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Database: UniProt
Entry: H3A2C6_LATCH
LinkDB: H3A2C6_LATCH
Original site: H3A2C6_LATCH 
ID   H3A2C6_LATCH            Unreviewed;       501 AA.
AC   H3A2C6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000003797.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000003797.1}
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|RuleBase:RU362067};
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|RuleBase:RU362067}.
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DR   EMBL; AFYH01183174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01183175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01183176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3A2C6; -.
DR   STRING; 7897.ENSLACP00000003797; -.
DR   Ensembl; ENSLACT00000003831.1; ENSLACP00000003797.1; ENSLACG00000003383.1.
DR   eggNOG; KOG0029; Eukaryota.
DR   GeneTree; ENSGT00940000160928; -.
DR   HOGENOM; CLU_004498_8_3_1; -.
DR   InParanoid; H3A2C6; -.
DR   OMA; YSTRQFL; -.
DR   TreeFam; TF313314; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR   Gene3D; 1.10.10.1620; -; 1.
DR   Gene3D; 3.30.70.2100; -; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR10742:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 2.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362067};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362067}; Membrane {ECO:0000256|RuleBase:RU362067};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|RuleBase:RU362067};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362067}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..501
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003579815"
FT   TRANSMEM        127..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362067"
FT   DOMAIN          68..121
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   DOMAIN          253..500
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   501 AA;  57032 MW;  D05A28AA7233BC20 CRC64;
     PAMTSLLVSF PVFLLAWFLL GMQAAKTEQD PLSECFKDPD YEELLNIAKR GLPKHSSPKH
     IIIVGAGIAG LVAATVLEQA GHNVTILEAS DRVGGRIHTY RPHTGDWYAE LGAMRLPTSH
     QMLHRKGLGF FFLLFRTFFL FLMLRFHSYK WAFQAGPPEM LQYQDRGLKH SSKHFLILKI
     IFFQVREDLK NSNCSYVLKK YDAYSVKQYL VDVCKLSKGA VQMVGDILND QSLFHTAFSE
     RLRLQAANNN KVHFKQIVGG TDRLPRAFQD RIKSPIYLNS QVIAINQTGD KVTVFYKETA
     YNFFSELQAD YVLITITARA TKFLDFHPAL SLSKIRALHA VHYGCSTKIL LVFREKFWEK
     DKIHGGKSIT DLPSRLIFYP SHTFQSNVGV LLASYTWSDE SSSFLGLSDE ECIMAALNDV
     AKIHGEHIRE LLESGVVKKW STDPYSLEAF ALYTPYQLRE YTEDLFKKEG RIHFAGEHTT
     LSHAWIETAM KSALKAARNI N
//
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