ID   RETST_DANRE             Reviewed;         607 AA.
AC   Q5BLE8; Q6DBT4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=All-trans-retinol 13,14-reductase {ECO:0000303|PubMed:17253779};
DE            EC=1.3.99.23 {ECO:0000269|PubMed:17253779};
DE   AltName: Full=All-trans-13,14-dihydroretinol saturase A {ECO:0000303|PubMed:17253779};
DE            Short=RetSat A {ECO:0000303|PubMed:17253779};
DE   AltName: Full=All-trans-retinol 7,8-reductase {ECO:0000305|PubMed:17253779};
DE   Flags: Precursor;
GN   Name=retsat {ECO:0000305}; Synonyms=retsata {ECO:0000303|PubMed:17253779};
GN   ORFNames=zgc:113107;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17253779; DOI=10.1021/bi062147u;
RA   Moise A.R., Isken A., Dominguez M., de Lera A.R., von Lintig J.,
RA   Palczewski K.;
RT   "Specificity of zebrafish retinol saturase: formation of all-trans-13,14-
RT   dihydroretinol and all-trans-7,8-dihydroretinol.";
RL   Biochemistry 46:1811-1820(2007).
CC   -!- FUNCTION: Catalyzes the saturation of all-trans-retinol to all-trans-
CC       13,14-dihydroretinol. In addition, saturates the 7-8 double bond of
CC       all-trans-retinol to produce all-trans-7,8-dihydroretinol. Can also use
CC       vitamin A2 (all-trans-3,4-didehydroretinol) as a substrate, to produce
CC       all-trans-13,14-dihydro-3,4-didehydroretinol or all-trans-7,8-dihydro-
CC       3,4-didehydroretinol. May play a role in vitamin A metabolism.
CC       {ECO:0000269|PubMed:17253779}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + all-trans-13,14-dihydroretinol = AH2 + all-trans-retinol;
CC         Xref=Rhea:RHEA:19193, ChEBI:CHEBI:13193, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:52075; EC=1.3.99.23;
CC         Evidence={ECO:0000269|PubMed:17253779};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000250|UniProtKB:Q8S4R4};
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:Q8S4R4};
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q8S4R4};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q64FW2}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q64FW2}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in liver at 72 hours post-fertilization
CC       (hpf) and gut at 96 hpf. Not detected at earlier stages of development.
CC       {ECO:0000269|PubMed:17253779}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtISO subfamily. {ECO:0000305}.
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DR   EMBL; BC078372; AAH78372.1; -; mRNA.
DR   EMBL; BC090469; AAH90469.1; -; mRNA.
DR   RefSeq; NP_001015061.1; NM_001015061.2.
DR   AlphaFoldDB; Q5BLE8; -.
DR   SMR; Q5BLE8; -.
DR   STRING; 7955.ENSDARP00000024120; -.
DR   PaxDb; Q5BLE8; -.
DR   Ensembl; ENSDART00000013167; ENSDARP00000024120; ENSDARG00000018600.
DR   GeneID; 325922; -.
DR   KEGG; dre:325922; -.
DR   CTD; 325922; -.
DR   ZFIN; ZDB-GENE-050320-11; retsat.2.
DR   eggNOG; KOG4254; Eukaryota.
DR   GeneTree; ENSGT00390000017613; -.
DR   HOGENOM; CLU_019722_1_0_1; -.
DR   InParanoid; Q5BLE8; -.
DR   OMA; AFMFADW; -.
DR   OrthoDB; 873686at2759; -.
DR   PhylomeDB; Q5BLE8; -.
DR   TreeFam; TF328375; -.
DR   BRENDA; 1.3.99.23; 928.
DR   PRO; PR:Q5BLE8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 3.
DR   Bgee; ENSDARG00000018600; Expressed in liver and 27 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0051786; F:all-trans-retinol 13,14-reductase activity; IDA:ZFIN.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Lipid metabolism; Membrane; NAD;
KW   NADP; Oxidoreductase; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..607
FT                   /note="All-trans-retinol 13,14-reductase"
FT                   /id="PRO_0000225669"
FT   CONFLICT        572
FT                   /note="L -> S (in Ref. 1; AAH78372)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   607 AA;  67937 MW;  4B387672D3AA2E02 CRC64;
     MWFAVVAIFL ALVAFLYRYV VGSGPNPFAI DTREPLKPMV FDRKLKNKVL KQGFLASRVP
     EDLDAVVVGS GIGGLAIAVL LAKVGKKVLV LEQHDRAGGC CHTFKEQGFE FDVGIHYIGE
     LSNHKPLRCI IDQMTNGQLQ WDPLENPFDN VVIGPPENRR IYQIYSGRKR YMDELKKCFP
     GEEKAIDEYV RLCKEVGQGV WVMVLLKFLP TPIANFLVRT GLANRLTSFS RYASRSLTDV
     VNELTQNKDL RAVLSYIFGT YGKIPKEASF SMHSLIVNHY MNGAWYPKGG ATEIAYHMIP
     IIEKAGGAVL VRAPVNRILL NDAKEAIGVS VLKGQEEVHV RAPIVISDAG IFNTYEYLLP
     KDVQTMPAIQ KQLSMLQHGD SGLSIFIGLD GTKEELGLKA DNYFIYPENN IDELLEDYRS
     GNREESAKKN PLIFVASPSA KDSTWPERTP GKSTLTVVSF ANYEWFEEWK DDKVKNRSTD
     YKQLKELFIN YILEAVTEIY PKIKDRIEYV DAGTPITNQH YIAAPRGEIY GADHGIPRFS
     AELNATIRAQ TPIKNLYLTG QDLMLCGFAG ALTGALTCGS VILNRNLHLE AFSLAKRVQN
     GNNKKKT