DRS7C_HUMAN
ID DRS7C_HUMAN Reviewed; 312 AA.
AC A6NNS2; B7ZW74; B9EJH3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Dehydrogenase/reductase SDR family member 7C {ECO:0000250|UniProtKB:Q8CHS7};
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:0000303|PubMed:19027726};
DE Short=Protein SDR32C2 {ECO:0000303|PubMed:19027726};
DE Flags: Precursor;
GN Name=DHRS7C {ECO:0000312|HGNC:HGNC:32423};
GN Synonyms=SDR32C2 {ECO:0000303|PubMed:19027726};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA Adamski J., Oppermann U.;
RT "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT nomenclature initiative.";
RL Chem. Biol. Interact. 178:94-98(2009).
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 In skeletal muscle, enriched in the longitudinal sarcoplasmic
CC reticulum. {ECO:0000250|UniProtKB:Q8CHS7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6NNS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NNS2-2; Sequence=VSP_054852;
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:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI47025.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI47026.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AC027045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147024; AAI47025.1; ALT_INIT; mRNA.
DR EMBL; BC147025; AAI47026.1; ALT_INIT; mRNA.
DR EMBL; BC171909; AAI71909.1; -; mRNA.
DR CCDS; CCDS56020.1; -. [A6NNS2-1]
DR CCDS; CCDS58517.1; -. [A6NNS2-2]
DR RefSeq; NP_001099041.1; NM_001105571.2. [A6NNS2-2]
DR RefSeq; NP_001207422.1; NM_001220493.1. [A6NNS2-1]
DR AlphaFoldDB; A6NNS2; -.
DR SMR; A6NNS2; -.
DR BioGRID; 128363; 1.
DR STRING; 9606.ENSP00000327975; -.
DR iPTMnet; A6NNS2; -.
DR PhosphoSitePlus; A6NNS2; -.
DR BioMuta; DHRS7C; -.
DR MassIVE; A6NNS2; -.
DR PaxDb; A6NNS2; -.
DR PeptideAtlas; A6NNS2; -.
DR PRIDE; A6NNS2; -.
DR ProteomicsDB; 1633; -. [A6NNS2-1]
DR Antibodypedia; 6297; 103 antibodies from 16 providers.
DR DNASU; 201140; -.
DR Ensembl; ENST00000330255.9; ENSP00000327975.4; ENSG00000184544.12. [A6NNS2-1]
DR Ensembl; ENST00000571134.2; ENSP00000459579.1; ENSG00000184544.12. [A6NNS2-2]
DR GeneID; 201140; -.
DR KEGG; hsa:201140; -.
DR MANE-Select; ENST00000571134.2; ENSP00000459579.1; NM_001105571.3; NP_001099041.1. [A6NNS2-2]
DR UCSC; uc010cof.4; human. [A6NNS2-1]
DR CTD; 201140; -.
DR DisGeNET; 201140; -.
DR GeneCards; DHRS7C; -.
DR HGNC; HGNC:32423; DHRS7C.
DR HPA; ENSG00000184544; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 616161; gene.
DR neXtProt; NX_A6NNS2; -.
DR OpenTargets; ENSG00000184544; -.
DR VEuPathDB; HostDB:ENSG00000184544; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000157100; -.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; A6NNS2; -.
DR OMA; ECYGYVD; -.
DR OrthoDB; 1313182at2759; -.
DR PhylomeDB; A6NNS2; -.
DR TreeFam; TF313474; -.
DR PathwayCommons; A6NNS2; -.
DR BioGRID-ORCS; 201140; 10 hits in 1055 CRISPR screens.
DR GenomeRNAi; 201140; -.
DR Pharos; A6NNS2; Tdark.
DR PRO; PR:A6NNS2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; A6NNS2; protein.
DR Bgee; ENSG00000184544; Expressed in vastus lateralis and 101 other tissues.
DR ExpressionAtlas; A6NNS2; baseline and differential.
DR Genevisible; A6NNS2; HS.
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 Alternative splicing; Membrane; NAD; NADP; Oxidoreductase;
KW Reference proteome; Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..312
FT /note="Dehydrogenase/reductase SDR family member 7C"
FT /id="PRO_0000333755"
FT ACT_SITE 192
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 192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT VAR_SEQ 90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054852"
FT VARIANT 227
FT /note="S -> L (in dbSNP:rs2280490)"
FT /id="VAR_043150"
SQ SEQUENCE 312 AA; 34878 MW; ADCE06D480B40E00 CRC64;
MGVMAMLMLP LLLLGISGLL FIYQEVSRLW SKSAVQNKVV VITDAISGLG KECARVFHTG
GARLVLCGKN WERLENLYDA LISVADPSKQ TFTPKLVLLD LSDISCVPDV AKEVLDCYGC
VDILINNASV KVKGPAHKIS LELDKKIMDA NYFGPITLTK ALLPNMISRR TGQIVLVNNI
QGKFGIPFRT TYAASKHAAL GFFDCLRAEV EEYDVVISTV SPTFIRSYHV YPEQGNWEAS
IWKFFFRKLT YGVHPVEVAE EVMRTVRRKK QEVFMANPIP KAAVYVRTFF PEFFFAVVAC
GVKEKLNVPE EG
