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Database: UniProt
Entry: O16925
LinkDB: O16925
Original site: O16925 
ID   STDH4_CAEEL             Reviewed;         263 AA.
AC   O16925;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Putative steroid dehydrogenase 4;
DE            EC=1.1.1.-;
GN   Name=stdh-4; Synonyms=tag-57; ORFNames=F25G6.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. 17-beta-HSD 3 subfamily. {ECO:0000305}.
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DR   EMBL; FO080489; CCD64105.2; -; Genomic_DNA.
DR   PIR; D89134; D89134.
DR   RefSeq; NP_505205.2; NM_072804.2.
DR   AlphaFoldDB; O16925; -.
DR   SMR; O16925; -.
DR   STRING; 6239.F25G6.5b.1; -.
DR   PaxDb; 6239-F25G6-5; -.
DR   EnsemblMetazoa; F25G6.5a.1; F25G6.5a.1; WBGene00006435.
DR   GeneID; 184934; -.
DR   KEGG; cel:CELE_F25G6.5; -.
DR   AGR; WB:WBGene00006435; -.
DR   WormBase; F25G6.5a; CE47137; WBGene00006435; stdh-4.
DR   eggNOG; KOG1014; Eukaryota.
DR   GeneTree; ENSGT00940000165708; -.
DR   HOGENOM; CLU_010194_38_0_1; -.
DR   InParanoid; O16925; -.
DR   OMA; HEHPIAM; -.
DR   PhylomeDB; O16925; -.
DR   PRO; PR:O16925; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00006435; Expressed in material anatomical entity and 2 other cell types or tissues.
DR   ExpressionAtlas; O16925; baseline.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd05356; 17beta-HSD1_like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43086:SF1; STEROID DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR43086; VERY-LONG-CHAIN 3-OXOOACYL-COA REDUCTASE; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PIRSF; PIRSF000126; 11-beta-HSD1; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW   Reference proteome; Steroid biosynthesis.
FT   CHAIN           1..263
FT                   /note="Putative steroid dehydrogenase 4"
FT                   /id="PRO_0000054582"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ   SEQUENCE   263 AA;  29521 MW;  4175D4AA01E80D50 CRC64;
     MKVVTGATDG IGRSYALDLA RRGFNIFLIS RTKSKLVKTK KQILNKYSDI EVRYAICDFT
     RVSYEDYKRL LHSLNEVDIG ILINNVGMCF DNPEVLHRVE GGIDTLTNVI NVNILPVTLL
     TAGILPQMMA RKSGIIVNIG SAAGSIHMAK WSVYSATKKY IEWFTSILQK EYENEGIICQ
     TITPLLVSTN MIKNPLSSIF CPNSDSFAKS SLNTIGNSSS TTGYITHQIQ FELIKFVPEI
     IIDLFVKNLN NQLLDYQLDK KRV
//
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