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   27-MAR-2024, entry version 170.
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; 4.
DR   STRING; 10090.ENSMUSP00000122552; -.
DR   iPTMnet; O88876; -.
DR   PhosphoSitePlus; O88876; -.
DR   SwissPalm; O88876; -.
DR   jPOST; O88876; -.
DR   MaxQB; O88876; -.
DR   PaxDb; 10090-ENSMUSP00000122552; -.
DR   ProteomicsDB; 279383; -. [O88876-1]
DR   ProteomicsDB; 279384; -. [O88876-2]
DR   Pumba; O88876; -.
DR   Antibodypedia; 2554; 216 antibodies from 26 providers.
DR   DNASU; 20148; -.
DR   Ensembl; ENSMUST00000105744.8; ENSMUSP00000101370.2; ENSMUSG00000066026.15. [O88876-2]
DR   Ensembl; ENSMUST00000154208.8; ENSMUSP00000122552.2; ENSMUSG00000066026.15. [O88876-1]
DR   GeneID; 20148; -.
DR   KEGG; mmu:20148; -.
DR   UCSC; uc008vrm.2; mouse. [O88876-2]
DR   UCSC; uc008vrn.2; mouse. [O88876-1]
DR   AGR; MGI:1315215; -.
DR   CTD; 9249; -.
DR   MGI; MGI:1315215; Dhrs3.
DR   VEuPathDB; HostDB:ENSMUSG00000066026; -.
DR   eggNOG; KOG1201; Eukaryota.
DR   GeneTree; ENSGT00940000158724; -.
DR   InParanoid; O88876; -.
DR   OMA; NWYAVLP; -.
DR   OrthoDB; 6845at2759; -.
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 80 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 269 other cell types or tissues.
DR   ExpressionAtlas; O88876; baseline and differential.
DR   GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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: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   CDD; cd05339; 17beta-HSDXI-like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR24322; PKSB; 1.
DR   PANTHER; PTHR24322:SF483; SHORT-CHAIN DEHYDROGENASE_REDUCTASE 3; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   Genevisible; O88876; MM.
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
//