UniProt: A0A3Q7STK6

Database: UniProt
Entry: A0A3Q7STK6_VULVU

LinkDB:  A0A3Q7STK6_VULVU 
Original site:  A0A3Q7STK6_VULVU

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Ontology (5)   
   GO (5)   
Gene (8)   
   KEGG GENES (1)   
   ENSEMBL-UP (7)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (5)   
   InterPro (4)   
   Pfam (1)   
All databases (19)   

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ID   A0A3Q7STK6_VULVU        Unreviewed;       532 AA.
AC   A0A3Q7STK6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|ARBA:ARBA00012850, ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   Name=LOC112923472 {ECO:0000313|RefSeq:XP_025859096.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025859096.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025859096.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025859096.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025859096.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004111}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004111}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC       ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177}.
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DR   RefSeq; XP_025859096.1; XM_026003311.1.
DR   AlphaFoldDB; A0A3Q7STK6; -.
DR   STRING; 9627.ENSVVUP00000034946; -.
DR   Ensembl; ENSVVUT00000046032; ENSVVUP00000034943; ENSVVUG00000025155.
DR   Ensembl; ENSVVUT00000046040; ENSVVUP00000034946; ENSVVUG00000025155.
DR   Ensembl; ENSVVUT00000046048; ENSVVUP00000034950; ENSVVUG00000025155.
DR   KEGG; vvp:112923472; -.
DR   OMA; YFRYATQ; -.
DR   OrthoDB; 2079054at2759; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0047822; F:hypotaurine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   InterPro; IPR002255; Flavin_mOase_3.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF81; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING] 6-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01123; FMOXYGENASE3.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|PIRNR:PIRNR000332};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000332};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR000332};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|SAM:Phobius};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|PIRNR:PIRNR000332};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000332};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000332};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        511..531
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   532 AA;  60425 MW;  C05B02BFE9315169 CRC64;
     MGKRVAIVGA GVSGLASIRC CLEEGLEPIC FERSNDVGGL WKFSDRAEEG RASIYRSVFT
     NSSKEMMCFP DFPYPDDYPN YMHHSKLQEY IRIFAQKKNL LRYIQFETLV SSIKKCPSFL
     VTGQWEVVSE KDGKQESAIF DAVMICSGHH VYPNLPTDSF PGLHQFQGQY LHSRDYKDPE
     AFRGKRVLVI GLGNSGSDIA VELSRLATQV IISSRSGSWV MSRVWNDGYP WDMVYVTRFA
     SFLQNTLPSF VSDWLYVKKM NTWFKHENYG LMPLNGPLRK EPVFNDELPS RILCGTVSIK
     PSVKEFTETS AVFEDGTMFE AIDSIIFATG YDYAYPFLDD SIIKSRNSEV TLFKGIFPPL
     IEKPTLAVIG LVQSLGAAIP TADLQARWAA KVFANSCTLP TTSEMMDDID EKMGKKLKWF
     GQSQTLQTDY ITYMDELSSF IGAKPNIPWL FLTDPQLALE VFFGPCSPYQ FRLMGPGKWD
     GARNAILTQW DRTVKPTRTR AVSEAQRPQH FYTLLKMLSF PVLLLVIWLT FY
//

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