ID   A0A0B2VAM9_TOXCA        Unreviewed;       615 AA.
AC   A0A0B2VAM9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=All-trans-retinol 13,14-reductase {ECO:0000313|EMBL:KHN78524.1};
GN   Name=Retsat {ECO:0000313|EMBL:KHN78524.1};
GN   ORFNames=Tcan_13961 {ECO:0000313|EMBL:KHN78524.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN78524.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN78524.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN78524.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtISO subfamily. {ECO:0000256|ARBA:ARBA00005855}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHN78524.1}.
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DR   EMBL; JPKZ01002087; KHN78524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VAM9; -.
DR   STRING; 6265.A0A0B2VAM9; -.
DR   OMA; AFMFADW; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   PANTHER; PTHR46091; BLR7054 PROTEIN; 1.
DR   PANTHER; PTHR46091:SF3; BLR7054 PROTEIN; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PRINTS; PR00891; RABGDIREP.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..615
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002096027"
SQ   SEQUENCE   615 AA;  70611 MW;  BB3BEF208917E99F CRC64;
     MWLVVIVVVS LLTLAVIRCI YRIRGGTINE NCFLKMACTG KPTEVALSEK EKHDILRQAF
     HPSKVCSQWD VIVIGSGLSG LTIAKILAAS GRKVLVLEQH DRAGGACHTF ELDRFEFDVG
     LHYVLDMYPG SELYKICSAV TDSQVQWQQM QEPFDVAVIG DKQYGRTAGD HEMFRKQLKE
     WFPTEKDKID AYFDYVNSCL REVPWLFRMK FFPRLLTRIL LKWGIFGSLS KVFKYSTRTL
     IETMQEFGFS NEIQVVCSYY CVNYGIPPTR ASFWQHWLFL MNSGYYPIGG ATMITSHIVR
     SIQKFGGKVL VKADVKEIRF ENEKVEGVVV DYGASDCFIA APMVVSTVHL THLFSNLIPK
     QIATKSSMFN VIKKLNAIDS LPVAAFQAYI GLRGSQEDLK LPSNNYFWYK CDEPMQIDTY
     LRMSIQEALD YGCPPFIYVT FPSAKDPTWN DRHPDISTCQ LISVINPQWF MDFKDKSKRK
     SLKRSNKEEY LNLKNTIGEL LIEQFIKMFP RLEKKIAFTE FSSSLSQQYY MQNSYGELYG
     LPQNVDRFKP QYWSELRCKT DIHGLFLSGQ DVLFCGVSSA LQNGMFSAGV ILQRDLFKDL
     NEAYSLQSND EMKSE
//