ID   RETST_MACFA             Reviewed;         610 AA.
AC   Q64FG0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   04-NOV-2026, entry version 75.
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   Flags: Precursor;
GN   Name=RETSAT; Synonyms=PPSIG;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15358783; DOI=10.1074/jbc.m409130200;
RA   Moise A.R., Kuksa V., Imanishi Y., Palczewski K.;
RT   "Identification of all-trans-retinol: all-trans-13,14-dihydroretinol
RT   saturase.";
RL   J. Biol. Chem. 279:50230-50242(2004).
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=all-trans-13,14-dihydroretinol + A = all-trans-retinol + AH2;
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   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtISO subfamily. {ECO:0000305}.
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DR   EMBL; AY707524; AAU34019.1; -; mRNA.
DR   AlphaFoldDB; Q64FG0; -.
DR   SMR; Q64FG0; -.
DR   STRING; 9541.ENSMFAP00000003799; -.
DR   eggNOG; KOG4254; Eukaryota.
DR   OMA; AANMLFW; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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:UniProtKB.
DR   GO; GO:0042572; P:retinol metabolic process; ISS:HGNC-UCL.
DR   FunFam; 3.50.50.60:FF:000139; All-trans-retinol 13,14-reductase; 1.
DR   FunFam; 3.50.50.60:FF:000178; All-trans-retinol 13,14-reductase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR052206; Retinol_saturase.
DR   PANTHER; PTHR46091:SF1; ALL-TRANS-RETINOL 13,14-REDUCTASE; 1.
DR   PANTHER; PTHR46091; BLR7054 PROTEIN; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..610
FT                   /note="All-trans-retinol 13,14-reductase"
FT                   /id="PRO_0000225666"
SQ   SEQUENCE   610 AA;  66918 MW;  FD74D22F28129FB1 CRC64;
     MWLPLVLFLA VLLLAVVCKV YLGLFSGKSP NPFSEDVKRP PAPLVTDKEA RKKVLKQAFS
     ASRVPEKLDV VVIGSGFGGL AAAAILAKAG KRVLVLEQHT KAGGACHTFG ENGLEFDTGI
     HYIGRMEEGS IGRFILDQIT EGQLDWVPMS SPFDIMVLEG PNGRKEYPMY SGEKAYIQGL
     KEKFPQEEAI IDKYIKLVKV VSNGVAHAIL LKFLPLPVIQ LLDRCGLLTR FSPFLHASTQ
     SLAEVLQQLG ASSELQAVLS YIFPTYGVTP RHSAFSMHAL LVNHYLKGAF YPRGGSSEIA
     FHTIPVIQRA GGAVLTRATV QSVLLDSAGK ACGVSVKKGH ELVNIYCPVV VSNAGLFNTY
     EHLLPGNARC LPGVKQQLGM VRPGLGMMSV FICLQGTKED LHLPSTNYYV YHDTDMDQAM
     ERYVSMPREK AAEHIPLLFI AFPSAKDPTW EDRFPGRSSM IMLIPSAYEW FEEWQAELKG
     KRGSDYETYK NSFVEASMSV AMKLFPQLEG KVESVTAGSP LTNQFYLAAP RGACYGADHD
     LGRLHPRVMA SLRAQSPIPN LYLTGQDIFT CGLVGALQGA LLCSSAILKR NLYSDLKDLG
     SRIQAQKKKN
//