DRS7C_MOUSE
ID DRS7C_MOUSE Reviewed; 311 AA.
AC Q8CHS7; B1ATJ2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Dehydrogenase/reductase SDR family member 7C {ECO:0000303|PubMed:29330505};
DE EC=1.1.1.105 {ECO:0000269|PubMed:21995425};
DE AltName: Full=Sarcoplasmic reticulum protein of 35 kDa {ECO:0000303|PubMed:21995425};
DE Short=Protein SRP-35 {ECO:0000303|PubMed:21995425};
DE AltName: Full=Short-chain dehydrogenase/reductase family 32C member 2 {ECO:0000250|UniProtKB:A6NNS2};
DE Short=Protein SDR32C2 {ECO:0000250|UniProtKB:A6NNS2};
DE Flags: Precursor;
GN Name=Dhrs7c {ECO:0000312|MGI:MGI:1915710};
GN Synonyms=Sdr32c2 {ECO:0000250|UniProtKB:A6NNS2},
GN Srp-35 {ECO:0000303|PubMed:21995425};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-112.
RA Marra M., Hillier L., Allen M., Bowles M., Dietrich N., Dubuque T.,
RA Geisel S., Kucaba T., Lacy M., Le M., Martin J., Morris M.,
RA Schellenberg K., Steptoe M., Tan F., Underwood K., Moore B., Theising B.,
RA Wylie T., Lennon G., Soares B., Wilson R., Waterston R.;
RT "The WashU-HHMI Mouse EST Project.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION BY RETINOIC ACID, AND DOMAIN.
RX PubMed=21995425; DOI=10.1042/bj20111457;
RA Treves S., Thurnheer R., Mosca B., Vukcevic M., Bergamelli L., Voltan R.,
RA Oberhauser V., Ronjat M., Csernoch L., Szentesi P., Zorzato F.;
RT "SRP-35, a newly identified protein of the skeletal muscle sarcoplasmic
RT reticulum, is a retinol dehydrogenase.";
RL Biochem. J. 441:731-741(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22143674; DOI=10.1093/eurjhf/hfr152;
RA Lu B., Tigchelaar W., Ruifrok W.P., van Gilst W.H., de Boer R.A.,
RA Sillje H.H.;
RT "DHRS7c, a novel cardiomyocyte-expressed gene that is down-regulated by
RT adrenergic stimulation and in heart failure.";
RL Eur. J. Heart Fail. 14:5-13(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF TYR-191 AND LYS-195.
RX PubMed=27806939; DOI=10.1152/ajpcell.00090.2016;
RA Arai S., Ikeda M., Ide T., Matsuo Y., Fujino T., Hirano K., Sunagawa K.,
RA Tsutsui H.;
RT "Functional loss of DHRS7C induces intracellular Ca2+ overload and myotube
RT enlargement in C2C12 cells via calpain activation.";
RL Am. J. Physiol. 312:C29-C39(2017).
RN [7]
RP FUNCTION.
RX PubMed=29330505; DOI=10.1038/s41598-017-18844-3;
RA Ruiz A., Dror E., Handschin C., Furrer R., Perez-Schindler J., Bachmann C.,
RA Treves S., Zorzato F.;
RT "Over-expression of a retinol dehydrogenase (SRP35/DHRS7C) in skeletal
RT muscle activates mTORC2, enhances glucose metabolism and muscle
RT performance.";
RL Sci. Rep. 8:636-636(2018).
CC -!- FUNCTION: NADH-dependent oxidoreductase which catalyzes the oxidation
CC of all-trans-retinol to all-trans-retinal (PubMed:21995425). Plays a
CC role in the regulation of cardiac and skeletal muscle metabolic
CC functions (PubMed:21995425, PubMed:27806939, PubMed:29330505)
CC (Probable). Maintains Ca(2+) intracellular homeostasis by repressing
CC Ca(2+) release from the sarcoplasmic reticulum (SR) in myotubes,
CC possibly through local alternations in NAD/NADH or retinol/retinal
CC (PubMed:21995425). Also plays a role in Ca(2+) homeostasis by
CC controlling Ca(2+) overload in the cytosol and the SR in myotubes
CC (PubMed:27806939). Involved in glucose uptake into skeletal muscles and
CC muscle performance by activating PI3K and mTORC2-mediated AKT1
CC phosphorylation signaling pathways, possibly through the action of its
CC downstream catalytic product all-trans-retinoic acid (PubMed:29330505).
CC {ECO:0000269|PubMed:21995425, ECO:0000269|PubMed:27806939,
CC ECO:0000269|PubMed:29330505, ECO:0000305|PubMed:22143674}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.105; Evidence={ECO:0000269|PubMed:21995425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285;
CC Evidence={ECO:0000305|PubMed:21995425};
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC {ECO:0000305|PubMed:21995425, ECO:0000305|PubMed:22143674,
CC ECO:0000305|PubMed:27806939}. Note=The N-terminus region encompasses a
CC short hydrophobic sequence bound to the sarcoplasmic reticulum
CC membrane, whereas the C-terminus catalytic domain faces the myoplasm.
CC In skeletal muscle, enriched in the longitudinal sarcoplasmic reticulum
CC (PubMed:21995425). {ECO:0000269|PubMed:21995425,
CC ECO:0000305|PubMed:21995425}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle and cardiac muscle
CC (PubMed:21995425, PubMed:22143674, PubMed:27806939). Also expressed in
CC liver, kidney, adipocytes and skin (PubMed:21995425, PubMed:22143674).
CC {ECO:0000269|PubMed:21995425, ECO:0000269|PubMed:22143674,
CC ECO:0000269|PubMed:27806939}.
CC -!- DEVELOPMENTAL STAGE: In skeletal muscle, expressed in differentiated
CC myotubes but not in undifferentiated myoblasts.
CC {ECO:0000269|PubMed:27806939}.
CC -!- INDUCTION: Induced by all-trans-retinoic acid (at transcriptional
CC level). {ECO:0000269|PubMed:21995425}.
CC -!- DOMAIN: The N-terminus region encompasses a short hydrophobic sequence
CC bound to the sarcoplasmic reticulum membrane, whereas the C-terminus
CC catalytic domain faces the myoplasm. {ECO:0000305|PubMed:21995425}.
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; AL646097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AA063835; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS48822.1; -.
DR RefSeq; NP_001013031.2; NM_001013013.2.
DR AlphaFoldDB; Q8CHS7; -.
DR SMR; Q8CHS7; -.
DR STRING; 10090.ENSMUSP00000130924; -.
DR iPTMnet; Q8CHS7; -.
DR PhosphoSitePlus; Q8CHS7; -.
DR MaxQB; Q8CHS7; -.
DR PaxDb; Q8CHS7; -.
DR PRIDE; Q8CHS7; -.
DR ProteomicsDB; 279581; -.
DR Antibodypedia; 6297; 103 antibodies from 16 providers.
DR DNASU; 68460; -.
DR Ensembl; ENSMUST00000168612; ENSMUSP00000130924; ENSMUSG00000033044.
DR GeneID; 68460; -.
DR KEGG; mmu:68460; -.
DR UCSC; uc011xwp.1; mouse.
DR CTD; 201140; -.
DR MGI; MGI:1915710; Dhrs7c.
DR VEuPathDB; HostDB:ENSMUSG00000033044; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000157100; -.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; Q8CHS7; -.
DR OMA; ECYGYVD; -.
DR OrthoDB; 1313182at2759; -.
DR PhylomeDB; Q8CHS7; -.
DR TreeFam; TF313474; -.
DR BioGRID-ORCS; 68460; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Dhrs7c; mouse.
DR PRO; PR:Q8CHS7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CHS7; protein.
DR Bgee; ENSMUSG00000033044; Expressed in temporalis muscle and 67 other tissues.
DR Genevisible; Q8CHS7; MM.
DR GO; GO:0014801; C:longitudinal sarcoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:UniProtKB.
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:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
DR GO; GO:0046323; P:glucose import; IDA:UniProtKB.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
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 1: Evidence at protein level;
KW Membrane; NAD; NADP; Oxidoreductase; Reference proteome;
KW Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..311
FT /note="Dehydrogenase/reductase SDR family member 7C"
FT /id="PRO_0000333756"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
SQ SEQUENCE 311 AA; 34468 MW; E223E8C363153E5F CRC64;
MGLMAVLMLP LLLLGISGLL FIYQEASRLW SKSAVQNKVV VITDAISGLG KECARVFHAG
GARLVLCGKN WEGLESLYAT LTSVADPSKT FTPKLVLLDL SDISCVQDVA KEVLDCYGCV
DILINNASVK VKGPAHKISL ELDKKIMDAN YFGPITLTKV LLPNMISRRT GQIVLVNNIQ
AKFGIPFRTA YAASKHAVMG FFDCLRAEVE EYDVVVSTVS PTFIRSYRAS PEQRNWETSI
CKFFCRKLAY GVHPVEVAEE VMRTVRRKKQ EVFMANPVPK AAVFIRTFFP EFFFAVVACG
VKEKLNVPEE G
