DRS7C_BOVIN
ID DRS7C_BOVIN Reviewed; 311 AA.
AC Q1RMJ5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 104.
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:0000250|UniProtKB:A6NNS2};
DE Short=Protein SDR32C2 {ECO:0000250|UniProtKB:A6NNS2};
DE Flags: Precursor;
GN Name=DHRS7C; Synonyms=SDR32C2 {ECO:0000250|UniProtKB:A6NNS2};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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=Q1RMJ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1RMJ5-2; Sequence=VSP_033520;
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}.
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DR EMBL; AAFC03081251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC114860; AAI14861.1; -; mRNA.
DR RefSeq; NP_001069013.1; NM_001075545.1. [Q1RMJ5-2]
DR RefSeq; XP_005220401.1; XM_005220344.3. [Q1RMJ5-1]
DR AlphaFoldDB; Q1RMJ5; -.
DR SMR; Q1RMJ5; -.
DR STRING; 9913.ENSBTAP00000006658; -.
DR PaxDb; Q1RMJ5; -.
DR PRIDE; Q1RMJ5; -.
DR Ensembl; ENSBTAT00000006658; ENSBTAP00000006658; ENSBTAG00000005048. [Q1RMJ5-1]
DR Ensembl; ENSBTAT00000044540; ENSBTAP00000042030; ENSBTAG00000005048. [Q1RMJ5-2]
DR GeneID; 511943; -.
DR KEGG; bta:511943; -.
DR CTD; 201140; -.
DR VEuPathDB; HostDB:ENSBTAG00000005048; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000157100; -.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; Q1RMJ5; -.
DR OMA; ECYGYVD; -.
DR OrthoDB; 1313182at2759; -.
DR TreeFam; TF313474; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000005048; Expressed in biceps femoris and 51 other tissues.
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..311
FT /note="Dehydrogenase/reductase SDR family member 7C"
FT /id="PRO_0000333754"
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"
FT VAR_SEQ 191..242
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033520"
SQ SEQUENCE 311 AA; 34422 MW; 53A8452AAF6AD152 CRC64;
MGVTAVLMLP LLLLGISGLL FIYQEVSRLW SKSVVQNKVV VITDAISGLG KECARVFHTG
GARLVLCGKN WERLQSLYDA LISVADPSKT FTPKLVLLDL SDISCVQDVA KEVLDCYGCV
DILINNASVK VKGPAHKISL ELDKKIMDAN YFGPIILTKA LLPDMISRRT GQIVLVNNIQ
GKLGIPFRTA YAASKHAALG FFDCLRAEVE EYDVVVSTVS PTFIRSYHVD PGQGNWEASI
WKFFFRKLTY GTHPVDVAEE VMRTVRRKKQ EVFLANPIPK AAVYIRTLFP ELFFAVVACG
VKEKLSVPEE G
