DRS7C_RAT
ID DRS7C_RAT Reviewed; 311 AA.
AC D3ZGP9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Dehydrogenase/reductase SDR family member 7C {ECO:0000303|PubMed:22143674};
DE EC=1.1.1.105 {ECO:0000250|UniProtKB:Q8CHS7};
DE AltName: Full=Sarcoplasmic reticulum protein of 35 kDa {ECO:0000250|UniProtKB:Q8CHS7};
DE Short=Protein SRP-35 {ECO:0000250|UniProtKB:Q8CHS7};
DE AltName: Full=Short-chain dehydrogenase/reductase family 32C member 2 {ECO:0000250|UniProtKB:Q8CHS7};
DE Short=Protein SDR32C2 {ECO:0000250|UniProtKB:A6NNS2};
DE Flags: Precursor;
GN Name=Dhrs7c {ECO:0000312|RGD:1306989};
GN Synonyms=Sdr32c2 {ECO:0000250|UniProtKB:A6NNS2};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND REPRESSION BY ADRENERGIC;
RP FORSKOLIN AND PHORBOL MYRISTATE ACETATE.
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).
CC -!- FUNCTION: NADH-dependent oxidoreductase which catalyzes the oxidation
CC of all-trans-retinol to all-trans-retinal. Plays a role in the
CC regulation of cardiac and skeletal muscle metabolic functions.
CC Maintains Ca(2+) intracellular homeostasis by repressing Ca(2+) release
CC from the sarcoplasmic reticulum (SR) in myotubes, possibly through
CC local alternations in NAD/NADH or retinol/retinal. Also plays a role in
CC Ca(2+) homeostasis by controlling Ca(2+) overload in the cytosol and
CC the SR in myotubes. Involved in glucose uptake into skeletal muscles
CC and 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.
CC {ECO:0000250|UniProtKB:Q8CHS7}.
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:0000250|UniProtKB:Q8CHS7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285;
CC Evidence={ECO:0000250|UniProtKB:Q8CHS7};
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8CHS7}. Note=The N-terminus region encompasses
CC a short hydrophobic sequence bound to the sarcoplasmic reticulum
CC membrane, whereas the C-terminus catalytic domain faces the myoplasm.
CC {ECO:0000250|UniProtKB:Q8CHS7}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, cardiac muscle and
CC skin. {ECO:0000269|PubMed:22143674}.
CC -!- DEVELOPMENTAL STAGE: Expression in cardiomyocytes is higher in adult as
CC compared with neonatal. {ECO:0000269|PubMed:22143674}.
CC -!- INDUCTION: Repressed by adrenergic agents (phenylephrine,
CC isoproterenol, dobutamine and clenbuterol), forskolin and phorbol
CC myristate acetate (at transcriptional levels) (PubMed:22143674). No
CC change in expression with endothelin-1 (PubMed:22143674).
CC {ECO:0000269|PubMed:22143674}.
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:0000250|UniProtKB:Q8CHS7}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000255|RuleBase:RU000363}.
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DR EMBL; AABR07029837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001258527.1; NM_001271598.1.
DR AlphaFoldDB; D3ZGP9; -.
DR SMR; D3ZGP9; -.
DR STRING; 10116.ENSRNOP00000031559; -.
DR PhosphoSitePlus; D3ZGP9; -.
DR PaxDb; D3ZGP9; -.
DR PeptideAtlas; D3ZGP9; -.
DR Ensembl; ENSRNOT00000036752; ENSRNOP00000031559; ENSRNOG00000026548.
DR GeneID; 287411; -.
DR CTD; 201140; -.
DR RGD; 1306989; Dhrs7c.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000157100; -.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; D3ZGP9; -.
DR OMA; ECYGYVD; -.
DR OrthoDB; 1313182at2759; -.
DR PhylomeDB; D3ZGP9; -.
DR TreeFam; TF313474; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000026548; Expressed in quadriceps femoris and 12 other tissues.
DR Genevisible; D3ZGP9; RN.
DR GO; GO:0014801; C:longitudinal sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0046323; P:glucose import; ISS:UniProtKB.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISS: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 2: Evidence at transcript 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 /evidence="ECO:0000255"
FT /id="PRO_0000454627"
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; 34366 MW; C14F432AEB951558 CRC64;
MGIMAVLMLP LLLLGVSGLL FIYQEASRLW SKSAVQNKVV VITDALSGLG KECARVFNAG
GARLVLCGKN WEGLESLYAA LTSVADPSKT FTPKLVLLDL SDISCVEDVA KEVLDCYGCV
DILINNASVK VKGPAHKISL ELDKKIMDAN YFGPITFTKV LLPNMISRRT GQIVLVNNIQ
AKFGIPFRTA YAASKHAVMG FFDCLRAEVE EYDVVVSTVS PTFIRSYQAY PEQRNWGSSI
CKFFCRKLTY GVHPVEVAEE VMRTVRRKKQ EVFMANPVPK AAVFIRTFFP ELFFAVVACG
VKEKLSVPEE G
