DRS7B_MOUSE
ID DRS7B_MOUSE Reviewed; 323 AA.
AC Q99J47; Q3UNS3; Q5NCT5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
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 {ECO:0000312|MGI:MGI:2384931};
GN Synonyms=Sdr32c1 {ECO:0000250|UniProtKB:Q6IAN0};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryonic heart, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Putative oxidoreductase. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5RJY4}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q5RJY4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99J47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99J47-2; Sequence=VSP_029698;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI35261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK052209; BAC34887.1; -; mRNA.
DR EMBL; AK139084; BAE23884.1; -; mRNA.
DR EMBL; AK144057; BAE25674.1; -; mRNA.
DR EMBL; AL596215; CAI35261.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC003479; AAH03479.1; -; mRNA.
DR CCDS; CCDS24800.1; -. [Q99J47-1]
DR RefSeq; NP_001165583.1; NM_001172112.1. [Q99J47-2]
DR RefSeq; NP_663403.1; NM_145428.2. [Q99J47-1]
DR AlphaFoldDB; Q99J47; -.
DR SMR; Q99J47; -.
DR BioGRID; 229794; 8.
DR STRING; 10090.ENSMUSP00000044924; -.
DR iPTMnet; Q99J47; -.
DR PhosphoSitePlus; Q99J47; -.
DR SwissPalm; Q99J47; -.
DR EPD; Q99J47; -.
DR jPOST; Q99J47; -.
DR MaxQB; Q99J47; -.
DR PaxDb; Q99J47; -.
DR PRIDE; Q99J47; -.
DR ProteomicsDB; 277500; -. [Q99J47-1]
DR ProteomicsDB; 277501; -. [Q99J47-2]
DR Antibodypedia; 2324; 138 antibodies from 18 providers.
DR DNASU; 216820; -.
DR Ensembl; ENSMUST00000042281; ENSMUSP00000044924; ENSMUSG00000042569. [Q99J47-1]
DR GeneID; 216820; -.
DR KEGG; mmu:216820; -.
DR UCSC; uc007jgq.2; mouse. [Q99J47-1]
DR CTD; 25979; -.
DR MGI; MGI:2384931; Dhrs7b.
DR VEuPathDB; HostDB:ENSMUSG00000042569; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000158171; -.
DR InParanoid; Q99J47; -.
DR OMA; YFWIMAK; -.
DR PhylomeDB; Q99J47; -.
DR TreeFam; TF313474; -.
DR Reactome; R-MMU-75896; Plasmalogen biosynthesis.
DR BioGRID-ORCS; 216820; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Dhrs7b; mouse.
DR PRO; PR:Q99J47; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99J47; protein.
DR Bgee; ENSMUSG00000042569; Expressed in ileal epithelium and 239 other tissues.
DR ExpressionAtlas; Q99J47; baseline and differential.
DR Genevisible; Q99J47; MM.
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; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0000140; F:acylglycerone-phosphate reductase activity; TAS:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
DR GO; GO:0030223; P:neutrophil differentiation; IMP:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:MGI.
DR GO; GO:0120161; P:regulation of cold-induced thermogenesis; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
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..323
FT /note="Dehydrogenase/reductase SDR family member 7B"
FT /id="PRO_0000312106"
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..323
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 205
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 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 240
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:16141072"
FT /id="VSP_029698"
SQ SEQUENCE 323 AA; 34987 MW; 6C75A07F9BC9B398 CRC64;
MISPSFRKGM LKERVMDLAS QTTILPLLFG CLGIFSLFRL LQRIRSKAYL RNAVVVVTGA
TSGLGRECAK VFHAAGAKLV LCGRNVKALE ELSRELAGSS QGQTHQPFVV TFDLADPGTI
AAAAAEILQC FGYVDVLINN AGISYRGTIS DTIVDVDRKV MEINYFGPVA LTKALLPSMV
ERKQGHIVAI SSIQGKISIP FRSAYSASKH ATQAFFDCLR AEMEEANIKV TVISPGYIHT
NLSVNAVTAD GSRYGALDKN TAQGRSAAEV AQDVFDAVGK KKKDVLLTDF VPSMAVYIRT
LAPGLFFRIM ASRARKERKS KSS
