DRS7B_HUMAN
ID DRS7B_HUMAN Reviewed; 325 AA.
AC Q6IAN0; B5MEF4; Q6UX59; Q9BTF9; Q9UFM6; Q9Y3A1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Dehydrogenase/reductase SDR family member 7B {ECO:0000303|PubMed:19027726};
DE EC=1.1.-.- {ECO:0000305};
DE AltName: Full=Short-chain dehydrogenase/reductase family 32C member 1 {ECO:0000303|PubMed:19027726};
DE Short=Protein SDR32C1 {ECO:0000303|PubMed:19027726};
GN Name=DHRS7B {ECO:0000312|HGNC:HGNC:24547};
GN Synonyms=SDR32C1 {ECO:0000303|PubMed:19027726};
GN ORFNames=CGI-93, UNQ212/PRO238;
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 MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-325.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [8]
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34088.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ88862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF151851; AAD34088.1; ALT_FRAME; mRNA.
DR EMBL; AL117567; CAB55997.1; -; mRNA.
DR EMBL; CR457124; CAG33405.1; -; mRNA.
DR EMBL; AC087393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471210; EAX02596.1; -; Genomic_DNA.
DR EMBL; BC004126; AAH04126.1; -; mRNA.
DR EMBL; BC009679; AAH09679.1; -; mRNA.
DR EMBL; AY358498; AAQ88862.1; ALT_INIT; mRNA.
DR CCDS; CCDS11215.1; -.
DR PIR; T17307; T17307.
DR RefSeq; NP_001317088.1; NM_001330159.1.
DR RefSeq; NP_056325.2; NM_015510.4.
DR RefSeq; XP_016879915.1; XM_017024426.1.
DR AlphaFoldDB; Q6IAN0; -.
DR SMR; Q6IAN0; -.
DR BioGRID; 117463; 123.
DR IntAct; Q6IAN0; 18.
DR MINT; Q6IAN0; -.
DR STRING; 9606.ENSP00000378887; -.
DR iPTMnet; Q6IAN0; -.
DR PhosphoSitePlus; Q6IAN0; -.
DR SwissPalm; Q6IAN0; -.
DR BioMuta; DHRS7B; -.
DR DMDM; 162416270; -.
DR EPD; Q6IAN0; -.
DR jPOST; Q6IAN0; -.
DR MassIVE; Q6IAN0; -.
DR MaxQB; Q6IAN0; -.
DR PaxDb; Q6IAN0; -.
DR PeptideAtlas; Q6IAN0; -.
DR PRIDE; Q6IAN0; -.
DR ProteomicsDB; 66366; -.
DR Antibodypedia; 2324; 138 antibodies from 18 providers.
DR DNASU; 25979; -.
DR Ensembl; ENST00000395511.8; ENSP00000378887.3; ENSG00000109016.18.
DR GeneID; 25979; -.
DR KEGG; hsa:25979; -.
DR MANE-Select; ENST00000395511.8; ENSP00000378887.3; NM_015510.5; NP_056325.2.
DR UCSC; uc002gyo.4; human.
DR CTD; 25979; -.
DR DisGeNET; 25979; -.
DR GeneCards; DHRS7B; -.
DR HGNC; HGNC:24547; DHRS7B.
DR HPA; ENSG00000109016; Low tissue specificity.
DR MIM; 616160; gene.
DR neXtProt; NX_Q6IAN0; -.
DR OpenTargets; ENSG00000109016; -.
DR PharmGKB; PA142671976; -.
DR VEuPathDB; HostDB:ENSG00000109016; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000158171; -.
DR InParanoid; Q6IAN0; -.
DR OMA; YFWIMAK; -.
DR OrthoDB; 1313182at2759; -.
DR PhylomeDB; Q6IAN0; -.
DR TreeFam; TF313474; -.
DR PathwayCommons; Q6IAN0; -.
DR Reactome; R-HSA-75896; Plasmalogen biosynthesis.
DR SignaLink; Q6IAN0; -.
DR BioGRID-ORCS; 25979; 26 hits in 1081 CRISPR screens.
DR ChiTaRS; DHRS7B; human.
DR GeneWiki; DHRS7B; -.
DR GenomeRNAi; 25979; -.
DR Pharos; Q6IAN0; Tdark.
DR PRO; PR:Q6IAN0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6IAN0; protein.
DR Bgee; ENSG00000109016; Expressed in hindlimb stylopod muscle and 162 other tissues.
DR ExpressionAtlas; Q6IAN0; baseline and differential.
DR Genevisible; Q6IAN0; HS.
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; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0000140; F:acylglycerone-phosphate reductase activity; TAS:Reactome.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0008611; P:ether lipid biosynthetic process; TAS:Reactome.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0030223; P:neutrophil differentiation; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0120161; P:regulation of cold-induced thermogenesis; IEA:Ensembl.
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 Endoplasmic reticulum; Membrane; NAD; NADP; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..325
FT /note="Dehydrogenase/reductase SDR family member 7B"
FT /id="PRO_0000312105"
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 CONFLICT 210
FT /note="S -> P (in Ref. 2; CAB55997)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="Y -> C (in Ref. 2; CAB55997)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="M -> T (in Ref. 3; CAG33405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 35119 MW; 18F4A4C40D3B95CE CRC64;
MVSPATRKSL PKVKAMDFIT STAILPLLFG CLGVFGLFRL LQWVRGKAYL RNAVVVITGA
TSGLGKECAK VFYAAGAKLV LCGRNGGALE ELIRELTASH ATKVQTHKPY LVTFDLTDSG
AIVAAAAEIL QCFGYVDILV NNAGISYRGT IMDTTVDVDK RVMETNYFGP VALTKALLPS
MIKRRQGHIV AISSIQGKMS IPFRSAYAAS KHATQAFFDC LRAEMEQYEI EVTVISPGYI
HTNLSVNAIT ADGSRYGVMD TTTAQGRSPV EVAQDVLAAV GKKKKDVILA DLLPSLAVYL
RTLAPGLFFS LMASRARKER KSKNS
