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   27-MAR-2024, entry version 127.
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.
DR   AlphaFoldDB; Q5RJY4; -.
DR   SMR; Q5RJY4; -.
DR   BioGRID; 252129; 1.
DR   IntAct; Q5RJY4; 3.
DR   MINT; Q5RJY4; -.
DR   STRING; 10116.ENSRNOP00000063346; -.
DR   PhosphoSitePlus; Q5RJY4; -.
DR   jPOST; Q5RJY4; -.
DR   PaxDb; 10116-ENSRNOP00000063744; -.
DR   Ensembl; ENSRNOT00000066250.4; ENSRNOP00000063346.3; ENSRNOG00000005360.9. [Q5RJY4-1]
DR   Ensembl; ENSRNOT00055044041; ENSRNOP00055036023; ENSRNOG00055025492. [Q5RJY4-1]
DR   Ensembl; ENSRNOT00060053080; ENSRNOP00060044129; ENSRNOG00060030543. [Q5RJY4-1]
DR   Ensembl; ENSRNOT00065013068; ENSRNOP00065009649; ENSRNOG00065008238. [Q5RJY4-1]
DR   GeneID; 287380; -.
DR   KEGG; rno:287380; -.
DR   UCSC; RGD:1311243; rat. [Q5RJY4-1]
DR   AGR; RGD:1311243; -.
DR   CTD; 25979; -.
DR   RGD; 1311243; Dhrs7b.
DR   eggNOG; KOG1205; Eukaryota.
DR   GeneTree; ENSGT00940000158171; -.
DR   InParanoid; Q5RJY4; -.
DR   OrthoDB; 7812at2759; -.
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 cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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: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:0006355; P:regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   CDD; cd05332; 11beta-HSD1_like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR44196; DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR   PANTHER; PTHR44196:SF1; DEHYDROGENASE_REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PIRSF; PIRSF000126; 11-beta-HSD1; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
DR   Genevisible; Q5RJY4; RN.
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
//