ID I3MUW2_ICTTR Unreviewed; 610 AA.
AC I3MUW2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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|Ensembl:ENSSTOP00000015907.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000015907.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000015907.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AGTP01097963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005338514.1; XM_005338457.2.
DR AlphaFoldDB; I3MUW2; -.
DR STRING; 43179.ENSSTOP00000015907; -.
DR Ensembl; ENSSTOT00000029471.2; ENSSTOP00000015907.1; ENSSTOG00000026131.2.
DR GeneID; 101972432; -.
DR CTD; 54884; -.
DR eggNOG; KOG4254; Eukaryota.
DR GeneTree; ENSGT00390000017613; -.
DR HOGENOM; CLU_019722_1_0_1; -.
DR InParanoid; I3MUW2; -.
DR OMA; AFMFADW; -.
DR OrthoDB; 36283at2759; -.
DR TreeFam; TF328375; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl.
DR GO; GO:0051786; F:all-trans-retinol 13,14-reductase activity; IEA:Ensembl.
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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..610
FT /note="All-trans-retinol 13,14-reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003677470"
SQ SEQUENCE 610 AA; 67232 MW; 5A1C911B3AAA9650 CRC64;
MWLSLVLLLV LLLLAGVRRV YLGLFAGRSP NPFLQDVKRP PAPLVTDKEA RKRVLKQVFS
ASQVPENLDV VVIGSGIGGL AAAAILAKAG KRVLVLEQHT KAGGCCHTFG KNGLEFDTGI
HYIGHMEEGT FGRFILDQIT EGQLDWASLS SPFDTVVLDR PSGRKEFPMY SGKKAYIEGL
KEKFPQEKDV IDKYIKLVKV VADGSIHAIL LKFLPLCVAQ LLSKCGLLTR FSPFLHASTQ
SLAEVLQQLG ASPELQAVLS YIFPTYGVTP SRTTFSMHAL LVNHYLQGAF YPRGGSSEIA
FHIIPVIKQA GGAVLTKATV QTVLLDSAGK ACGVRVKKGQ ELVDIYCPTV VSNAGLFNTY
EHLLPESARC LSGVQQQLQM VRPGLSMFSV FICLHGTKEE LGLQSTNYYV YFDINMDKAM
ERYISMPREK AVEHIPLYFI ASPSSKDPTW PGRFPDRSTL TVLIPTAYEW FEEWQEEPQG
KRSHDYETLK SSFVEASISV VLRLFPQLEG KVESATGGSP LTNQFFLAAT RGATYGADHD
LDRLHPYVMA SIRAQSPIPN LYLTGQDIFT CGLMGALQGA LLCSSAILKR NLYSDLKDLG
SRVRAQKKMM
//
