DHRS1_MOUSE
ID DHRS1_MOUSE Reviewed; 313 AA.
AC Q99L04; Q3THW0; Q9D148;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Dehydrogenase/reductase SDR family member 1 {ECO:0000250|UniProtKB:Q96LJ7};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q96LJ7};
DE AltName: Full=Short chain dehydrogenase/reductase family 19C member 1 {ECO:0000250|UniProtKB:Q96LJ7};
DE Short=Protein SDR19C1 {ECO:0000250|UniProtKB:Q96LJ7};
GN Name=Dhrs1 {ECO:0000312|MGI:MGI:1196314}; Synonyms=D14ertd484e;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-21, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: NADPH-dependent oxidoreductase which catalyzes the reduction
CC of some steroids (estrone, androstene-3,17-dione and cortisone) as well
CC as prostaglandin E1, isatin and xenobiotics in vitro. May have a role
CC in steroid and/or xenobiotic metabolism.
CC {ECO:0000250|UniProtKB:Q96LJ7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC Xref=Rhea:RHEA:16705, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q96LJ7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16707;
CC Evidence={ECO:0000250|UniProtKB:Q96LJ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC NADPH; Xref=Rhea:RHEA:14981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q96LJ7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14983;
CC Evidence={ECO:0000250|UniProtKB:Q96LJ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + prostaglandin E1 = NADP(+) + prostaglandin F1;
CC Xref=Rhea:RHEA:68612, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:178049;
CC Evidence={ECO:0000250|UniProtKB:Q96LJ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68613;
CC Evidence={ECO:0000250|UniProtKB:Q96LJ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + isatin + NADPH = 3-hydroxyindolin-2-one + NADP(+);
CC Xref=Rhea:RHEA:68608, ChEBI:CHEBI:15378, ChEBI:CHEBI:27539,
CC ChEBI:CHEBI:28536, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q96LJ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68609;
CC Evidence={ECO:0000250|UniProtKB:Q96LJ7};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q96LJ7}. Note=May be attached to the ER membrane
CC by its C-terminus segment. {ECO:0000250|UniProtKB:Q96LJ7}.
CC -!- DOMAIN: May be attached to the ER membrane by its C-terminus segment.
CC {ECO:0000250|UniProtKB:Q96LJ7}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AK003958; BAB23093.1; -; mRNA.
DR EMBL; AK146317; BAE27072.1; -; mRNA.
DR EMBL; AK168115; BAE40086.1; -; mRNA.
DR EMBL; AK168147; BAE40112.1; -; mRNA.
DR EMBL; BC003930; AAH03930.1; -; mRNA.
DR CCDS; CCDS36934.1; -.
DR RefSeq; NP_081095.2; NM_026819.3.
DR AlphaFoldDB; Q99L04; -.
DR SMR; Q99L04; -.
DR BioGRID; 206675; 5.
DR STRING; 10090.ENSMUSP00000002403; -.
DR iPTMnet; Q99L04; -.
DR PhosphoSitePlus; Q99L04; -.
DR SwissPalm; Q99L04; -.
DR EPD; Q99L04; -.
DR jPOST; Q99L04; -.
DR MaxQB; Q99L04; -.
DR PaxDb; Q99L04; -.
DR PeptideAtlas; Q99L04; -.
DR PRIDE; Q99L04; -.
DR ProteomicsDB; 277450; -.
DR Antibodypedia; 23; 157 antibodies from 27 providers.
DR DNASU; 52585; -.
DR Ensembl; ENSMUST00000002403; ENSMUSP00000002403; ENSMUSG00000002332.
DR GeneID; 52585; -.
DR KEGG; mmu:52585; -.
DR UCSC; uc007uan.2; mouse.
DR CTD; 115817; -.
DR MGI; MGI:1196314; Dhrs1.
DR VEuPathDB; HostDB:ENSMUSG00000002332; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000157797; -.
DR HOGENOM; CLU_010194_14_1_1; -.
DR InParanoid; Q99L04; -.
DR OMA; PADVTGY; -.
DR OrthoDB; 1513822at2759; -.
DR PhylomeDB; Q99L04; -.
DR TreeFam; TF314146; -.
DR BioGRID-ORCS; 52585; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Dhrs1; mouse.
DR PRO; PR:Q99L04; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q99L04; protein.
DR Bgee; ENSMUSG00000002332; Expressed in ciliary body and 255 other tissues.
DR Genevisible; Q99L04; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISS:UniProtKB.
DR GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IEA:RHEA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Methylation; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..313
FT /note="Dehydrogenase/reductase SDR family member 1"
FT /id="PRO_0000054641"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT MOD_RES 21
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 194
FT /note="G -> R (in Ref. 1; BAB23093)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="W -> L (in Ref. 1; BAB23093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 34005 MW; 60E05BD7911BDC0C CRC64;
MVAPMKGQVC VVTGASRGIG RGIALQLCKA GATVYITGRH LDTLRATAQE AQSLGGRCVP
VVCDSSQESE VKSLFEQVDR EQKGRLDVLV NNAYAGVQAI LNTTNKSFWE VPASIWDDIN
NVGLRGHYLC SVYGARLMVP AGKGLIVIVS SPGGLQHMFN VPYGVGKAAC DRLAADCAHE
LRRHGVSYVS LWPGLVQTEM VKEFMAKEDT PEDPLFKKMK PDFSSAESPE MSGKCVVALA
TDPNILNLSG KVLPSCDLAR RYGLKDIDGR PVKDYFSLGY ALSQVSSLGW LNSFLPGFLR
VPKWVVTLYN SKF
