ID M3YE03_MUSPF Unreviewed; 380 AA.
AC M3YE03;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Alcohol dehydrogenase 4 (class II), pi polypeptide {ECO:0000313|Ensembl:ENSMPUP00000009560.1};
DE SubName: Full=All-trans-retinol dehydrogenase [NAD(+)] ADH4 {ECO:0000313|RefSeq:XP_004748248.1};
GN Name=ADH4 {ECO:0000313|Ensembl:ENSMPUP00000009560.1,
GN ECO:0000313|RefSeq:XP_004748248.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000009560.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000009560.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004748248.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004748248.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-II subfamily. {ECO:0000256|ARBA:ARBA00007704}.
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DR EMBL; AEYP01024328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004748248.1; XM_004748191.3.
DR STRING; 9669.ENSMPUP00000009560; -.
DR Ensembl; ENSMPUT00000009716.1; ENSMPUP00000009560.1; ENSMPUG00000009636.1.
DR GeneID; 101689481; -.
DR KEGG; mpuf:101689481; -.
DR CTD; 127; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000162645; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR OMA; LNWAPSC; -.
DR OrthoDB; 1077476at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IEA:Ensembl.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:Ensembl.
DR GO; GO:0005503; F:all-trans retinal binding; IEA:Ensembl.
DR GO; GO:0019115; F:benzaldehyde dehydrogenase [NAD(P)+] activity; IEA:Ensembl.
DR GO; GO:0051287; F:NAD binding; IEA:Ensembl.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IEA:Ensembl.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:Ensembl.
DR GO; GO:0019841; F:retinol binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0046164; P:alcohol catabolic process; IEA:Ensembl.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:Ensembl.
DR GO; GO:0006069; P:ethanol oxidation; IEA:Ensembl.
DR GO; GO:0010430; P:fatty acid omega-oxidation; IEA:Ensembl.
DR GO; GO:1901661; P:quinone metabolic process; IEA:Ensembl.
DR GO; GO:0042572; P:retinol metabolic process; IEA:Ensembl.
DR CDD; cd08299; alcohol_DH_class_I_II_IV; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_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 PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF14; ALL-TRANS-RETINOL DEHYDROGENASE [NAD(+)] ADH4; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 19..378
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 380 AA; 40733 MW; 62FE0FBFE394EDE6 CRC64;
MGTKGKVIKC KAAVAWETGK PLCIEEVEVA PPKAHEVRVQ IIATALCHTD AHPINPKFKD
GLLPVILGHE GAGIVESVGP GVTNFKPGDK VIPLYMPQCR KCKFCLSPLT NFCTKLSLDK
NPLIDQELMQ DKTSRFTCKG KPIYHFMGTS TFAQYTVVSD INLAKIDDDA NLERVCLFGC
GFSTGYGAAI NTAKVTPGST CAVFGLGGVG LSAIMGCKVA GASRIIAIDI NSEKFTKAKA
LGATDCLNPR NLDKPIQEVI IEMTGGGVDF ALDCAGGPET MRAALDSTTA GWGSCTFIGV
DSEMRGLMIS PVELIMGRTV NGTCFGGWKS IDSIPKLVTD YKKKKIDLDI LVTHTLPFDK
INEAFELMNQ GKSIRIVLTF
//
