ID   RETST_RAT               Reviewed;         609 AA.
AC   Q8VHE9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=All-trans-retinol 13,14-reductase;
DE            EC=1.3.99.23 {ECO:0000250|UniProtKB:Q64FW2};
DE   AltName: Full=All-trans-13,14-dihydroretinol saturase;
DE            Short=RetSat;
DE   AltName: Full=PPAR-alpha-regulated and starvation-induced gene protein;
DE   AltName: Full=RMT-7;
DE   Flags: Precursor;
GN   Name=Retsat; Synonyms=Ppsig, Rmt7;
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   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=11753649; DOI=10.1038/sj.onc.1204941;
RA   Wang Y., Hu L., Yao R., Wang M., Crist K.A., Grubbs C.J., Johanning G.L.,
RA   Lubet R.A., You M.;
RT   "Altered gene expression profile in chemically induced rat mammary
RT   adenocarcinomas and its modulation by an aromatase inhibitor.";
RL   Oncogene 20:7710-7721(2001).
CC   -!- FUNCTION: Catalyzes the saturation of all-trans-retinol to all-trans-
CC       13,14-dihydroretinol. Does not exhibit any activity toward all-trans-
CC       retinoic acid, nor 9-cis, 11-cis or 13-cis-retinol isomers. May play a
CC       role in the metabolism of vitamin A. Independently of retinol
CC       conversion, may regulate liver metabolism upstream of MLXIPL/ChREBP.
CC       May play a role in adipocyte differentiation.
CC       {ECO:0000250|UniProtKB:Q64FW2}.
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:0000250|UniProtKB:Q64FW2};
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   -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney and heart.
CC       {ECO:0000269|PubMed:11753649}.
CC   -!- INDUCTION: Down-regulated in mammary adenocarcinomas.
CC       {ECO:0000269|PubMed:11753649}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtISO subfamily. {ECO:0000305}.
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DR   EMBL; AF465614; AAL73494.1; -; mRNA.
DR   RefSeq; NP_659552.1; NM_145084.1.
DR   AlphaFoldDB; Q8VHE9; -.
DR   SMR; Q8VHE9; -.
DR   STRING; 10116.ENSRNOP00000019571; -.
DR   iPTMnet; Q8VHE9; -.
DR   PhosphoSitePlus; Q8VHE9; -.
DR   jPOST; Q8VHE9; -.
DR   PaxDb; Q8VHE9; -.
DR   PRIDE; Q8VHE9; -.
DR   GeneID; 246298; -.
DR   KEGG; rno:246298; -.
DR   UCSC; RGD:628802; rat.
DR   CTD; 54884; -.
DR   RGD; 628802; Retsat.
DR   eggNOG; KOG4254; Eukaryota.
DR   InParanoid; Q8VHE9; -.
DR   OrthoDB; 873686at2759; -.
DR   PhylomeDB; Q8VHE9; -.
DR   PRO; PR:Q8VHE9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC-UCL.
DR   GO; GO:0031965; C:nuclear membrane; ISS:HGNC-UCL.
DR   GO; GO:0005640; C:nuclear outer membrane; ISS:HGNC-UCL.
DR   GO; GO:0051786; F:all-trans-retinol 13,14-reductase activity; ISS:HGNC-UCL.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0042572; P:retinol metabolic process; ISS:HGNC-UCL.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Lipid metabolism; Membrane; NAD;
KW   NADP; Oxidoreductase; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..609
FT                   /note="All-trans-retinol 13,14-reductase"
FT                   /id="PRO_0000225668"
SQ   SEQUENCE   609 AA;  67531 MW;  D492DC98E8D23963 CRC64;
     MWITALLLVV LLLVVVHRVY VGLFTGSSPN PFAEDVKRPP EPLVTDKEAR KKVLKQAFSV
     SRVPEKLDAV VIGSGIGGLA SAAVLAKAGK RVLVLEQHTK AGGCCHTFGE NGLEFDTGIH
     YIGRMREGNI GRFILDQITE GQLDWAPMAS PFDLMILEGP NGRKEFPMYS GRKEYIQGLK
     EKFPKEEAVI DKYMELVKVV AHGVSHAILL KFLPLPLTQL LNKFGLLTRF SPFCRASTQS
     LAEVLKQLGA SPELQAVLSY ILPTYGVTPS HTTFSLHALL VDHYIQGAYY PRRGSSEIAF
     HTIPLIQRAG GAVLTRATVQ SVLLDSAGRA CGVSVKKGQE LVNIYCPVVI SNAGMFNTYQ
     HLLPESVRYL PDVKKQLTMV KPGLSMLSIF ICLKGTKEEL KLQSTNYYVY FDTDMDKAME
     CYVSMPKEKA PEHIPLLFIP FPSSKDPTWE DRFPDRSTMT VLVPTAFEWF EEWQEEPKGK
     RGVDYETLKN TFREASMSVI MKLFPQLEGK VESVTGGSPL TNQYYLAAHR GATYGADHDL
     ARLHPHAMAS LRAQTPIPNL YLTGQDIFTC GLMGALQGAL LCSSAILKRN LYSDLQALGS
     KVRAQKKKK