ID   HSDL2_RAT               Reviewed;         524 AA.
AC   Q4V8F9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Hydroxysteroid dehydrogenase-like protein 2;
DE            EC=1.-.-.-;
GN   Name=Hsdl2;
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=Testis;
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).
CC   -!- FUNCTION: Has apparently no steroid dehydrogenase activity.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; BC097407; AAH97407.1; -; mRNA.
DR   RefSeq; NP_001020868.1; NM_001025697.1.
DR   AlphaFoldDB; Q4V8F9; -.
DR   SMR; Q4V8F9; -.
DR   BioGRID; 260349; 1.
DR   STRING; 10116.ENSRNOP00000056213; -.
DR   iPTMnet; Q4V8F9; -.
DR   PhosphoSitePlus; Q4V8F9; -.
DR   jPOST; Q4V8F9; -.
DR   PaxDb; Q4V8F9; -.
DR   PRIDE; Q4V8F9; -.
DR   GeneID; 313200; -.
DR   KEGG; rno:313200; -.
DR   CTD; 84263; -.
DR   RGD; 1305387; Hsdl2.
DR   VEuPathDB; HostDB:ENSRNOG00000016692; -.
DR   eggNOG; KOG0725; Eukaryota.
DR   eggNOG; KOG4170; Eukaryota.
DR   HOGENOM; CLU_010194_25_0_1; -.
DR   InParanoid; Q4V8F9; -.
DR   OMA; KFGMSLC; -.
DR   OrthoDB; 1361949at2759; -.
DR   PhylomeDB; Q4V8F9; -.
DR   PRO; PR:Q4V8F9; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000016692; Expressed in heart and 19 other tissues.
DR   Genevisible; Q4V8F9; RN.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; ISO:RGD.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1050.10; -; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003033; SCP2_sterol-bd_dom.
DR   InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF02036; SCP2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF55718; SSF55718; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Hydroxylation; NADP; Oxidoreductase; Peroxisome;
KW   Reference proteome.
FT   CHAIN           1..524
FT                   /note="Hydroxysteroid dehydrogenase-like protein 2"
FT                   /id="PRO_0000319891"
FT   DOMAIN          414..521
FT                   /note="SCP2"
FT   REGION          283..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..406
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         17..23
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YN16"
FT   MOD_RES         116
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TPA8"
FT   MOD_RES         424
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TPA8"
SQ   SEQUENCE   524 AA;  58344 MW;  1A8C5149397F5A4E CRC64;
     MLPNTGKLAG CTVFITGASR GIGKAIALKA AKDGANIVIA AKTTQRHPKL LGTIYTAAEE
     IEAAGGKALP CVVDVRDEQQ INSAVEKAVE RFGGIDILVN NASAISLTNT LETPTKRVDL
     MMSVNTRGTY LTSKACIPFL KKSKVAHILN LSPPLNLNPM WFKQHCAYTI AKYGMSMCVL
     GMAEEFRGEI AVNALWPRTA IHTAAMDMLG GAGVESQCRK VDIIADAAYS IFKRPKSFTG
     NFIIDENILK EEGIKDFDIY AITPGHPLLP DFFLDEHPDA VMEEKESYDP VPEVKEEKLQ
     LQEQPQLQEQ PQLQEKPQLQ EQPQLQEKPQ LQEQPQLQEQ PQLQEQPQQQ PQLQEQPQLQ
     EKPQLQEQPQ QQEKPQPQQQ PQQQPQQRPQ QRPQPQPQPQ PLLQSVLPPK PHFGAVEETF
     RIVKDSLSDE VVRATQAVYQ FELSGEDGGT WFLDLKSKGG KVGHGEPSDR ADVVMSMATE
     DFVKMFSGKL KPTMAFMSGK LKIKGNIALA IKLEKLMTHM NSRL