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 27-MAR-2024, entry version 121.
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; 7955-ENSDARP00000024120; -.
DR GeneID; 325922; -.
DR KEGG; dre:325922; -.
DR AGR; ZFIN:ZDB-GENE-050320-11; -.
DR CTD; 325922; -.
DR ZFIN; ZDB-GENE-050320-11; retsat.2.
DR eggNOG; KOG4254; Eukaryota.
DR HOGENOM; CLU_019722_1_0_1; -.
DR InParanoid; Q5BLE8; -.
DR OMA; AFMFADW; -.
DR OrthoDB; 36283at2759; -.
DR PhylomeDB; Q5BLE8; -.
DR TreeFam; TF328375; -.
DR BRENDA; 1.3.99.23; 928.
DR PRO; PR:Q5BLE8; -.
DR Proteomes; UP000000437; Chromosome 3.
DR Bgee; ENSDARG00000018600; Expressed in liver and 27 other cell types or 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:0042572; P:retinol metabolic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR46091:SF1; ALL-TRANS-RETINOL 13,14-REDUCTASE; 1.
DR PANTHER; PTHR46091; BLR7054 PROTEIN; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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
//
