ADH4_STRCA
ID ADH4_STRCA Reviewed; 379 AA.
AC P80468;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=All-trans-retinol dehydrogenase [NAD(+)] ADH4 {ECO:0000250|UniProtKB:P08319};
DE EC=1.1.1.105 {ECO:0000250|UniProtKB:P08319};
DE AltName: Full=Alcohol dehydrogenase 4;
DE AltName: Full=Alcohol dehydrogenase class II;
GN Name=ADH4 {ECO:0000250|UniProtKB:P08319};
OS Struthio camelus (Common ostrich).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=8801;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7479907; DOI=10.1073/pnas.92.24.10904;
RA Hjelmqvist L., Estonius M., Joernvall H.;
RT "The vertebrate alcohol dehydrogenase system: variable class II type form
RT elucidates separate stages of enzymogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10904-10908(1995).
RN [2]
RP PROTEIN SEQUENCE OF 1-13, AND ACETYLATION AT THR-1.
RX PubMed=8706859; DOI=10.1016/0014-5793(96)00657-6;
RA Bergman T., Gheorghe M.T., Hjelmqvist L., Joernvall H.;
RT "Alcoholytic deblocking of N-terminally acetylated peptides and proteins
RT for sequence analysis.";
RL FEBS Lett. 390:199-202(1996).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT THR-1.
RX PubMed=7607314; DOI=10.1016/0014-5793(95)00572-q;
RA Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J.,
RA Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Joernvall H.;
RT "Multiplicity of N-terminal structures of medium-chain alcohol
RT dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and
RT higher vertebrate class I, II, and III forms of the enzyme.";
RL FEBS Lett. 367:237-240(1995).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of either all-trans-
CC retinol or 9-cis-retinol (By similarity). Also oxidizes long chain
CC omega-hydroxy fatty acids, such as 20-HETE, producing both the
CC intermediate aldehyde, 20-oxoarachidonate and the end product, a
CC dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (By
CC similarity). Also catalyzes the reduction of benzoquinones (By
CC similarity). {ECO:0000250|UniProtKB:P08319,
CC ECO:0000250|UniProtKB:Q9QYY9}.
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:P08319};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285;
CC Evidence={ECO:0000250|UniProtKB:P08319};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinol + NAD(+) = 9-cis-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:42052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC Evidence={ECO:0000250|UniProtKB:P08319};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42053;
CC Evidence={ECO:0000250|UniProtKB:P08319};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O + NAD(+) =
CC (5Z,8Z,11Z,14Z)-eicosatetraenedioate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:39803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76645,
CC ChEBI:CHEBI:76647; Evidence={ECO:0000250|UniProtKB:Q9QYY9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39804;
CC Evidence={ECO:0000250|UniProtKB:Q9QYY9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + NAD(+) = 20-
CC oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + NADH;
CC Xref=Rhea:RHEA:39799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:76624, ChEBI:CHEBI:76645;
CC Evidence={ECO:0000250|UniProtKB:Q9QYY9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39800;
CC Evidence={ECO:0000250|UniProtKB:Q9QYY9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,4-benzoquinone + H(+) + NADH = hydroquinone + NAD(+);
CC Xref=Rhea:RHEA:60660, ChEBI:CHEBI:15378, ChEBI:CHEBI:16509,
CC ChEBI:CHEBI:17594, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P08319};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60661;
CC Evidence={ECO:0000250|UniProtKB:P08319};
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 -!- ACTIVITY REGULATION: Oxidation of 20-HETE is inhibited by low
CC concentrations of N-heptylformamide. Oxidation of 20-HETE is a
CC decreased by 55-65% by either all-trans-retinol or all-trans-retinoic
CC acid. Strongly inhibited by omega-hydroxy fatty acids.
CC {ECO:0000250|UniProtKB:Q9QYY9}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-II subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P80468; -.
DR SMR; P80468; -.
DR iPTMnet; P80468; -.
DR SABIO-RK; P80468; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IEA:InterPro.
DR GO; GO:0035276; F:ethanol binding; IEA:InterPro.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR GO; GO:0010430; P:fatty acid omega-oxidation; ISS:UniProtKB.
DR GO; GO:0042572; P:retinol 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 InterPro; IPR028632; Zinc_ADH_II.
DR PANTHER; PTHR43880:SF14; PTHR43880:SF14; 1.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Lipid metabolism;
KW Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..379
FT /note="All-trans-retinol dehydrogenase [NAD(+)] ADH4"
FT /id="PRO_0000160686"
FT BINDING 46
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 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 204..209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 297..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:7607314,
FT ECO:0000269|PubMed:8706859"
SQ SEQUENCE 379 AA; 40310 MW; 9BD05DFC286561BF CRC64;
TTEGKVIKCK AAIAWEAGKP LSVEEIEVSP PKDHEVRVKI VATGVCRTDE HAINPSFKEG
VFPVILGHEG AGIVESIGQG VSKFKPGDKV IPLYMPQCGH CKFCLNPKTN LCEKISKIKT
PISDQEVMSD GTSRFTCKGK PIYHFMGTST FSEYTVVSES SLAKIDAAAP LDKVCLIGCG
FSTGYGAAIN TAQVEPGSTC AVFGLGGVGL SAVMGCKAAG ASKIFGIDIN KDKFPLAKKL
GATDCLNPQD IRKPVQEIIA EMTNGGVDFA IECIGNPDVM KAAFESTTVG WGTCVIVGVA
VGEQSIPFSP MQLIMGRKIK ATFFGGWKSV KSVPKLVSDY MAKKFDLDAL VSHTLPLDKI
NDAFDLMNAG KSNRTILVF
