ID   DHB13_RAT               Reviewed;         300 AA.
AC   Q5M875;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=17-beta-hydroxysteroid dehydrogenase 13;
DE            Short=17-beta-HSD 13;
DE            EC=1.1.-.-;
DE   AltName: Full=Short-chain dehydrogenase/reductase 9;
DE   Flags: Precursor;
GN   Name=Hsd17b13; Synonyms=Scdr9;
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 [LARGE SCALE MRNA].
RC   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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-69, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q8VCR2}. Lipid droplet
CC       {ECO:0000250|UniProtKB:Q8VCR2}. Note=Redistributed from the endoplasmic
CC       reticulum to lipids droplets in the cell upon induction of lipids
CC       droplet formation. {ECO:0000250|UniProtKB:Q8VCR2}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; BC088191; AAH88191.1; -; mRNA.
DR   RefSeq; NP_001009684.1; NM_001009684.1.
DR   AlphaFoldDB; Q5M875; -.
DR   SMR; Q5M875; -.
DR   IntAct; Q5M875; 1.
DR   STRING; 10116.ENSRNOP00000029333; -.
DR   iPTMnet; Q5M875; -.
DR   PhosphoSitePlus; Q5M875; -.
DR   jPOST; Q5M875; -.
DR   PaxDb; Q5M875; -.
DR   PRIDE; Q5M875; -.
DR   Ensembl; ENSRNOT00000038188; ENSRNOP00000029333; ENSRNOG00000002212.
DR   GeneID; 305150; -.
DR   KEGG; rno:305150; -.
DR   CTD; 345275; -.
DR   RGD; 1359553; Hsd17b13.
DR   eggNOG; KOG1201; Eukaryota.
DR   GeneTree; ENSGT00940000161743; -.
DR   HOGENOM; CLU_010194_2_5_1; -.
DR   InParanoid; Q5M875; -.
DR   OMA; GRWTAYE; -.
DR   OrthoDB; 1373099at2759; -.
DR   PhylomeDB; Q5M875; -.
DR   TreeFam; TF312837; -.
DR   Reactome; R-RNO-8964572; Lipid particle organization.
DR   PRO; PR:Q5M875; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000002212; Expressed in pancreas and 17 other tissues.
DR   Genevisible; Q5M875; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; ISS: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:RGD.
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; Endoplasmic reticulum; Lipid droplet; NADP; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..300
FT                   /note="17-beta-hydroxysteroid dehydrogenase 13"
FT                   /id="PRO_0000042585"
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:0007744|PubMed:22673903"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCR2"
SQ   SEQUENCE   300 AA;  33494 MW;  2BE40FE0A053F1F7 CRC64;
     MNLILELLLL VGIIIYSYLE SLVKFFIPQR RKSVAGQTVL ITGAGHGIGR LTAYEFAKQK
     SRLVLWDISK HGVEETAAKC RKLGAVVHVF VVDCSNRAEI YKSVDQVKKE VGDIEIVVNN
     AGAIYPADLL STKDEEITKT FEVNILGHFW IIKALLPSML RRNSGHIVTV ASVCGHRVIP
     YLIPYCSSKF AAVGFHRALT AELDTLGKTG IKTSCLCPVF VNTGFTKNPS TRLWPVLEPD
     EVARSLIDGI LTNKKMIFVP SYINISLIVE MFFPERVLKA INRIQNIQFE AIVGHRTKRK