ADH1B_PAPHA
ID ADH1B_PAPHA Reviewed; 375 AA.
AC P14139;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
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 Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2748595; DOI=10.1073/pnas.86.14.5454;
RA Trezise A.E.O., Godfrey E.A., Holmes R.S., Beacham I.R.;
RT "Cloning and sequencing of cDNA encoding baboon liver alcohol
RT dehydrogenase: evidence for a common ancestral lineage with the human
RT alcohol dehydrogenase beta subunit and for class I ADH gene duplications
RT predating primate radiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5454-5458(1989).
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;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- SUBUNIT: Homodimer or heterodimer of closely related subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in liver.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M25035; AAA35378.1; -; mRNA.
DR AlphaFoldDB; P14139; -.
DR SMR; P14139; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
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; 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_0000160663"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
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; 39846 MW; 4A617082B29F7C9B CRC64;
MSTAGKVIKC KAAVLWEVKK PFSIEDVEVA PPKAYEVRIK MVAVGICRTD DHVVSGNLVS
PLPAILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRVCKSPEGN YCVKNDLSNP
RGTLQDGTRR FTCRGKPIHH FVGTSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
YGSAVNVAKV TPGSVCAVFG LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ
NLSINPMLLL TGRTWKGAVY GGFKSREGIP KLVADFMAKK FSLDALITHV LPFEKINEGF
DLLRSGKSIR TVLTF
