HSDL2_PONAB
ID HSDL2_PONAB Reviewed; 418 AA.
AC Q5RA68;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Hydroxysteroid dehydrogenase-like protein 2;
DE EC=1.-.-.-;
GN Name=HSDL2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859151; CAH91342.1; -; mRNA.
DR RefSeq; NP_001125794.1; NM_001132322.1.
DR AlphaFoldDB; Q5RA68; -.
DR SMR; Q5RA68; -.
DR STRING; 9601.ENSPPYP00000021856; -.
DR GeneID; 100172722; -.
DR KEGG; pon:100172722; -.
DR CTD; 84263; -.
DR eggNOG; KOG0725; Eukaryota.
DR eggNOG; KOG4170; Eukaryota.
DR InParanoid; Q5RA68; -.
DR OrthoDB; 1361949at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IPR020904; Sc_DH/Rdtase_CS.
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.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Hydroxylation; NADP; Oxidoreductase; Peroxisome;
KW Reference proteome.
FT CHAIN 1..418
FT /note="Hydroxysteroid dehydrogenase-like protein 2"
FT /id="PRO_0000319890"
FT DOMAIN 306..415
FT /note="SCP2"
FT REGION 287..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
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 318
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q2TPA8"
SQ SEQUENCE 418 AA; 45395 MW; EB8595932ECF061F CRC64;
MLPNTGRLAG CTVFITGASR GIGKAIALKA AKDGANIVIA AKTAQPHPKL LGTIYTAAEE
IEAVGGKALP CIVDVRDEQQ INAAVEKAIK QFGGIDILVN NASAISLTNT LDTPTKRLDL
MMNVNTRGTY LASKACIPYL KKSKVAHILN ISPPLNLNPI WFKQHCAYTI AKYGMSMYVL
GMAEEFKGEI AVNALWPKTA IHTAAMDMLG GPGIESQCRK VDIIADAAYS IFQKPKSFTG
NFVIDESILK EEGIENFDVY AIKPGHPLQP DFFLDEYPEA VSKKMESTGA VPEFKEEKPQ
PQPKPRSGAV EETFRIVKDS LSDDVVKATQ AVYLFELSGE DGGTWFLDLK SKGGNVGYGE
PSDQADVVMS MTTDDFVKMF SGKLKPTMAF MSGKLKIKGN MALAIKLEKL MNQMNARL
