127; -.
DisGeNET; 127; -.
EuPathDB; HostDB:ENSG00000198099.8; -.
GeneCards; ADH4; -.
H-InvDB; HIX0200651; -.
HGNC; HGNC:252; ADH4.
HPA; HPA020525; -.
MIM; 103740; gene.
neXtProt; NX_P08319; -.
OpenTargets; ENSG00000198099; -.
PharmGKB; PA24573; -.
eggNOG; KOG0022; Eukaryota.
eggNOG; COG1062; LUCA.
GeneTree; ENSGT00430000030800; -.
HOGENOM; HOG000294674; -.
HOVERGEN; HBG000195; -.
InParanoid; P08319; -.
KO; K13980; -.
OMA; MKAALDC; -.
OrthoDB; EOG091G08N3; -.
PhylomeDB; P08319; -.
TreeFam; TF300429; -.
BioCyc; MetaCyc:HS06569-MONOMER; -.
BRENDA; 1.1.1.1; 2681.
Reactome; R-HSA-5365859; RA biosynthesis pathway.
Reactome; R-HSA-71384; Ethanol oxidation.
SABIO-RK; P08319; -.
EvolutionaryTrace; P08319; -.
GeneWiki; ADH4; -.
GenomeRNAi; 127; -.
PRO; PR:P08319; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000198099; -.
CleanEx; HS_ADH4; -.
ExpressionAtlas; P08319; baseline and differential.
Genevisible; P08319; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:UniProtKB.
GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IDA:UniProtKB.
GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:Ensembl.
GO; GO:0005503; F:all-trans retinal binding; IDA:UniProtKB.
GO; GO:0019115; F:benzaldehyde dehydrogenase activity; IDA:UniProtKB.
GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
GO; GO:0003960; F:NADPH:quinone reductase activity; ISS:UniProtKB.
GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
GO; GO:0019841; F:retinol binding; IDA:UniProtKB.
GO; GO:0004745; F:retinol dehydrogenase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0046164; P:alcohol catabolic process; ISS:UniProtKB.
GO; GO:0006066; P:alcohol metabolic process; IDA:UniProtKB.
GO; GO:0006081; P:cellular aldehyde metabolic process; IDA:UniProtKB.
GO; GO:0006069; P:ethanol oxidation; IDA:UniProtKB.
GO; GO:1901661; P:quinone metabolic process; ISS:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB.
GO; GO:0042572; P:retinol metabolic process; 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.
InterPro; IPR028632; Zinc_ADH_II.
PANTHER; PTHR43880:SF14; PTHR43880:SF14; 1.
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; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Metal-binding; NAD; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome; Zinc.
CHAIN 1 380 Alcohol dehydrogenase 4.
/FTId=PRO_0000160681.
NP_BIND 48 49 NAD. {ECO:0000269|Ref.8}.
NP_BIND 205 210 NAD. {ECO:0000269|Ref.8}.
NP_BIND 298 300 NAD. {ECO:0000269|Ref.8}.
NP_BIND 323 325 NAD. {ECO:0000269|Ref.8}.
METAL 47 47 Zinc 1; catalytic.
METAL 69 69 Zinc 1; catalytic.
METAL 99 99 Zinc 2.
METAL 102 102 Zinc 2.
METAL 105 105 Zinc 2.
METAL 113 113 Zinc 2.
METAL 180 180 Zinc 1; catalytic.
BINDING 229 229 NAD. {ECO:0000269|Ref.8}.
BINDING 234 234 NAD. {ECO:0000269|Ref.8}.
BINDING 375 375 NAD. {ECO:0000269|Ref.8}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 6 MGTKGK -> MLVRGPHFELQRCKTHLFSSNYLTQ (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036788.
VARIANT 309 309 I -> V (in dbSNP:rs1126671).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_023461.
VARIANT 318 318 R -> H (in dbSNP:rs29001219).
{ECO:0000269|Ref.4}.
/FTId=VAR_023462.
VARIANT 374 374 V -> I (in dbSNP:rs1126673).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_023463.
CONFLICT 52 52 T -> S (in Ref. 1; AAA51595 and 2;
CAA39813). {ECO:0000305}.
CONFLICT 380 380 F -> FGRCQEQFRILSD (in Ref. 1; AAA51595).
{ECO:0000305}.
STRAND 8 15 {ECO:0000244|PDB:3COS}.
STRAND 23 29 {ECO:0000244|PDB:3COS}.
STRAND 36 45 {ECO:0000244|PDB:3COS}.
HELIX 48 52 {ECO:0000244|PDB:3COS}.
STRAND 63 65 {ECO:0000244|PDB:3COS}.
STRAND 70 78 {ECO:0000244|PDB:3COS}.
STRAND 90 93 {ECO:0000244|PDB:3COS}.
STRAND 100 102 {ECO:0000244|PDB:3COS}.
TURN 103 106 {ECO:0000244|PDB:3COS}.
HELIX 122 124 {ECO:0000244|PDB:3COS}.
STRAND 135 138 {ECO:0000244|PDB:3COS}.
STRAND 141 144 {ECO:0000244|PDB:3COS}.
TURN 147 149 {ECO:0000244|PDB:3COS}.
STRAND 152 159 {ECO:0000244|PDB:3COS}.
STRAND 162 165 {ECO:0000244|PDB:3COS}.
HELIX 172 175 {ECO:0000244|PDB:3COS}.
HELIX 176 179 {ECO:0000244|PDB:3COS}.
HELIX 181 190 {ECO:0000244|PDB:3COS}.
TURN 191 193 {ECO:0000244|PDB:3COS}.
STRAND 200 204 {ECO:0000244|PDB:3COS}.
HELIX 208 219 {ECO:0000244|PDB:3COS}.
STRAND 223 228 {ECO:0000244|PDB:3COS}.
HELIX 232 234 {ECO:0000244|PDB:3COS}.
HELIX 235 240 {ECO:0000244|PDB:3COS}.
STRAND 244 247 {ECO:0000244|PDB:3COS}.
HELIX 249 251 {ECO:0000244|PDB:3COS}.
HELIX 256 263 {ECO:0000244|PDB:3COS}.
STRAND 268 273 {ECO:0000244|PDB:3COS}.
HELIX 278 286 {ECO:0000244|PDB:3COS}.
TURN 290 292 {ECO:0000244|PDB:3COS}.
STRAND 293 297 {ECO:0000244|PDB:3COS}.
STRAND 307 309 {ECO:0000244|PDB:3COS}.
HELIX 311 315 {ECO:0000244|PDB:3COS}.
STRAND 318 322 {ECO:0000244|PDB:3COS}.
HELIX 325 327 {ECO:0000244|PDB:3COS}.
HELIX 330 342 {ECO:0000244|PDB:3COS}.
HELIX 349 351 {ECO:0000244|PDB:3COS}.
STRAND 352 357 {ECO:0000244|PDB:3COS}.
HELIX 358 360 {ECO:0000244|PDB:3COS}.
HELIX 361 369 {ECO:0000244|PDB:3COS}.
STRAND 374 379 {ECO:0000244|PDB:3COS}.
SEQUENCE 380 AA; 40222 MW; 45721A08197629F1 CRC64;
MGTKGKVIKC KAAIAWEAGK PLCIEEVEVA PPKAHEVRIQ IIATSLCHTD ATVIDSKFEG
LAFPVIVGHE AAGIVESIGP GVTNVKPGDK VIPLYAPLCR KCKFCLSPLT NLCGKISNLK
SPASDQQLME DKTSRFTCKG KPVYHFFGTS TFSQYTVVSD INLAKIDDDA NLERVCLLGC
GFSTGYGAAI NNAKVTPGST CAVFGLGGVG LSAVMGCKAA GASRIIGIDI NSEKFVKAKA
LGATDCLNPR DLHKPIQEVI IELTKGGVDF ALDCAGGSET MKAALDCTTA GWGSCTFIGV
AAGSKGLTIF PEELIIGRTI NGTFFGGWKS VDSIPKLVTD YKNKKFNLDA LVTHTLPFDK
ISEAFDLMNQ GKSVRTILIF


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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