ID H9Z3H1_MACMU Unreviewed; 610 AA.
AC H9Z3H1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=All-trans-retinol 13,14-reductase {ECO:0000256|ARBA:ARBA00041141};
DE EC=1.3.99.23 {ECO:0000256|ARBA:ARBA00038979};
GN Name=RETSAT {ECO:0000313|EMBL:AFH30487.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFH30487.1};
RN [1] {ECO:0000313|EMBL:AFH30487.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thymus {ECO:0000313|EMBL:AFH30487.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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:0000256|ARBA:ARBA00036004};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|ARBA:ARBA00001937};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC CrtISO subfamily. {ECO:0000256|ARBA:ARBA00005855}.
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DR EMBL; JU473683; AFH30487.1; -; mRNA.
DR AlphaFoldDB; H9Z3H1; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 2: Evidence at transcript level;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..610
FT /note="All-trans-retinol 13,14-reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003623437"
SQ SEQUENCE 610 AA; 66976 MW; 0FCB695FC4102485 CRC64;
MWLPLVLFLT 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 FICLRGTKED LHLPSTNYYV YHDTDMDQAM
ERYVSMPREK AAEHIPLLFI AFPSAKDPTW EDRFPGRSSM TMLIPSAYEW FEEWQAELKG
KRGSDYETFK NSFVEASMSV VMKLFPQLEG KVESVTAGSP LTNQFYLAAP RGACYGADHD
LGRLHPRVMA SLRAQSPIPN LYLTGQDIFT CGLVGALQGA LLCSSAILKR NLYSDLKDLG
SRIQAQKKKN
//
