ID   HSDL1_DANRE             Reviewed;         319 AA.
AC   A5WWC6; Q5PR56;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Inactive hydroxysteroid dehydrogenase-like protein 1;
GN   Name=hsdl1; ORFNames=si:ch211-172b19.1, zgc:103498;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19026618; DOI=10.1016/j.cbi.2008.10.036;
RA   Meier M., Tokarz J., Haller F., Mindnich R., Adamski J.;
RT   "Human and zebrafish hydroxysteroid dehydrogenase like 1 (HSDL1) proteins
RT   are inactive enzymes but conserved among species.";
RL   Chem. Biol. Interact. 178:197-205(2009).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19026618}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. 17-beta-HSD 3 subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although it belongs to the SDR family, Phe-218 is present
CC       instead of the conserved Tyr which is an active site residue. It is
CC       therefore expected that this protein lacks oxidoreductase activity.
CC       {ECO:0000305}.
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DR   EMBL; CT955964; CAN88283.1; -; Genomic_DNA.
DR   EMBL; BC086821; AAH86821.1; -; mRNA.
DR   RefSeq; NP_001008607.1; NM_001008607.1.
DR   AlphaFoldDB; A5WWC6; -.
DR   SMR; A5WWC6; -.
DR   STRING; 7955.ENSDARP00000061172; -.
DR   PaxDb; A5WWC6; -.
DR   PeptideAtlas; A5WWC6; -.
DR   DNASU; 494064; -.
DR   Ensembl; ENSDART00000061173; ENSDARP00000061172; ENSDARG00000041736.
DR   GeneID; 494064; -.
DR   KEGG; dre:494064; -.
DR   CTD; 83693; -.
DR   ZFIN; ZDB-GENE-041212-31; hsdl1.
DR   eggNOG; KOG1014; Eukaryota.
DR   GeneTree; ENSGT00940000160053; -.
DR   HOGENOM; CLU_010194_38_0_1; -.
DR   InParanoid; A5WWC6; -.
DR   OMA; QYGLMKC; -.
DR   OrthoDB; 913128at2759; -.
DR   PhylomeDB; A5WWC6; -.
DR   TreeFam; TF314591; -.
DR   PRO; PR:A5WWC6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 20.
DR   Bgee; ENSDARG00000041736; Expressed in early embryo and 24 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IDA:ZFIN.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; NADP; Reference proteome.
FT   CHAIN           1..319
FT                   /note="Inactive hydroxysteroid dehydrogenase-like protein
FT                   1"
FT                   /id="PRO_0000313676"
FT   REGION          2..82
FT                   /note="Required for mitochondria translocation"
FT                   /evidence="ECO:0000250"
FT   BINDING         74..80
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        148
FT                   /note="L -> I (in Ref. 2; AAH86821)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="N -> D (in Ref. 2; AAH86821)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="K -> R (in Ref. 2; AAH86821)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        233
FT                   /note="H -> Q (in Ref. 2; AAH86821)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   319 AA;  35124 MW;  8C21E1A95DEB67B3 CRC64;
     MAAVDSFQLL YREIARSCSG YVETLALVGA CYMASKTVIF MRDCYSLIRL YFVPRLVRHR
     DLSQQYGQWA IICGASEAIA KAYAEELARH GICVILISKD LSSVSDTARL ISNNYGVEAI
     CIEADFNQGP SACKPIKDAI SSKDIGFLVN SFDGTLEISQ NFLELSESVL WGTINRNIAA
     TTLVTRLALP AMMEKGRGAV VNISSGHCFH PIPRKAAFSA STAFLDNFSR SLHYEYGDQG
     VFVQSLLPFR VASQRPEGSA PPASWLVPSP QVYASHALST LGISHRTTGY WPHSMQLGLV
     KMMPEWVWML GSRVFTMAT