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All-trans-retinol 13,14-reductase (EC 1.3.99.23) (All-trans-13,14-dihydroretinol saturase) (RetSat) (PPAR-alpha-regulated and starvation-induced gene protein)

 RETST_MOUSE             Reviewed;         609 AA.
Q64FW2; Q149J8; Q3UNN9; Q78JX8; Q8VHE7; Q9CW85;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
10-OCT-2018, entry version 115.
RecName: Full=All-trans-retinol 13,14-reductase;
EC=1.3.99.23;
AltName: Full=All-trans-13,14-dihydroretinol saturase;
Short=RetSat;
AltName: Full=PPAR-alpha-regulated and starvation-induced gene protein;
Flags: Precursor;
Name=Retsat; Synonyms=Ppsig;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=A/J;
PubMed=11753649; DOI=10.1038/sj.onc.1204941;
Wang Y., Hu L., Yao R., Wang M., Crist K.A., Grubbs C.J.,
Johanning G.L., Lubet R.A., You M.;
"Altered gene expression profile in chemically induced rat mammary
adenocarcinomas and its modulation by an aromatase inhibitor.";
Oncogene 20:7710-7721(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=15358783; DOI=10.1074/jbc.M409130200;
Moise A.R., Kuksa V., Imanishi Y., Palczewski K.;
"Identification of all-trans-retinol: all-trans-13,14-dihydroretinol
saturase.";
J. Biol. Chem. 279:50230-50242(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=129/Sv, and 129S6/SvEvTac; TISSUE=Liver, and Spleen;
PubMed=18289917; DOI=10.1016/j.biocel.2008.01.006;
Sun Y., Ng L., Lam W., Lo C.K., Chan P.T., Yuen Y.L., Wong P.F.,
Tsang D.S., Cheung W.T., Lee S.S.;
"Identification and characterization of a novel mouse peroxisome
proliferator-activated receptor alpha-regulated and starvation-induced
gene, Ppsig.";
Int. J. Biochem. Cell Biol. 40:1775-1791(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C3H/HeJ, and C57BL/6J; TISSUE=Brain, and Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, INDUCTION BY PPARG, AND MUTAGENESIS OF 1-MET--HIS-17;
91-ARG--GLU-96 AND GLU-96.
PubMed=19139408; DOI=10.1073/pnas.0812065106;
Schupp M., Lefterova M.I., Janke J., Leitner K., Cristancho A.G.,
Mullican S.E., Qatanani M., Szwergold N., Steger D.J., Curtin J.C.,
Kim R.J., Suh M.J., Suh M., Albert M.R., Engeli S., Gudas L.J.,
Lazar M.A.;
"Retinol saturase promotes adipogenesis and is downregulated in
obesity.";
Proc. Natl. Acad. Sci. U.S.A. 106:1105-1110(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=19940255; DOI=10.1096/fj.09-147207;
Moise A.R., Lobo G.P., Erokwu B., Wilson D.L., Peck D., Alvarez S.,
Dominguez M., Alvarez R., Flask C.A., de Lera A.R., von Lintig J.,
Palczewski K.;
"Increased adiposity in the retinol saturase-knockout mouse.";
FASEB J. 24:1261-1270(2010).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=28855500; DOI=10.1038/s41467-017-00430-w;
Heidenreich S., Witte N., Weber P., Goehring I., Tolkachov A.,
von Loeffelholz C., Doecke S., Bauer M., Stockmann M.,
Pfeiffer A.F.H., Birkenfeld A.L., Pietzke M., Kempa S., Muenzner M.,
Schupp M.;
"Retinol saturase coordinates liver metabolism by regulating ChREBP
activity.";
Nat. Commun. 8:384-384(2017).
-!- FUNCTION: Catalyzes the saturation of all-trans-retinol to all-
trans-13,14-dihydroretinol (PubMed:19940255). Does not exhibit any
activity toward all-trans-retinoic acid, nor 9-cis, 11-cis or 13-
cis-retinol isomers. May play a role in the metabolism of vitamin
A (PubMed:15358783). Independently of retinol conversion, may
regulate liver metabolism upstream of MLXIPL/ChREBP
(PubMed:28855500). Required for adipocyte differentiation in a
3T3-L1 cell culture model (PubMed:19139408). This effect seems not
to mimic the in vivo situation in which animals show increased
adiposity in the absence of RETSAT (PubMed:19940255).
{ECO:0000269|PubMed:15358783, ECO:0000269|PubMed:19139408,
ECO:0000269|PubMed:19940255, ECO:0000269|PubMed:28855500}.
-!- CATALYTIC ACTIVITY: All-trans-13,14-dihydroretinol + acceptor =
all-trans-retinol + reduced acceptor.
{ECO:0000269|PubMed:15358783}.
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15358783, ECO:0000269|PubMed:19139408};
Peripheral membrane protein {ECO:0000269|PubMed:15358783}.
-!- TISSUE SPECIFICITY: Predominantly expressed in the liver (at
protein level) (PubMed:19940255). Also expressed at high levels in
kidney, intestine, and white fat and brown fat (PubMed:15358783,
PubMed:18289917, PubMed:19139408, PubMed:28855500). Weakly
expressed in heart, skeletal muscle and testis and barely detected
in the lung, brain and spleen (PubMed:15358783, PubMed:18289917,
PubMed:28855500). Up-regulated in the liver of diet-induced obese
mice, compared to lean animals (PubMed:28855500). Down-regulated
in adipose tissue of obese mice; this decrease could be due to the
impact of inflammatory cells on adipocytes (PubMed:19139408).
{ECO:0000269|PubMed:15358783, ECO:0000269|PubMed:18289917,
ECO:0000269|PubMed:19139408, ECO:0000269|PubMed:19940255,
ECO:0000269|PubMed:28855500}.
-!- DEVELOPMENTAL STAGE: Up-regulated during adipocyte differentiation
in a 3T3-L1 cell culture model (at protein level).
{ECO:0000269|PubMed:19139408, ECO:0000269|PubMed:19940255}.
-!- INDUCTION: Up-regulated during starvation (PubMed:18289917). Up-
regulated by PPARG (PubMed:19139408).
{ECO:0000269|PubMed:18289917, ECO:0000269|PubMed:19139408}.
-!- DISRUPTION PHENOTYPE: Knockout mice fed either low-fat or high-fat
(HFD) diets gain weight at a similar rate as their wild-type
littermates and show normal insulin resistance and glucose
tolerance. However, they exhibit increased adiposity and increased
expression of key adipogenic markers, including PPAR-gamma and its
target adipocyte P2 (aP2/FABP4), while maintained on an HFD.
{ECO:0000269|PubMed:19940255}.
-!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase
family. CrtISO subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB22406.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF466400; AAL73986.1; -; Genomic_DNA.
EMBL; AY704159; AAU25836.1; -; mRNA.
EMBL; EF620363; ABS17600.1; -; mRNA.
EMBL; EF620364; ABS17601.1; -; mRNA.
EMBL; EF620365; ABS17602.1; -; mRNA.
EMBL; EF620366; ABS17603.1; -; Genomic_DNA.
EMBL; AK002851; BAB22406.2; ALT_INIT; mRNA.
EMBL; AK144115; BAE25708.1; -; mRNA.
EMBL; AC125039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466523; EDK98989.1; -; Genomic_DNA.
EMBL; BC011203; AAH11203.2; -; mRNA.
EMBL; BC117751; AAI17752.1; -; mRNA.
CCDS; CCDS20244.1; -.
RefSeq; NP_080435.3; NM_026159.4.
UniGene; Mm.305108; -.
ProteinModelPortal; Q64FW2; -.
STRING; 10090.ENSMUSP00000068568; -.
iPTMnet; Q64FW2; -.
PhosphoSitePlus; Q64FW2; -.
MaxQB; Q64FW2; -.
PaxDb; Q64FW2; -.
PRIDE; Q64FW2; -.
Ensembl; ENSMUST00000070597; ENSMUSP00000068568; ENSMUSG00000056666.
GeneID; 67442; -.
KEGG; mmu:67442; -.
UCSC; uc009cix.1; mouse.
CTD; 54884; -.
MGI; MGI:1914692; Retsat.
eggNOG; KOG4254; Eukaryota.
eggNOG; COG1233; LUCA.
GeneTree; ENSGT00390000017613; -.
HOGENOM; HOG000233930; -.
HOVERGEN; HBG079484; -.
InParanoid; Q64FW2; -.
KO; K09516; -.
OMA; QDIFTCG; -.
OrthoDB; EOG091G04VP; -.
TreeFam; TF328375; -.
BioCyc; MetaCyc:MONOMER-16797; -.
BRENDA; 1.3.99.23; 3474.
ChiTaRS; Retsat; mouse.
PRO; PR:Q64FW2; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000056666; Expressed in 238 organ(s), highest expression level in liver.
ExpressionAtlas; Q64FW2; baseline and differential.
Genevisible; Q64FW2; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC.
GO; GO:0031965; C:nuclear membrane; IDA:HGNC.
GO; GO:0005640; C:nuclear outer membrane; IDA:HGNC.
GO; GO:0051786; F:all-trans-retinol 13,14-reductase activity; IDA:HGNC.
GO; GO:0016491; F:oxidoreductase activity; IDA:HGNC.
GO; GO:0055114; P:oxidation-reduction process; IDA:HGNC.
GO; GO:0042572; P:retinol metabolic process; IDA:HGNC.
Gene3D; 3.50.50.60; -; 2.
InterPro; IPR036188; FAD/NAD-bd_sf.
SUPFAM; SSF51905; SSF51905; 2.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane;
NAD; NADP; Oxidoreductase; Reference proteome; Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 609 All-trans-retinol 13,14-reductase.
/FTId=PRO_0000225667.
NP_BIND 69 97 FAD or NAD or NADP. {ECO:0000255}.
MUTAGEN 1 17 Missing: Loss of localization to the
endoplasmic reticulum.
{ECO:0000269|PubMed:19139408}.
MUTAGEN 91 96 Missing: Loss of catalytic activity, as
measured by the saturation of retinol to
13,14-dihydroretinol. Loss of adipocyte
differentiation in a 3T3-L1 cell culture
model. {ECO:0000269|PubMed:19139408}.
MUTAGEN 96 96 E->A: Loss of catalytic activity, as
measured by the saturation of retinol to
13,14-dihydroretinol. Loss of adipocyte
differentiation in a 3T3-L1 cell culture
model. {ECO:0000269|PubMed:19139408}.
CONFLICT 273 273 A -> T (in Ref. 1; AAL73986 and 4;
BAE25708). {ECO:0000305}.
CONFLICT 293 293 G -> R (in Ref. 1; AAL73986 and 4;
BAE25708). {ECO:0000305}.
CONFLICT 306 306 I -> V (in Ref. 7; AAH11203).
{ECO:0000305}.
CONFLICT 451 451 E -> D (in Ref. 4; BAE25708).
{ECO:0000305}.
CONFLICT 495 495 A -> V (in Ref. 4; BAB22406).
{ECO:0000305}.
SEQUENCE 609 AA; 67334 MW; 7BC21825B8A4ABD2 CRC64;
MWITALLLAV LLLVILHRVY VGLYAASSPN PFAEDVKRPP EPLVTDKEAR KKVLKQAFSV
SRVPEKLDAV VIGSGIGGLA SAAVLAKAGK RVLVLEQHTK AGGCCHTFGE NGLEFDTGIH
YIGRMREGNI GRFILDQITE GQLDWAPMAS PFDLMILEGP NGRKEFPMYS GRKEYIQGLK
KKFPKEEAVI DKYMELVKVV ARGVSHAVLL KFLPLPLTQL LSKFGLLTRF SPFCRASTQS
LAEVLQQLGA SRELQAVLSY IFPTYGVTPS HTAFSLHALL VDHYIQGAYY PRGGSSEIAF
HTIPLIQRAG GAVLTRATVQ SVLLDSAGRA CGVSVKKGQE LVNIYCPVVI SNAGMFNTYQ
HLLPETVRHL PDVKKQLAMV RPGLSMLSIF ICLKGTKEDL KLQSTNYYVY FDTDMDKAME
RYVSMPKEKA PEHIPLLFIA FPSSKDPTWE ERFPDRSTMT ALVPMAFEWF EEWQEEPKGK
RGVDYETLKN AFVEASMSVI MKLFPQLEGK VESVTGGSPL TNQYYLAAPR GATYGADHDL
ARLHPHAMAS IRAQTPIPNL YLTGQDIFTC GLMGALQGAL LCSSAILKRN LYSDLQALGS
KVKAQKKKM


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