ID W5N617_LEPOC Unreviewed; 608 AA.
AC W5N617;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Amine oxidase domain-containing protein {ECO:0000259|Pfam:PF01593};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016076.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016076.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC CrtISO subfamily. {ECO:0000256|ARBA:ARBA00005855}.
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DR EMBL; AHAT01028964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N617; -.
DR STRING; 7918.ENSLOCP00000016076; -.
DR Ensembl; ENSLOCT00000016106.1; ENSLOCP00000016076.1; ENSLOCG00000013049.1.
DR eggNOG; KOG4254; Eukaryota.
DR GeneTree; ENSGT00940000163871; -.
DR HOGENOM; CLU_019722_1_0_1; -.
DR InParanoid; W5N617; -.
DR OMA; GLATWFK; -.
DR Proteomes; UP000018468; Linkage group LG15.
DR Bgee; ENSLOCG00000013049; Expressed in intestine and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; BLR7054 PROTEIN; 1.
DR PANTHER; PTHR46091:SF2; INACTIVE ALL-TRANS-RETINOL 13,14-REDUCTASE-RELATED; 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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 203..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..473
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 608 AA; 68154 MW; 3A162E366F06D5EF CRC64;
LKMWLLLFAA GFLILGFALY SRLFANSASP FSRDAVRPPA PLVTDQKQRD KVLKQGFSAD
RVPAELDAVV IGSGIGGLTA AAVLAKAGKR VLVLEQHDQA GGCCHTYMEK GFEFDVGLHY
LGQLHENSLL RVAVDQITEG QLQFAQLEQH FDTVIIGEKE ARRHYHIHSG KTEMAESLRR
QFPHDTEAVD EFMRLMKIAA RKTHYLASLK LVPLWLALFL IKTRLVHCFS SIFRMSATSH
TEVLNTLTSN KDLHVIFSYF FYGVPPKDSS CTINTLLLQH YKRGAYYPRG GASEIPFHII
PVIQKAGGAV LVRAPVQRIL VNQEGAAYGV TVKKGQEEVK VLAPVVISDA GMFNTFEKFL
PPEIQAKPEI RSRLSMVRHS MGSFLVFVGL DGTQEELSIV STNFWLFKNN DMDGSMDYFA
SLSREEVADN IPMMFITFPS AKDPTAKIRH PGKSCMTLLT MAKYEWFEEW KDTTVKKRGP
DYESLKMGIA NALLGWALEI FPQLRDKVVF MEAATPLSNM HYLGSPRGEM YGAEQDLARF
TPEVVARIRS ETPVRNLYIT GQDVFCNGIA GALHGGLLCA STVLNQIIYI DLLVLKKRLK
WEKARKRS
//
