ADH1B_PANTR
ID ADH1B_PANTR Reviewed; 375 AA.
AC Q5R1W2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=All-trans-retinol dehydrogenase [NAD(+)] ADH1B {ECO:0000250|UniProtKB:P00325};
DE EC=1.1.1.105 {ECO:0000250|UniProtKB:P00325};
DE AltName: Full=Alcohol dehydrogenase 1B {ECO:0000250|UniProtKB:P00325};
DE AltName: Full=Alcohol dehydrogenase subunit beta;
GN Name=ADH1B {ECO:0000250|UniProtKB:P00325};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RA Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y., Osada N.,
RA Hashimoto K.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of all-trans-retinol
CC and its derivatives such as all-trans-4-hydroxyretinol and may
CC participate in retinoid metabolism. In vitro can also catalyzes the
CC NADH-dependent reduction of all-trans-retinal and its derivatives such
CC as all-trans-4-oxoretinal. Catalyzes in the oxidative direction with
CC higher efficiency. Has the same affinity for all-trans-4-hydroxyretinol
CC and all-trans-4-oxoretinal. {ECO:0000250|UniProtKB:P00325}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:P00325};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285;
CC Evidence={ECO:0000250|UniProtKB:P00325};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-4-hydroxyretinol + NAD(+) = all-trans-4-
CC hydroxyretinal + H(+) + NADH; Xref=Rhea:RHEA:55936,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:132259, ChEBI:CHEBI:139346;
CC Evidence={ECO:0000250|UniProtKB:P00325};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55937;
CC Evidence={ECO:0000250|UniProtKB:P00325};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-4-oxoretinol + NAD(+) = all-trans-4-oxoretinal +
CC H(+) + NADH; Xref=Rhea:RHEA:60632, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:44597, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:139347; Evidence={ECO:0000250|UniProtKB:P00325};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer or heterodimer of closely related subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AB188285; BAD74036.1; -; mRNA.
DR RefSeq; NP_001029330.1; NM_001034158.1.
DR AlphaFoldDB; Q5R1W2; -.
DR SMR; Q5R1W2; -.
DR STRING; 9598.ENSPTRP00000028001; -.
DR PaxDb; Q5R1W2; -.
DR Ensembl; ENSPTRT00000030335; ENSPTRP00000028001; ENSPTRG00000039360.
DR Ensembl; ENSPTRT00000086655; ENSPTRP00000071388; ENSPTRG00000039360.
DR GeneID; 461396; -.
DR KEGG; ptr:461396; -.
DR CTD; 125; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000155234; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; Q5R1W2; -.
DR OrthoDB; 664798at2759; -.
DR TreeFam; TF300429; -.
DR Proteomes; UP000002277; Chromosome 4.
DR Bgee; ENSPTRG00000039360; Expressed in liver and 20 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006069; P:ethanol oxidation; IBA:GO_Central.
DR GO; GO:0042573; P:retinoic acid metabolic process; IBA:GO_Central.
DR GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Lipid metabolism; Metal-binding; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00325"
FT CHAIN 2..375
FT /note="All-trans-retinol dehydrogenase [NAD(+)] ADH1B"
FT /id="PRO_0000160662"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00325"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00325"
FT MOD_RES 35
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00325"
SQ SEQUENCE 375 AA; 39826 MW; 5CE9BC266A776F25 CRC64;
MSTAGKVIKC KAAVLWEVKK PFSIEDVEVA PPKAYEVRIK MVAVGICRTD DHVVSGNLVT
PLPAILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRVCKNPESN YCLKNDLGNP
RGTLQDGTRR FTCRGKPIHH FLGTSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
YGSAVNVAKV TPGSTCAVFG LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPASQ
NLSINPMLLL TGRTWKGAVY GGFKSKEGIP KLVADFMAKK FSLDALITHV LPFEKINEGF
DLLHSGKSIR TVLTF
