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ADH7_RAT
ID   ADH7_RAT                Reviewed;         374 AA.
AC   P41682; O55146;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=All-trans-retinol dehydrogenase [NAD(+)] ADH7 {ECO:0000305};
DE            EC=1.1.1.105 {ECO:0000250|UniProtKB:P40394};
DE   AltName: Full=Alcohol dehydrogenase class 4 mu/sigma chain;
DE            EC=1.1.1.1 {ECO:0000250|UniProtKB:P40394};
DE   AltName: Full=Alcohol dehydrogenase class IV mu/sigma chain;
DE   AltName: Full=Omega-hydroxydecanoate dehydrogenase ADH7 {ECO:0000250|UniProtKB:P40394};
DE            EC=1.1.1.66 {ECO:0000250|UniProtKB:P40394};
GN   Name=Adh7;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC   STRAIN=Sprague-Dawley; TISSUE=Stomach;
RX   PubMed=8127901; DOI=10.1073/pnas.91.5.1893;
RA   Pares X., Cederlund E., Moreno A., Hjelmqvist L., Farres J., Joernvall H.;
RT   "Mammalian class IV alcohol dehydrogenase (stomach alcohol dehydrogenase):
RT   structure, origin, and correlation with enzymology.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:1893-1897(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Lung;
RX   PubMed=10829036; DOI=10.1074/jbc.m910040199;
RA   Crosas B., Allali-Hassani A., Martinez S.E., Martras S., Persson B.,
RA   Jornvall H., Pares X., Farres J.;
RT   "Molecular basis for differential substrate specificity in class IV alcohol
RT   dehydrogenases: a conserved function in retinoid metabolism but not in
RT   ethanol oxidation.";
RL   J. Biol. Chem. 275:25180-25187(2000).
RN   [3]
RP   ACTIVITY REGULATION.
RX   PubMed=9600267; DOI=10.1016/s0014-5793(98)00374-3;
RA   Allali-Hassani A., Peralba J.M., Martras S., Farres J., Pares X.;
RT   "Retinoids, omega-hydroxyfatty acids and cytotoxic aldehydes as
RT   physiological substrates, and H2-receptor antagonists as pharmacological
RT   inhibitors, of human class IV alcohol dehydrogenase.";
RL   FEBS Lett. 426:362-366(1998).
CC   -!- FUNCTION: Catalyzes the NAD-dependent oxidation of all-trans-retinol,
CC       alcohol, aldehyde and omega-hydroxy fatty acids and their derivatives.
CC       Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol,
CC       9-cis-retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such
CC       as juniperic acid. In vitro can also catalyzes the NADH-dependent
CC       reduction of all-trans-retinal and aldehydes and their derivatives.
CC       Reduces preferentially all trans-retinal, all-trans-4-oxoretinal and
CC       hexanal. Catalyzes in the oxidative direction with higher efficiency.
CC       Therefore may participate in retinoid metabolism, fatty acid omega-
CC       oxidation, and elimination of cytotoxic aldehydes produced by lipid
CC       peroxidation. {ECO:0000250|UniProtKB:P40394}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10737;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10738;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=10-hydroxydecanoate + NAD(+) = 10-oxodecanoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:20880, ChEBI:CHEBI:11305, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58022; EC=1.1.1.66;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20881;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
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:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
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:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42053;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-3,4-didehydroretinol + NAD(+) = all-trans-3,4-
CC         didehydroretinal + H(+) + NADH; Xref=Rhea:RHEA:55940,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28537, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:132246;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55941;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
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:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55937;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
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:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60634;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12-hydroxydodecanoate + NAD(+) = 12-oxododecanoate + H(+) +
CC         NADH; Xref=Rhea:RHEA:60980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36204,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144067;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60981;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16-hydroxyhexadecanoate + NAD(+) = 16-oxohexadecanoate + H(+)
CC         + NADH; Xref=Rhea:RHEA:60984, ChEBI:CHEBI:15378, ChEBI:CHEBI:55329,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144068;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60985;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexan-1-ol + NAD(+) = H(+) + hexanal + NADH;
CC         Xref=Rhea:RHEA:60972, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:87393, ChEBI:CHEBI:88528;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60973;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60974;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-hex-2-en-1-ol + NAD(+) = (E)-hex-2-enal + H(+) + NADH;
CC         Xref=Rhea:RHEA:60988, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:141205;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60989;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60990;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-hydroxynon-2-en-1-ol + NAD(+) = (E)-4-hydroxynon-2-enal
CC         + H(+) + NADH; Xref=Rhea:RHEA:60976, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58968,
CC         ChEBI:CHEBI:142617; Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60978;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
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: Retinol oxidation is inhibited by the detergent
CC       Tween 80. Ethanol inhibits both all-trans-retinol and 9-cis-retinol
CC       oxidation. 13-cis-retinol is an effective competitive inhibitor of the
CC       9-cis-retinol oxidation. All-trans-retinoic acid is a powerful
CC       inhibitor of all-trans-retinol oxidation. 13-cis-retinoic acid is a
CC       powerful inhibitor of all-trans-retinol oxidation (By similarity).
CC       Cimetidine and ranitidine inhibited ethanol oxidation (PubMed:9600267).
CC       {ECO:0000250|UniProtKB:P40394, ECO:0000269|PubMed:9600267}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in stomach.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-IV subfamily. {ECO:0000305}.
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DR   EMBL; X98746; CAA67297.1; -; mRNA.
DR   PIR; A53142; A53142.
DR   RefSeq; NP_599156.1; NM_134329.1.
DR   AlphaFoldDB; P41682; -.
DR   SMR; P41682; -.
DR   STRING; 10116.ENSRNOP00000015870; -.
DR   iPTMnet; P41682; -.
DR   PhosphoSitePlus; P41682; -.
DR   jPOST; P41682; -.
DR   PaxDb; P41682; -.
DR   PRIDE; P41682; -.
DR   GeneID; 171178; -.
DR   KEGG; rno:171178; -.
DR   CTD; 131; -.
DR   RGD; 621638; Adh7.
DR   eggNOG; KOG0022; Eukaryota.
DR   InParanoid; P41682; -.
DR   OrthoDB; 664798at2759; -.
DR   PhylomeDB; P41682; -.
DR   Reactome; R-RNO-71384; Ethanol oxidation.
DR   PRO; PR:P41682; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:RGD.
DR   GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; ISO:RGD.
DR   GO; GO:0004031; F:aldehyde oxidase activity; ISO:RGD.
DR   GO; GO:0035276; F:ethanol binding; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0051287; F:NAD binding; IDA:RGD.
DR   GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0050153; F:omega-hydroxydecanoate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048019; F:receptor antagonist activity; ISO:RGD.
DR   GO; GO:0019841; F:retinol binding; IDA:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR   GO; GO:0006068; P:ethanol catabolic process; ISO:RGD.
DR   GO; GO:0006067; P:ethanol metabolic process; IDA:RGD.
DR   GO; GO:0006069; P:ethanol oxidation; ISO:RGD.
DR   GO; GO:0010430; P:fatty acid omega-oxidation; ISO:RGD.
DR   GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR   GO; GO:0045471; P:response to ethanol; ISO:RGD.
DR   GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD.
DR   GO; GO:0001523; P:retinoid metabolic process; ISO:RGD.
DR   GO; GO:0042572; P:retinol metabolic process; IDA:RGD.
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; IPR028635; Zinc_ADH_IV.
DR   PANTHER; PTHR43880:SF2; PTHR43880:SF2; 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; Reference proteome; Zinc.
FT   CHAIN           1..374
FT                   /note="All-trans-retinol dehydrogenase [NAD(+)] ADH7"
FT                   /id="PRO_0000160696"
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         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
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         292..294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000305|PubMed:8127901"
FT   CONFLICT        1..4
FT                   /note="MDTA -> SNRV (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="G -> E (in Ref. 2; CAA67297)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="V -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  40105 MW;  DD745E7FCB01E452 CRC64;
     MDTAGKVIKC KAAVLWGTNQ PFSIEDIEVA PPKAKEVRVK ILATGICGTD DHVIKGTMVS
     KFPVIVGHEA VGIVESVGEE VTTVRPGDKV IPLFLPQCRE CNPCRNPEGN LCIRSDLTGR
     GVLADGTTRF TCKGKPVQHF MNTSTFTEYT VLDESSVAKI DAEAPPEKAC LIGCGFSTGY
     GAAVKTAKVS PGSTCAVFGL GGVGLSVVMG CKAAGASRII GIDINKDKFQ KALDVGATEC
     INPRDFTKPI SEVLSDMTGN TVQYTFEVIG RLETMVDALS SCHMNYGTSV VVGAPPSAKM
     LSYDPMLLFT GRTWKGCVFG GWKSRDDVPK LVTEFLEKKF DLGQLITHTL PFHNISEGFE
     LLYSGQSIRT VLTF
 
 
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