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AMX1_CAEEL
ID   AMX1_CAEEL              Reviewed;         824 AA.
AC   Q21988;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Amine oxidase family member 1;
GN   Name=amx-1; ORFNames=R13G10.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; Z35602; CAA84671.3; -; Genomic_DNA.
DR   PIR; T24218; T24218.
DR   RefSeq; NP_497772.2; NM_065371.4.
DR   AlphaFoldDB; Q21988; -.
DR   SMR; Q21988; -.
DR   BioGRID; 40731; 1.
DR   STRING; 6239.R13G10.2; -.
DR   EPD; Q21988; -.
DR   PaxDb; Q21988; -.
DR   PeptideAtlas; Q21988; -.
DR   EnsemblMetazoa; R13G10.2.1; R13G10.2.1; WBGene00000137.
DR   GeneID; 175493; -.
DR   KEGG; cel:CELE_R13G10.2; -.
DR   UCSC; R13G10.2; c. elegans.
DR   CTD; 175493; -.
DR   WormBase; R13G10.2; CE41445; WBGene00000137; amx-1.
DR   eggNOG; KOG0029; Eukaryota.
DR   GeneTree; ENSGT00940000174336; -.
DR   HOGENOM; CLU_007885_0_0_1; -.
DR   InParanoid; Q21988; -.
DR   OMA; GNLEYAC; -.
DR   OrthoDB; 1034142at2759; -.
DR   PhylomeDB; Q21988; -.
DR   Reactome; R-CEL-3214842; HDMs demethylate histones.
DR   PRO; PR:Q21988; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000137; Expressed in embryo and 4 other tissues.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0140682; F:histone H3-di/monomethyl-lysine-4 FAD-dependent demethylase activity; IGI:WormBase.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0034720; P:histone H3-K4 demethylation; IGI:WormBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..824
FT                   /note="Amine oxidase family member 1"
FT                   /id="PRO_0000099879"
FT   DOMAIN          245..346
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         352..407
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   824 AA;  93433 MW;  801E8919124D4072 CRC64;
     MTTELEIDDR KEEEAQIPGE TSESEEGDEP VKMNRVKRAC AMAAESLKEA KRIKNMLMEE
     ECVLQLGNCK KTASYGHRLS KTEACCPSCF SVAFRGKDYE NEFTIWKQKA MDGQTHVRSE
     QFVKRYVNSC FLPYYAKCHQ CSKYSKLITS DSLSAQQLSD FKCDCASTIE SPKIERVRED
     SEWCFNEFGH PPLLQNNISY DLLVDHYVTR TTGMDATCQE KAALIDNGGI EFRDTRRIMN
     MFYVPFTDVI ANIVHPEFME TDEKFAFPKF ADDPISIYYL QVRNTIIAMW LKHPFVELTV
     KMIEPQIIVR GHARIFFIEH LIHPILEFLT IKGVVNYGAF DFRIDPLNGM RPKIAIIGAG
     ISGISTARHL KHLGIDAVLF EAKDRFGGRM MDDQSLGVSV GKGAQIIVGN INNPITLLCE
     QIGIKYRNSN FFCPLIDENG RCFTLERKEL DDQVDLHYNN VLDAIRNKYQ SDRNFPDVPL
     EVTNFRHFTE MFSKMSSGLL SAADLDSLYT PEFEKLLDFH LGNLEFSCGT HVSNLSAKDY
     DHNEKFGNFA GEHAVITDGA QRIIDFLATG LDIRLNCPVK CIDWGRDDRK VKIFFENAEQ
     AAEEFDKVVI TTSLSVLKSN HSKMFVPPLP IEKQKAIDDL GAGLIEKIAV KFDRRFWDTV
     DADGLRTEYF GKVSDCKTDR SLFNIFYDFS GKDPNGEDTF VLMSYVTAEH VNLVNVLTES
     EVADKFCATL RKMFPSAVIN PLGHMMSHWG ADRFVGMSYT FVPFGSDGDA TYNQLKKSID
     EKLYFAGEHT IAAEPQTMAG AYISGLREAG QIVMSLKRDS ATFE
 
 
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