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Database: UniProt
Entry: F1S6B6_PIG
LinkDB: F1S6B6_PIG
Original site: F1S6B6_PIG 
ID   F1S6B6_PIG              Unreviewed;       535 AA.
AC   F1S6B6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 3.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   Name=FMO2 {ECO:0000313|Ensembl:ENSSSCP00000016190.3,
GN   ECO:0000313|VGNC:VGNC:88171};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016190.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000016190.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016190.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HCZ81499.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000016190.3}
RP   IDENTIFICATION.
RG   Ensembl;
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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   EMBL; DQIR01026024; HCZ81499.1; -; Transcribed_RNA.
DR   RefSeq; XP_003130152.1; XM_003130104.3.
DR   STRING; 9823.ENSSSCP00000016190; -.
DR   PaxDb; 9823-ENSSSCP00000016190; -.
DR   Ensembl; ENSSSCT00000016636.5; ENSSSCP00000016190.3; ENSSSCG00000015267.5.
DR   GeneID; 100525884; -.
DR   KEGG; ssc:100525884; -.
DR   CTD; 2327; -.
DR   VGNC; VGNC:88171; FMO2.
DR   eggNOG; KOG1399; Eukaryota.
DR   GeneTree; ENSGT00940000161099; -.
DR   HOGENOM; CLU_006909_8_2_1; -.
DR   OMA; QTNHIDY; -.
DR   OrthoDB; 2079054at2759; -.
DR   TreeFam; TF105285; -.
DR   Reactome; R-SSC-217271; FMO oxidises nucleophiles.
DR   Proteomes; UP000008227; Chromosome 9.
DR   Bgee; ENSSSCG00000015267; Expressed in penis and 22 other cell types or tissues.
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; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR   GO; GO:0070995; P:NADPH oxidation; IEA:Ensembl.
DR   GO; GO:0046322; P:negative regulation of fatty acid oxidation; IEA:Ensembl.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0072592; P:oxygen metabolic process; IEA:Ensembl.
DR   GO; GO:0009404; P:toxin metabolic process; IEA:Ensembl.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
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; IPR002254; Flavin_mOase_2.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF84; FLAVIN-CONTAINING MONOOXYGENASE 2; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01122; FMOXYGENASE2.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   1: Evidence at protein level;
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   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
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   Proteomics identification {ECO:0007829|PeptideAtlas:F1S6B6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   TRANSMEM        510..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   535 AA;  60978 MW;  5E4E77A2231BE75F CRC64;
     MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FEQTEDIGGL WRFKENVEDG RASIYQSVIT
     NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAQKFDL LKYIQFQTTV LSVKKRPDFS
     SSGQWTVVTE SNGKEQSAVF DAVMVCSGHH ILPHIPLESF PGIQKFKGQY FHSRQYKHPE
     GFERKRILVI GIGNSASDIA VELSKKAAQV FISTRHGSWV MGRISEDGYP WDMVFHTRFS
     SMLRNVLPRT VVKWMMGQQM NRWFNHENYG LIPQNKYLMK EPILNDDLPS RILYGAIKVK
     SKVKEITETS AIFEDGTVEE GIDVIVFATG YTFSFPFLED PLVKVEDNMV LLYKYMFPPQ
     LEKSTLACIG LIQPLGSIFP TVELQARWVT RVFKGLCTLP SERTMMADII SRNKRRIDLF
     GESNSQILQT NYIDYLDELA LEIGVKPDLV SLLLKDLKLA VKLCFGPCNS YQYRLVGPGQ
     WKGARNAIFT QKQRILKPLK TRALKTSSNL PAFFLLKILG LLAVVVAFFF QLQWF
//
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