DR9C7_MOUSE
ID DR9C7_MOUSE Reviewed; 313 AA.
AC Q8K3P0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Short-chain dehydrogenase/reductase family 9C member 7;
DE EC=1.1.1.-;
DE AltName: Full=Orphan short-chain dehydrogenase/reductase;
DE Short=SDR-O;
DE AltName: Full=RDH-S;
GN Name=Sdr9c7; Synonyms=Rdhs, Sdro;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=12234675; DOI=10.1016/s0378-1119(02)00757-6;
RA Chen W., Song M.-S., Napoli J.L.;
RT "SDR-O: an orphan short-chain dehydrogenase/reductase localized at mouse
RT chromosome 10/human chromosome 12.";
RL Gene 294:141-146(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 MRNA].
RC TISSUE=Jaw, and Limb;
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: Displays weak conversion of all-trans-retinal to all-trans-
CC retinol in the presence of NADH. Has apparently no steroid
CC dehydrogenase activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:12234675}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver.
CC {ECO:0000269|PubMed:12234675}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY044433; AAK95855.1; -; mRNA.
DR EMBL; AK037184; BAC29742.1; -; mRNA.
DR EMBL; BC064820; AAH64820.1; -; mRNA.
DR CCDS; CCDS24256.1; -.
DR RefSeq; NP_081577.1; NM_027301.3.
DR AlphaFoldDB; Q8K3P0; -.
DR SMR; Q8K3P0; -.
DR STRING; 10090.ENSMUSP00000036628; -.
DR iPTMnet; Q8K3P0; -.
DR PhosphoSitePlus; Q8K3P0; -.
DR MaxQB; Q8K3P0; -.
DR PaxDb; Q8K3P0; -.
DR PRIDE; Q8K3P0; -.
DR ProteomicsDB; 277393; -.
DR Antibodypedia; 43915; 229 antibodies from 16 providers.
DR DNASU; 70061; -.
DR Ensembl; ENSMUST00000047134; ENSMUSP00000036628; ENSMUSG00000040127.
DR GeneID; 70061; -.
DR KEGG; mmu:70061; -.
DR UCSC; uc007hkw.1; mouse.
DR CTD; 121214; -.
DR MGI; MGI:1917311; Sdr9c7.
DR VEuPathDB; HostDB:ENSMUSG00000040127; -.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000161764; -.
DR HOGENOM; CLU_010194_2_0_1; -.
DR InParanoid; Q8K3P0; -.
DR OMA; IRRELHF; -.
DR OrthoDB; 942985at2759; -.
DR PhylomeDB; Q8K3P0; -.
DR TreeFam; TF325617; -.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR BioGRID-ORCS; 70061; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8K3P0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8K3P0; protein.
DR Bgee; ENSMUSG00000040127; Expressed in tail skin and 33 other tissues.
DR Genevisible; Q8K3P0; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR032968; SDR_9C7.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43313:SF5; PTHR43313:SF5; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..313
FT /note="Short-chain dehydrogenase/reductase family 9C member
FT 7"
FT /id="PRO_0000316886"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 29..53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEX9"
SQ SEQUENCE 313 AA; 35149 MW; 8C93F6A4448911E6 CRC64;
MAALTDFAFM YRWFKNCNLV KNLSEKYVFI TGCDSGFGNL LAKQLVDRGM KVLAACLTEE
GAQKLLQDTS HQLQTFLLDV TKSENVKEAA QWVRDQVGEQ GLWALVNNAG VGLPSGPNEW
LTIKDFVKVI NINLVGLIDV TLNMLPMIKK ARGRVVNMSS SGGRVAIFGG GYCVSKFGVE
AFSDSIRREL HFFGVKVSII EPGNYKTSIL GQEALESRMK KLWDRLPQET RDSYGEEYFQ
TYTKKLVNLM RSAEPRISDV TNSMEHAIVS RSPRIRYNPG LDVKFLYLTL AKLPTPVTDF
ILSRYLPRPA DSV
