DRS7B_RAT
ID DRS7B_RAT Reviewed; 325 AA.
AC Q5RJY4; A4GWE3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dehydrogenase/reductase SDR family member 7B {ECO:0000250|UniProtKB:Q6IAN0};
DE EC=1.1.-.- {ECO:0000305};
DE AltName: Full=Short-chain dehydrogenase/reductase family 32C member 1 {ECO:0000250|UniProtKB:Q6IAN0};
DE Short=Protein SDR32C1 {ECO:0000250|UniProtKB:Q6IAN0};
GN Name=Dhrs7b; Synonyms=Sdr32c1 {ECO:0000250|UniProtKB:Q6IAN0};
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 [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=17522052; DOI=10.1074/jbc.m610910200;
RA Islinger M., Lueers G.H., Li K.W., Loos M., Voelkl A.;
RT "Rat liver peroxisomes after fibrate treatment: a survey using quantitative
RT mass spectrometry.";
RL J. Biol. Chem. 282:23055-23069(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 SUBCELLULAR LOCATION.
RX PubMed=18775470; DOI=10.1016/j.mce.2008.07.022;
RA Keller B., Meier M., Adamski J.;
RT "Comparison of predicted and experimental subcellular localization of two
RT putative rat steroid dehydrogenases from the short-chain
RT dehydrogenase/reductase protein superfamily.";
RL Mol. Cell. Endocrinol. 301:43-46(2009).
CC -!- FUNCTION: Putative oxidoreductase. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17522052, ECO:0000269|PubMed:18775470}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:17522052,
CC ECO:0000269|PubMed:18775470}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Dhrs7b.1;
CC IsoId=Q5RJY4-1; Sequence=Displayed;
CC Name=2; Synonyms=Dhrs7b.2;
CC IsoId=Q5RJY4-2; Sequence=VSP_029700;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; EF445633; ABO31120.1; -; mRNA.
DR EMBL; BC086453; AAH86453.1; -; mRNA.
DR RefSeq; NP_001008507.1; NM_001008507.1. [Q5RJY4-1]
DR RefSeq; XP_006246534.1; XM_006246472.3. [Q5RJY4-2]
DR RefSeq; XP_006246535.1; XM_006246473.3. [Q5RJY4-2]
DR RefSeq; XP_006246536.1; XM_006246474.3. [Q5RJY4-2]
DR AlphaFoldDB; Q5RJY4; -.
DR SMR; Q5RJY4; -.
DR BioGRID; 252129; 1.
DR IntAct; Q5RJY4; 3.
DR MINT; Q5RJY4; -.
DR STRING; 10116.ENSRNOP00000063744; -.
DR jPOST; Q5RJY4; -.
DR PaxDb; Q5RJY4; -.
DR PRIDE; Q5RJY4; -.
DR Ensembl; ENSRNOT00000066250; ENSRNOP00000063346; ENSRNOG00000005360. [Q5RJY4-1]
DR GeneID; 287380; -.
DR KEGG; rno:287380; -.
DR UCSC; RGD:1311243; rat. [Q5RJY4-1]
DR CTD; 25979; -.
DR RGD; 1311243; Dhrs7b.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000158171; -.
DR InParanoid; Q5RJY4; -.
DR OMA; YFWIMAK; -.
DR OrthoDB; 1313182at2759; -.
DR PhylomeDB; Q5RJY4; -.
DR TreeFam; TF313474; -.
DR Reactome; R-RNO-75896; Plasmalogen biosynthesis.
DR PRO; PR:Q5RJY4; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000005360; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q5RJY4; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0060612; P:adipose tissue development; ISO:RGD.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0008611; P:ether lipid biosynthetic process; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0030223; P:neutrophil differentiation; ISO:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:RGD.
DR GO; GO:0120161; P:regulation of cold-induced thermogenesis; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
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 Alternative splicing; Endoplasmic reticulum; Membrane; NAD; NADP;
KW Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..325
FT /note="Dehydrogenase/reductase SDR family member 7B"
FT /id="PRO_0000312108"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..325
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 62
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 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17522052"
FT /id="VSP_029700"
SQ SEQUENCE 325 AA; 35342 MW; AFC1DEA2610F2D2D CRC64;
MISPSSRKGM LKERAMDLVT QTTILPLLFG CLGIFSLFRL LQRTRSKAYL RNAVVVVTGA
TSGLGKECAR VFHAAGAKVV LCGRNVKALE EFTRELADSS SSQGQTHQPC VVTFDLADPG
AIAPAAAEIL QCFGYVDILI NNAGISYRGA ISDTIVDVDR KVMEINYFGP VALTKALLPS
MVERKRGHIV AISSIQGKIS IPFRSAYAAS KHATQAFFDC LRAEMKDSDI EVTVISPGYI
HTNLSVNAVT ADGSRYGALD KNTAQGRSAV EVAQDIFDAV GKKKKDVLLT DFLPTMAVYI
RTLAPRLFFR IMASRARKER KSKNS
