ID   RTSTL_DANRE             Reviewed;         604 AA.
AC   B0S6C5;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Inactive all-trans-retinol 13,14-reductase {ECO:0000305};
DE   AltName: Full=Inactive all-trans-13,14-dihydroretinol saturase B {ECO:0000303|PubMed:17253779};
DE            Short=RetSat B {ECO:0000303|PubMed:17253779};
DE   AltName: Full=Retinol saturase (all-trans-retinol 13,14-reductase)-like protein {ECO:0000312|ZFIN:ZDB-GENE-051113-252};
DE   Flags: Precursor;
GN   Name=retsatl {ECO:0000312|ZFIN:ZDB-GENE-051113-252};
GN   Synonyms=retsatb {ECO:0000303|PubMed:17253779};
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 {ECO:0000312|Proteomes:UP000000437};
RN   [1] {ECO:0000312|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
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] {ECO:0000305}
RP   LACK OF CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17253779; DOI=10.1021/bi062147u;
RA   Moise A.R., Isken A., Dominguez M., de Lera A.R., von Lintig J.,
RA   Palczewski K.;
RT   "Specificity of zebrafish retinol saturase: formation of all-trans-13,14-
RT   dihydroretinol and all-trans-7,8-dihydroretinol.";
RL   Biochemistry 46:1811-1820(2007).
CC   -!- DEVELOPMENTAL STAGE: Detected from the 6-somite stage onwards.
CC       Expressed in cells near the anterior part of the yolk sac at 48 hours
CC       post-fertilization (hpf). Expression refines to the intestine by 72
CC       hpf. {ECO:0000269|PubMed:17253779}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtISO subfamily. {ECO:0000305}.
CC   -!- CAUTION: Has no detectable retinol saturase activity.
CC       {ECO:0000269|PubMed:17253779}.
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DR   EMBL; BX510317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; B0S6C5; -.
DR   SMR; B0S6C5; -.
DR   STRING; 7955.ENSDARP00000043898; -.
DR   PaxDb; B0S6C5; -.
DR   PeptideAtlas; B0S6C5; -.
DR   PRIDE; B0S6C5; -.
DR   Ensembl; ENSDART00000141434; ENSDARP00000115830; ENSDARG00000034989.
DR   ZFIN; ZDB-GENE-051113-252; retsatl.
DR   GeneTree; ENSGT00940000163871; -.
DR   HOGENOM; CLU_019722_1_0_1; -.
DR   OMA; GGCTHSF; -.
DR   PhylomeDB; B0S6C5; -.
DR   PRO; PR:B0S6C5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 9.
DR   Bgee; ENSDARG00000034989; Expressed in bone element and 22 other tissues.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; NAD; NADP; Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..604
FT                   /note="Inactive all-trans-retinol 13,14-reductase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5002755333"
SQ   SEQUENCE   604 AA;  67930 MW;  ADCFCDE567171783 CRC64;
     MWWILLFLEW FVDWARGTFW YLFGRRSGLC KGTISPQGPL VVDQEKKDKV LQKEYASNEV
     PDNLDVIVIG SGIGGLTAAA VLARLGKKVL VLEQDKQAGG LCKTFTEKGF EFDCGFYYVG
     QLHENSFLKI ALDLITDGQV HFAEQGSHVE TVVIGKGPEC KEYTIYNGKK QMEAHLKKQF
     PNDAKAVEEF FKIMKICSEK VRLLCMLKMV PLWFARFILR TGIADFISPI LKYSRTSTSE
     VVKSLTSNQD LLTVFSKTFC GVPPKNSSCM IDALLLHHSK RGVYYPQGGA SEIPYHIIQV
     LEKHGGKVLV NAPVSRVLVN EQQNAYGVAV KTGDEDIEIK ASVVVSNAGV FTTFQKLLTP
     EIQADPQVQE YLKALKPGKG FFQVFAGFNA TMEELGISST DMRLYKGNNV DEMMEEYFAS
     DKQDAPDNVP MMYLSFPSAK DPTSSTRFPG QSRMVIHTLV NPKWFEQWEN VNEAERGEEY
     ENYKMRFANH LFDWACVRFP QLKEKVALLH AVTPINMHGL GASYCSMSAE HNLERYQPLN
     IATIRCNTPV KNLYLSGQDI FTAGYSGALH GGFLCASTVM DRCLHIDLLL QQKKLKSKSV
     KKLE