ID H2MF51_ORYLA Unreviewed; 316 AA.
AC H2MF51;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Retinol dehydrogenase {ECO:0000256|PIRNR:PIRNR000095};
DE EC=1.1.1.300 {ECO:0000256|PIRNR:PIRNR000095};
GN Name=zgc:109982 {ECO:0000313|Ensembl:ENSORLP00000017221.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000017221.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000017221.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017221.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000017221.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017221.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Retinol dehydrogenase with a clear preference for NADP.
CC Converts all-trans-retinal to all-trans-retinol. May play a role in the
CC regeneration of visual pigment at high light intensity.
CC {ECO:0000256|PIRNR:PIRNR000095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.300; Evidence={ECO:0000256|PIRNR:PIRNR000095};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|PIRNR:PIRNR000095}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|PIRNR:PIRNR000095,
CC ECO:0000256|RuleBase:RU000363}.
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DR RefSeq; XP_004068197.1; XM_004068149.2.
DR AlphaFoldDB; H2MF51; -.
DR STRING; 8090.ENSORLP00000017221; -.
DR Ensembl; ENSORLT00000017222.2; ENSORLP00000017221.2; ENSORLG00000013730.2.
DR GeneID; 101168360; -.
DR KEGG; ola:101168360; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000155412; -.
DR HOGENOM; CLU_010194_2_9_1; -.
DR InParanoid; H2MF51; -.
DR OrthoDB; 2898074at2759; -.
DR TreeFam; TF105451; -.
DR Proteomes; UP000001038; Chromosome 4.
DR Bgee; ENSORLG00000013730; Expressed in sexually immature organism and 3 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase [NAD(P)] activity; IEA:InterPro.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR011348; 17beta_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43391:SF9; RETINOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43391; RETINOL DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR PIRSF; PIRSF000095; 17beta-HSD; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|PIRNR:PIRNR000095};
KW NADP {ECO:0000256|PIRNR:PIRNR000095};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000095};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Sensory transduction {ECO:0000256|PIRNR:PIRNR000095}.
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000095-1"
FT BINDING 10..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000095-2"
FT BINDING 64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000095-2"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000095-2"
FT BINDING 158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000095-2"
SQ SEQUENCE 316 AA; 35801 MW; AAD65BE2A4DC5C4E CRC64;
MNQKVVLITG CSSGIGLALA CRIAKDEKKR FMVYATMRDL HKAKPLIDAA GRTLGRTLEI
KKLDVCDEDS IKDCIDSLPE RRVDILISNA GMGLIGPIEC QSIDEMKTVM DTNFFGLVRL
LKEILPDMKK RKKGHIVVIS SVMGIQGILF NDVYAASKFA VEGFCESLAI QALRFNLNIS
LIEPGPVLTE FERKVYDEGV KIDLSKADKP TADMFTNIYL KNYKQIFETL GQSAEDIAEH
TLKIITMENP PFRHQTNTLY TPMTTLKYAD PNGDLPIDTF YKMVFEHDKV FNASLNFLKL
LRWRSRKSFT LEKDKN
//
