DHB13_MOUSE
ID DHB13_MOUSE Reviewed; 304 AA.
AC Q8VCR2; A8Y5N6; Q8CIU2;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=17-beta-hydroxysteroid dehydrogenase 13;
DE Short=17-beta-HSD 13;
DE EC=1.1.-.-;
DE AltName: Full=Alcohol dehydrogenase PAN1B-like;
DE AltName: Full=Short-chain dehydrogenase/reductase 9;
DE Flags: Precursor;
GN Name=Hsd17b13; Synonyms=Scdr9;
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 [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ;
RA Oliver P.L., Isaacs A.M., Davies K.E.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18359291; DOI=10.1016/j.bbrc.2008.03.063;
RA Horiguchi Y., Araki M., Motojima K.;
RT "17beta-Hydroxysteroid dehydrogenase type 13 is a liver-specific lipid
RT droplet-associated protein.";
RL Biochem. Biophys. Res. Commun. 370:235-238(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Pancreas;
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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000305|PubMed:18359291}. Lipid droplet
CC {ECO:0000269|PubMed:18359291}. Note=Redistributed from the endoplasmic
CC reticulum to lipids droplets in the cell upon induction of lipids
CC droplet formation. {ECO:0000269|PubMed:18359291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VCR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VCR2-2; Sequence=VSP_015861;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the liver (at protein
CC level). {ECO:0000269|PubMed:18359291}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AY101768; AAM51176.1; -; mRNA.
DR EMBL; AL714024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL20237.1; -; Genomic_DNA.
DR EMBL; BC019427; AAH19427.1; -; mRNA.
DR CCDS; CCDS19480.1; -. [Q8VCR2-1]
DR CCDS; CCDS51576.1; -. [Q8VCR2-2]
DR RefSeq; NP_001156958.1; NM_001163486.1. [Q8VCR2-2]
DR RefSeq; NP_932147.2; NM_198030.2. [Q8VCR2-1]
DR AlphaFoldDB; Q8VCR2; -.
DR SMR; Q8VCR2; -.
DR IntAct; Q8VCR2; 1.
DR STRING; 10090.ENSMUSP00000046772; -.
DR iPTMnet; Q8VCR2; -.
DR PhosphoSitePlus; Q8VCR2; -.
DR SwissPalm; Q8VCR2; -.
DR jPOST; Q8VCR2; -.
DR MaxQB; Q8VCR2; -.
DR PaxDb; Q8VCR2; -.
DR PeptideAtlas; Q8VCR2; -.
DR PRIDE; Q8VCR2; -.
DR ProteomicsDB; 277326; -. [Q8VCR2-1]
DR ProteomicsDB; 277327; -. [Q8VCR2-2]
DR Antibodypedia; 25413; 164 antibodies from 24 providers.
DR DNASU; 243168; -.
DR Ensembl; ENSMUST00000048118; ENSMUSP00000046772; ENSMUSG00000034528. [Q8VCR2-1]
DR Ensembl; ENSMUST00000112803; ENSMUSP00000108422; ENSMUSG00000034528. [Q8VCR2-2]
DR GeneID; 243168; -.
DR KEGG; mmu:243168; -.
DR UCSC; uc008yjw.2; mouse. [Q8VCR2-1]
DR UCSC; uc008yjx.2; mouse. [Q8VCR2-2]
DR CTD; 345275; -.
DR MGI; MGI:2140804; Hsd17b13.
DR VEuPathDB; HostDB:ENSMUSG00000034528; -.
DR eggNOG; KOG1201; Eukaryota.
DR GeneTree; ENSGT00940000161743; -.
DR InParanoid; Q8VCR2; -.
DR OMA; GRWTAYE; -.
DR OrthoDB; 1373099at2759; -.
DR PhylomeDB; Q8VCR2; -.
DR TreeFam; TF312837; -.
DR Reactome; R-MMU-8964572; Lipid particle organization.
DR BioGRID-ORCS; 243168; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Hsd17b13; mouse.
DR PRO; PR:Q8VCR2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VCR2; protein.
DR Bgee; ENSMUSG00000034528; Expressed in left lobe of liver and 30 other tissues.
DR ExpressionAtlas; Q8VCR2; baseline and differential.
DR Genevisible; Q8VCR2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IDA: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:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISO:MGI.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endoplasmic reticulum; Lipid droplet;
KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..304
FT /note="17-beta-hydroxysteroid dehydrogenase 13"
FT /id="PRO_0000042584"
FT REGION 276..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40..67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M875"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 272..304
FT /note="GPGFSSKHPHGGSQQPVTPIPGDLTPSSDFLKH -> FLPERALKAISRIQN
FT IQFEAIVGHKTKMK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015861"
FT CONFLICT 212
FT /note="Q -> K (in Ref. 4; AAH19427)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="S -> F (in Ref. 4; AAH19427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 33458 MW; 91D3A09C56024F01 CRC64;
MNLILEFLLL VGVIIYSYLE SLVKFFIPRR RKSVTGQTVL ITGAGHGIGR LTAYEFAKQK
SRLVLWDINK RGVEETADKC RKLGAVVHVF VVDCSNRAEI YNSVDQVKRE VGDVEIVVNN
AGAIYPADLL SAKDEEITKT FEVNILGHFW IIKALLPSML RRNSGHIVTV ASVCGHGVIP
YLIPYCSSKF AAVGFHRALT AELDTLGKTG IQTSCLCPVF VNTGFTKNPS TRLWPVLEPE
EVARSLINGI LTNKKMIFVP SYINISLILE KGPGFSSKHP HGGSQQPVTP IPGDLTPSSD
FLKH
