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   25-NOV-2008, entry version 26.
DE   RecName: Full=All-trans-retinol 13,14-reductase;
DE            EC=1.3.99.23;
DE   AltName: Full=All-trans-13,14-dihydroretinol saturase;
DE            Short=RetSat;
DE   Flags: Precursor;
GN   Name=RETSAT;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; 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: Retinol saturase carrying out the saturation of the 13-
CC       14 double bond of all-trans-retinol to produce all-trans-13,14-
CC       dihydroretinol. Has activity toward all-trans-retinol as
CC       substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis
CC       or 13-cis-retinol isomers as substrates. May play a role in the
CC       metabolism of vitamin A (By similarity).
CC   -!- CATALYTIC ACTIVITY: All-trans-13,14-dihydroretinol + acceptor =
CC       all-trans-retinol + reduced acceptor.
CC   -!- COFACTOR: NAD, NADP, or FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase
CC       family. CrtISO subfamily.
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DR   EMBL; AY707524; AAU34019.1; -; mRNA.
DR   HOVERGEN; Q64FG0; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC.
DR   GO; GO:0005640; C:nuclear outer membrane; ISS:HGNC.
DR   GO; GO:0051786; F:all-trans-retinol 13,14-reductase activity; ISS:HGNC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; ISS:HGNC.
DR   GO; GO:0042572; P:retinol metabolic process; ISS:HGNC.
DR   InterPro; IPR000759; Adrndx_reductase.
DR   InterPro; IPR003953; FAD_bind2_N.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   ProDom; PD139017; Phytn_dehydro; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Membrane; NAD; NADP;
KW   Oxidoreductase; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    610       All-trans-retinol 13,14-reductase.
FT                                /FTId=PRO_0000225666.
FT   NP_BIND      70     98       FAD or NAD or NADP (Potential).
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
//