ID G3R0H2_GORGO Unreviewed; 610 AA.
AC G3R0H2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
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:ENSGGOP00000008657.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000008657.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000008657.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000008657.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000008657.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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; CABD030011702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004029584.1; XM_004029535.2.
DR AlphaFoldDB; G3R0H2; -.
DR STRING; 9593.ENSGGOP00000008657; -.
DR Ensembl; ENSGGOT00000008893.3; ENSGGOP00000008657.2; ENSGGOG00000008852.3.
DR GeneID; 101149338; -.
DR KEGG; ggo:101149338; -.
DR CTD; 54884; -.
DR eggNOG; KOG4254; Eukaryota.
DR GeneTree; ENSGT00390000017613; -.
DR HOGENOM; CLU_019722_1_0_1; -.
DR InParanoid; G3R0H2; -.
DR OMA; FCADVHY; -.
DR OrthoDB; 36283at2759; -.
DR TreeFam; TF328375; -.
DR Proteomes; UP000001519; Chromosome 2A.
DR Bgee; ENSGGOG00000008852; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl.
DR GO; GO:0051786; F:all-trans-retinol 13,14-reductase activity; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
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:UP000001519};
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_5003451740"
SQ SEQUENCE 610 AA; 66792 MW; 151412DBB4F96578 CRC64;
MWLPLVLLLA VLLLAVLCKV YLGLFSGSSP NPFSEDVKRP PAPLVTDKEA RKKVLKQAFS
ANRVPEKLDV VVIGSGFGGL AAAAILAKAG KRVLVLEQHT KAGGCCHTFG KNGLEFDTGI
HYIGRMEEGS IGRFILDQIT EGQLDWAPLS SPFDIMVLEG PNGRKEYPMY SGEKAYIQGL
KEKFPQEEAI IDKYIKLVKV VSSGAPHAIL LKFLPLPVVQ LLDRCGLLTR FSPFLQASTQ
SLAEVLQQLG ASSELQAVLS YIFPTYGVTP SHSAFSMHAL LVNHYMKGGF YPRGGSSEIA
FHTIPVIQRA GGAVLTKATV QSVLLDSAGK ACGVSVKKGH ELVNIHCPIV VSNAGLFNTY
EHLLPGNARC LPGVKQQLGT VRPGLGMTSV FICLRGTKED LHLPSTNYYV YYDTDMDQAM
ERYVSMPREE AAEHIPLLFF AFPSAKDPTW EDRFPGRSTM IILIPTAYEW FEEWQAELKG
KRGSDYETFK NSFVEASMSV VLKLFPQLEG KVESVTAGSP LTNQFYLASP RGACYGADHD
LGRLHPCVMA SLRAQSPIPN LYLTGQDIFT CGLVGALQGA LLCSSAILKR NLYSDLKNLD
SRIRAQKKKN
//