DHRS3_MOUSE
ID DHRS3_MOUSE Reviewed; 302 AA.
AC O88876; Q3UAD1; Q91WR0; Q91XC3; Q922A6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Short-chain dehydrogenase/reductase 3;
DE EC=1.1.1.300 {ECO:0000250|UniProtKB:O75911};
DE AltName: Full=Retinal short-chain dehydrogenase/reductase 1;
DE Short=retSDR1;
GN Name=Dhrs3; Synonyms=Rsdr1;
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] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=9705317; DOI=10.1074/jbc.273.34.21790;
RA Haeseleer F., Huang J., Lebioda L., Saari J.C., Palczewski K.;
RT "Molecular characterization of a novel short-chain dehydrogenase/reductase
RT that reduces all-trans-retinal.";
RL J. Biol. Chem. 273:21790-21799(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Mesenchymal cell;
RX PubMed=9853961;
RX DOI=10.1002/(sici)1097-0177(199812)213:4<398::aid-aja5>3.0.co;2-t;
RA Baechner D., Ahrens M., Schroeder D., Hoffmann A., Lauber J., Betat N.,
RA Steinert P., Flohe L., Gross G.;
RT "Bmp-2 downstream targets in mesenchymal development identified by
RT subtractive cloning from recombinant mesenchymal progenitors (C3H10T1/2).";
RL Dev. Dyn. 213:398-411(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC TISSUE=Retina;
RA Haeseleer F., Palczewski K.;
RT "Structure of retinal short-chain dehydrogenase/reductase retSDR1 gene.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Mesonephros;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, Kidney, and Mammary gland;
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the reduction of all-trans-retinal to all-trans-
CC retinol in the presence of NADPH. {ECO:0000250|UniProtKB:O75911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.300; Evidence={ECO:0000250|UniProtKB:O75911};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88876-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88876-2; Sequence=VSP_050734, VSP_050735;
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in developing osteogenic
CC and chondrogenic tissues of vertebra, rib, tooth and limb bud.
CC {ECO:0000269|PubMed:9853961}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF061743; AAC63265.1; -; mRNA.
DR EMBL; X95281; CAA64602.1; -; mRNA.
DR EMBL; AF179241; AAD55403.1; -; Genomic_DNA.
DR EMBL; AF179238; AAD55403.1; JOINED; Genomic_DNA.
DR EMBL; AF179239; AAD55403.1; JOINED; Genomic_DNA.
DR EMBL; AF179240; AAD55403.1; JOINED; Genomic_DNA.
DR EMBL; AK032958; BAC28098.1; -; mRNA.
DR EMBL; AK151419; BAE30384.1; -; mRNA.
DR EMBL; BC008980; AAH08980.1; -; mRNA.
DR EMBL; BC010972; AAH10972.1; -; mRNA.
DR EMBL; BC013540; AAH13540.1; -; mRNA.
DR CCDS; CCDS18912.1; -. [O88876-1]
DR RefSeq; NP_035433.1; NM_011303.6. [O88876-1]
DR AlphaFoldDB; O88876; -.
DR SMR; O88876; -.
DR BioGRID; 203026; 3.
DR STRING; 10090.ENSMUSP00000122552; -.
DR iPTMnet; O88876; -.
DR PhosphoSitePlus; O88876; -.
DR jPOST; O88876; -.
DR MaxQB; O88876; -.
DR PaxDb; O88876; -.
DR PRIDE; O88876; -.
DR ProteomicsDB; 279383; -. [O88876-1]
DR ProteomicsDB; 279384; -. [O88876-2]
DR Antibodypedia; 2554; 203 antibodies from 26 providers.
DR DNASU; 20148; -.
DR Ensembl; ENSMUST00000105744; ENSMUSP00000101370; ENSMUSG00000066026. [O88876-2]
DR Ensembl; ENSMUST00000154208; ENSMUSP00000122552; ENSMUSG00000066026. [O88876-1]
DR GeneID; 20148; -.
DR KEGG; mmu:20148; -.
DR UCSC; uc008vrm.2; mouse. [O88876-2]
DR UCSC; uc008vrn.2; mouse. [O88876-1]
DR CTD; 9249; -.
DR MGI; MGI:1315215; Dhrs3.
DR VEuPathDB; HostDB:ENSMUSG00000066026; -.
DR eggNOG; KOG1201; Eukaryota.
DR GeneTree; ENSGT00940000158724; -.
DR InParanoid; O88876; -.
DR OMA; LCLRAQV; -.
DR OrthoDB; 1373099at2759; -.
DR PhylomeDB; O88876; -.
DR TreeFam; TF312837; -.
DR BRENDA; 1.1.1.300; 3474.
DR Reactome; R-MMU-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR BioGRID-ORCS; 20148; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Dhrs3; mouse.
DR PRO; PR:O88876; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O88876; protein.
DR Bgee; ENSMUSG00000066026; Expressed in vestibular membrane of cochlear duct and 266 other tissues.
DR ExpressionAtlas; O88876; baseline and differential.
DR Genevisible; O88876; MM.
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:0004745; F:NAD-retinol dehydrogenase activity; IMP:MGI.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC.
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:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0060411; P:cardiac septum morphogenesis; IMP:MGI.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IMP:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0030278; P:regulation of ossification; IMP:MGI.
DR GO; GO:0048385; P:regulation of retinoic acid receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001523; P:retinoid metabolic process; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR InterPro; IPR032969; DHRS3.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24322:SF483; PTHR24322:SF483; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..302
FT /note="Short-chain dehydrogenase/reductase 3"
FT /id="PRO_0000054645"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050734"
FT VAR_SEQ 114..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050735"
FT CONFLICT 68
FT /note="L -> F (in Ref. 5; AAH10972)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="F -> L (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 33652 MW; E530F36877C3C610 CRC64;
MVWKWLGALV VFPLQMIYLV TKAAVGMVLP PKLRDLSRES VLITGGGRGI GRHLAREFAE
RGARKIVLWG RTEKCLKETT EEIRQMGTEC HYFICDVGNR EEVYQMAKAV REKVGDITIL
VNNAAVVHGK SLMDSDDDAL LKSQHVNTLG QFWTTKAFLP RMLELQNGHI VCLNSVLALS
AIPGAIDYCT SKASAFAFME SLTLGLLDCP GVSATTVLPF HTSTEMFQGM RVRFPNLFPP
LKPETVARRT VDAVQQNQAL LLLPWTMNIL IILKSILPQA ALEEIHRFSG TYTCMNTFKG
RT
