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Database: UniProt
Entry: A0A3P8N7C6_ASTCA
LinkDB: A0A3P8N7C6_ASTCA
Original site: A0A3P8N7C6_ASTCA 
ID   A0A3P8N7C6_ASTCA        Unreviewed;       658 AA.
AC   A0A3P8N7C6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=All-trans-retinol 13,14-reductase {ECO:0000256|ARBA:ARBA00041141};
DE            EC=1.3.99.23 {ECO:0000256|ARBA:ARBA00038979};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000000666.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000000666.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000000666.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3P8N7C6; -.
DR   STRING; 8154.ENSACLP00000000666; -.
DR   Ensembl; ENSACLT00000000681.1; ENSACLP00000000666.1; ENSACLG00000000495.1.
DR   GeneTree; ENSGT00390000017613; -.
DR   OMA; AFMFADW; -.
DR   Proteomes; UP000265100; Chromosome 4.
DR   Bgee; ENSACLG00000000495; Expressed in liver and 8 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; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR46091:SF1; ALL-TRANS-RETINOL 13,14-REDUCTASE; 1.
DR   PANTHER; PTHR46091; BLR7054 PROTEIN; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        221..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   658 AA;  72946 MW;  E33CD87E2DA982A1 CRC64;
     MEPNEEVNAV TVPSGLGRGA IMIAVSIICA AIVIFLLHYV FGGRGPDPFE KDTREPLKKR
     VYDKKEKNKV LKQGFVANRV PENLDAIVIG SGVGGLGLAV LLAKVGKRVL VLEQHSRAGG
     CCHTFTEKGF EFDVGIHYIG ELLDHKPFRC MLDQMTNGQL EWEPLENPFD HVVLGPPENR
     RRYPIYSGRT RFTDELKKCF PGEEKAIDEF MKLAKKTGNG VWFLALLKIL PLPLAKFLVH
     TGLLRHLSFF FKMAPRSLTD VVNELTENKD LRAVFSYIFG TYGKIPKEAS FAMHSLLVTH
     YLNGAWYPKG GASEIAYHMI PIIEKAGGAV LVRAPVNRIL FNDAKEACGG SSVSLHTVSS
     TSHRGGDSLC LCFMVSGVSV MKGQEEVHIH APLIISDAGI FNTYQKLIPK DLQTMPAIQK
     QLSMLKHGEG GLSVFMGLNG TKEELGLKAD NYWIFAENNF DELVMNYMKK DREEAAKNVP
     LLFVASPSAK DPTWEARSPG KSTLSLVTFA KYEWFEEWKD GKVTNRGRDY TELKQAFIDT
     ILEVVMDVFP KITRDKIEYI DAGTPITNTH YIGAPKGEIY GADHGISRFD PELNITVRAQ
     TPLKNLYLTG QDVFLCGFAG ALAGALTCGS AILKRNLHLD TIALAKRTAF INTKLKGE
//
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