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Database: UniProt
Entry: G3P4E2_GASAC
LinkDB: G3P4E2_GASAC
Original site: G3P4E2_GASAC 
ID   G3P4E2_GASAC            Unreviewed;       613 AA.
AC   G3P4E2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=All-trans-retinol 13,14-reductase {ECO:0000256|ARBA:ARBA00041141};
DE            EC=1.3.99.23 {ECO:0000256|ARBA:ARBA00038979};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000012465.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000012465.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000012465.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + all-trans-13,14-dihydroretinol = AH2 + all-trans-retinol;
CC         Xref=Rhea:RHEA:19193, ChEBI:CHEBI:13193, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:52075; EC=1.3.99.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00036004};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|ARBA:ARBA00001937};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtISO subfamily. {ECO:0000256|ARBA:ARBA00005855}.
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DR   AlphaFoldDB; G3P4E2; -.
DR   STRING; 69293.ENSGACP00000012465; -.
DR   Ensembl; ENSGACT00000012489.1; ENSGACP00000012465.1; ENSGACG00000009445.1.
DR   eggNOG; KOG4254; Eukaryota.
DR   GeneTree; ENSGT00390000017613; -.
DR   InParanoid; G3P4E2; -.
DR   OMA; AFMFADW; -.
DR   TreeFam; TF328375; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000009445; Expressed in intestinal epithelial cell and 13 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR46091:SF1; ALL-TRANS-RETINOL 13,14-REDUCTASE; 1.
DR   PANTHER; PTHR46091; BLR7054 PROTEIN; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..613
FT                   /note="All-trans-retinol 13,14-reductase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003449361"
FT   DOMAIN          77..480
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   613 AA;  68517 MW;  B27DCABD3216A97D CRC64;
     SFLTHLFLTM CRLLVSRCLT VSINYCSGPN PFEKDTREPL KKMVHDRKQK NKVLKQGFLA
     SRVPDNLDAI IIGSGIGGLG LGVLLAKVGK KVLVLEQHDR AGGCCHTFTE KGFEFDVGIH
     YIGDLLEHKP FRCMLDSMTN GQLQWEPLEN PYDQVVLGPP ENRRKYPIYS GRTRFPEELK
     KCFPGEEKAI DEYVRLAKKV GRGIWLLAML KICPVPLAKF LVYTGLAQRL SFFFKMAPRS
     LTEVVNELTD NKDLRAVFSY IFGTYGNIPK DSSFAMHSLL VTHYLNGAWY PKGGASEIAY
     HMIPIIEKAG GAVLVRAPVN RILFNDSKEA TGVSVMKGQE EMHIHAPMVI SNAGIFNTYQ
     KLLPKELQAM PAIQKQTSMM KNGEGGLSVF VGLNGTKEEL GLKADNYWIF AENNFDELVE
     KYSNGKREES AHKVPLLFVA SPSAKDPTWE ERSPGKSTVS LVSFANYEWF EEWKDDKVSN
     RSPEYKELKQ AFIDSILEVV FDVFPKITRD KVEFIDAGTP ITNTHYIGAP KGEIYGADHG
     IARFSPELNA TVRPQTPLKN LYLTGQDVFT CGFAGALAGA LSCGSIILNR NLHLDAIAMA
     KKIRFMNPKL KGE
//
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