ID A0A0R4J0C2_MOUSE Unreviewed; 630 AA.
AC A0A0R4J0C2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN Name=Il4i1 {ECO:0000313|Ensembl:ENSMUSP00000033015.8};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000033015.8, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000033015.8, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000033015.8,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000033015.8}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000033015.8};
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 RefSeq; NP_034345.2; NM_010215.3.
DR AlphaFoldDB; A0A0R4J0C2; -.
DR SMR; A0A0R4J0C2; -.
DR EPD; A0A0R4J0C2; -.
DR ProteomicsDB; 365099; -.
DR Antibodypedia; 32207; 168 antibodies from 25 providers.
DR DNASU; 14204; -.
DR Ensembl; ENSMUST00000033015.8; ENSMUSP00000033015.8; ENSMUSG00000074141.14.
DR GeneID; 14204; -.
DR KEGG; mmu:14204; -.
DR CTD; 259307; -.
DR MGI; MGI:109552; Il4i1.
DR VEuPathDB; HostDB:ENSMUSG00000074141; -.
DR GeneTree; ENSGT00940000162082; -.
DR OMA; GIAVGWH; -.
DR OrthoDB; 3597164at2759; -.
DR BioGRID-ORCS; 14204; 4 hits in 46 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 7.
DR Bgee; ENSMUSG00000074141; Expressed in peripheral lymph node and 76 other cell types or tissues.
DR ExpressionAtlas; A0A0R4J0C2; baseline and differential.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR Gene3D; 3.90.660.10; -; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF21; L-AMINO-ACID OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 1: Evidence at protein level;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Proteomics identification {ECO:0007829|EPD:A0A0R4J0C2,
KW ECO:0007829|MaxQB:A0A0R4J0C2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..630
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006451949"
FT DOMAIN 68..502
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 532..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 70163 MW; 667515D60D893955 CRC64;
MAGLALRLVL AATLLGLAGS LDWKAASSLN PIEKCMEDHD YEQLLKVVTL GLNRTSKPQK
VVVVGAGVAG LVAAKMLSDA GHKVTILEAD NRIGGRIFTF RDEKTGWIGE LGAMRMPSSH
RILHKLCRTL GLNLTQFTQY DENTWTEVHN VKLRNYVVEK MPEKLGYNLN NRERGHSPED
IYQMALNKAF KDLKALGCKK AMNKFNKHTL LEYLLEEGNL SRPAVQLLGD VMSEEGFFYL
SFAEALRAHA CLSDRLRYSR IVGGWDLLPR ALLSSLSGAL LLNAPVVSIT QGRNDVRVHI
ATSLHSEKTL TADVVLLTAS GPALQRITFS PPLTRKRQEA LRALHYVAAS KVFLSFRRPF
WHEEHIEGGH SNTDRPSRLI FYPAQGEGSL LLASYTWSDA AAPFAGLSTD QTLRLVLQDV
AALHGPVVFR LWDGRGVVKR WAEDPHSQGG FVVQPPLYGR EAEDYDWSAP FGRIYFAGEH
TALPHGWVET AVKSGLRAAV RINNNYGYGE VDPQMMEHAY AEANYLDQYP EGERPEEQQA
REEVSPDEQE PSHKHLLVET SPEGQQHAFV EAIPELQGHV FVETVPQEKG HAHQNIYPSE
HVQVHGEVIP EWHGHGGSGT PQMHRVGDHS
//
