RDHE2_MOUSE
ID RDHE2_MOUSE Reviewed; 309 AA.
AC Q7TQA3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Epidermal retinol dehydrogenase 2;
DE Short=EPHD-2;
DE Short=RDH-E2;
DE EC=1.1.1.105 {ECO:0000250|UniProtKB:Q8N3Y7};
DE AltName: Full=Retinal short-chain dehydrogenase reductase 2;
DE Short=retSDR2;
DE AltName: Full=Short-chain dehydrogenase reductase 9;
DE AltName: Full=Short-chain dehydrogenase/reductase family 16C member 5;
GN Name=Sdr16c5 {ECO:0000312|MGI:MGI:2668443}; Synonyms=Rdhe2, Scdr9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.Q., Wu S.L., Cheng Z.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Oxidoreductase with strong preference for NAD. Active in both
CC the oxidative and reductive directions. Oxidizes all-trans-retinol in
CC all-trans-retinaldehyde. No activity was detected with 11-cis-retinol
CC or 11-cis-retinaldehyde as substrates with either NAD(+)/NADH or
CC NADP(+)/NADPH. {ECO:0000250|UniProtKB:Q8N3Y7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-
CC trans-retinal--[retinol-binding protein] + H(+) + NADH;
CC Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:Q8N3Y7};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:Q8N3Y7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N3Y7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AY277588; AAP41074.1; -; mRNA.
DR EMBL; AK136508; BAE23016.1; -; mRNA.
DR EMBL; AL807387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104134; AAI04135.1; -; mRNA.
DR EMBL; BC104135; AAI04136.1; -; mRNA.
DR CCDS; CCDS17944.1; -.
DR RefSeq; NP_871789.1; NM_181989.1.
DR AlphaFoldDB; Q7TQA3; -.
DR SMR; Q7TQA3; -.
DR STRING; 10090.ENSMUSP00000046298; -.
DR PhosphoSitePlus; Q7TQA3; -.
DR PaxDb; Q7TQA3; -.
DR PRIDE; Q7TQA3; -.
DR ProteomicsDB; 255057; -.
DR Antibodypedia; 11761; 118 antibodies from 22 providers.
DR DNASU; 242285; -.
DR Ensembl; ENSMUST00000040925; ENSMUSP00000046298; ENSMUSG00000028236.
DR GeneID; 242285; -.
DR KEGG; mmu:242285; -.
DR UCSC; uc008rww.1; mouse.
DR CTD; 195814; -.
DR MGI; MGI:2668443; Sdr16c5.
DR VEuPathDB; HostDB:ENSMUSG00000028236; -.
DR eggNOG; KOG1201; Eukaryota.
DR GeneTree; ENSGT00940000156731; -.
DR HOGENOM; CLU_010194_2_5_1; -.
DR InParanoid; Q7TQA3; -.
DR OMA; GQSENAY; -.
DR OrthoDB; 1373099at2759; -.
DR PhylomeDB; Q7TQA3; -.
DR TreeFam; TF312837; -.
DR BRENDA; 1.1.1.105; 3474.
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 242285; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q7TQA3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q7TQA3; protein.
DR Bgee; ENSMUSG00000028236; Expressed in tail skin and 24 other tissues.
DR Genevisible; Q7TQA3; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISO:MGI.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; ISO:MGI.
DR GO; GO:0035067; P:negative regulation of histone acetylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0042574; P:retinal metabolic process; ISO:MGI.
DR GO; GO:0042572; P:retinol metabolic process; ISO:MGI.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; NAD; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..309
FT /note="Epidermal retinol dehydrogenase 2"
FT /id="PRO_0000305974"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 44..68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
SQ SEQUENCE 309 AA; 34193 MW; C5DE4B63AB35A665 CRC64;
MSQNLESVKN LLVFLGKSLL SVLEALLFHV ISKPRKNVAG EIVLITGAGS GLGRLLALQF
ARLGAVLVLW DVNKEANDET HQLAREAGAA RVHAYTCDCS RREEVYRVAD QVKKEVGDVS
ILINNAGIVT GRNFLDCPDD LMEKSFDVNF KAHLWMYKAF LPAMIANNHG HLVCISSSAG
LIGVNGLSDY CASKFAALGF AESMFIETLA KKQWGIKTTI VCPFFIKTGM FEGCTTKCPT
LLPILDPEYA VRKIIDAILQ EQLYLYMPKF LYFIVFLKSI LPIKTGILIA DYLGVFHMTE
GFTGQKKKT
