ID   OXLA_MOUSE              Reviewed;         630 AA.
AC   O09046; Q1LZI6; Q3T9N9; Q3U7S6; Q3V0K2; Q6Y632; Q6YBV6; Q6YDI8; Q8R2G8;
AC   Q9CXK7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-NOV-2023, entry version 168.
DE   RecName: Full=L-amino-acid oxidase {ECO:0000305};
DE            Short=LAAO {ECO:0000305};
DE            Short=LAO {ECO:0000305};
DE            EC=1.4.3.2 {ECO:0000269|PubMed:15383589};
DE            EC=1.4.3.25 {ECO:0000250|UniProtKB:Q96RQ9};
DE   AltName: Full=Interleukin-4-induced protein 1 {ECO:0000303|Ref.2};
DE            Short=IL4-induced protein 1 {ECO:0000303|Ref.2};
DE            Short=mIL4I1 {ECO:0000303|PubMed:26599209};
DE   AltName: Full=Protein Fig-1 {ECO:0000303|PubMed:9122225};
DE            Short=mFIG1 {ECO:0000303|PubMed:9122225};
DE   Flags: Precursor;
GN   Name=Il4i1 {ECO:0000303|Ref.2, ECO:0000312|MGI:MGI:109552};
GN   Synonyms=Fig1 {ECO:0000303|PubMed:9122225};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   AND INDUCTION.
RC   STRAIN=BALB/cJ, and CBA/J;
RX   PubMed=9122225; DOI=10.1073/pnas.94.6.2507;
RA   Chu C.C., Paul W.E.;
RT   "Fig1, an interleukin 4-induced mouse B cell gene isolated by cDNA
RT   representational difference analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:2507-2512(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   STRAIN=CBA/J, MRL/MpJ, and NZW/LacJ;
RA   Chu C.C., Kim J.A., Gupta N., Yuen G.J., Thomas R.R., George J., Hsueh K.;
RT   "Interleukin-four induced gene-1 polymorphisms correlate with Sle3
RT   autoimmune susceptibility.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Embryonic head, Spleen, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 122-289.
RC   STRAIN=BALB/cJ; TISSUE=Spleen;
RX   PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA   Chu C.C., Paul W.E.;
RT   "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT   representational difference analysis.";
RL   Mol. Immunol. 35:487-502(1998).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=15383589; DOI=10.4049/jimmunol.173.7.4561;
RA   Mason J.M., Naidu M.D., Barcia M., Porti D., Chavan S.S., Chu C.C.;
RT   "IL-4-induced gene-1 is a leukocyte L-amino acid oxidase with an unusual
RT   acidic pH preference and lysosomal localization.";
RL   J. Immunol. 173:4561-4567(2004).
RN   [7]
RP   ALTERNATIVE PROMOTER USAGE, AND TISSUE SPECIFICITY.
RX   PubMed=16029492; DOI=10.1186/1741-7007-3-16;
RA   Wiemann S., Kolb-Kokocinski A., Poustka A.;
RT   "Alternative pre-mRNA processing regulates cell-type specific expression of
RT   the IL4l1 and NUP62 genes.";
RL   BMC Biol. 3:16-16(2005).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen, and Testis;
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   [9]
RP   FUNCTION.
RX   PubMed=21469114; DOI=10.1002/eji.201041119;
RA   Lasoudris F., Cousin C., Prevost-Blondel A., Martin-Garcia N.,
RA   Abd-Alsamad I., Ortonne N., Farcet J.P., Castellano F.,
RA   Molinier-Frenkel V.;
RT   "IL4I1: an inhibitor of the CD8(+) antitumor T-cell response in vivo.";
RL   Eur. J. Immunol. 41:1629-1638(2011).
RN   [10]
RP   FUNCTION.
RX   PubMed=25778793; DOI=10.1002/eji.201445000;
RA   Cousin C., Aubatin A., Le Gouvello S., Apetoh L., Castellano F.,
RA   Molinier-Frenkel V.;
RT   "The immunosuppressive enzyme IL4I1 promotes FoxP3(+) regulatory T
RT   lymphocyte differentiation.";
RL   Eur. J. Immunol. 45:1772-1782(2015).
RN   [11]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=26599209; DOI=10.1371/journal.pone.0142979;
RA   Yue Y., Huang W., Liang J., Guo J., Ji J., Yao Y., Zheng M., Cai Z., Lu L.,
RA   Wang J.;
RT   "IL4I1 is a novel regulator of M2 macrophage polarization that can inhibit
RT   T Cell activation via L-tryptophan and arginine depletion and IL-10
RT   production.";
RL   PLoS ONE 10:e0142979-e0142979(2015).
RN   [12]
RP   FUNCTION.
RX   PubMed=28405502; DOI=10.1080/2162402x.2016.1278331;
RA   Bod L., Lengagne R., Wrobel L., Ramspott J.P., Kato M., Avril M.F.,
RA   Castellano F., Molinier-Frenkel V., Prevost-Blondel A.;
RT   "IL4-induced gene 1 promotes tumor growth by shaping the immune
RT   microenvironment in melanoma.";
RL   OncoImmunology 6:e1278331-e1278331(2017).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=29288206; DOI=10.4049/jimmunol.1601609;
RA   Bod L., Douguet L., Auffray C., Lengagne R., Bekkat F., Rondeau E.,
RA   Molinier-Frenkel V., Castellano F., Richard Y., Prevost-Blondel A.;
RT   "IL-4-induced gene 1: a negative immune checkpoint controlling B cell
RT   differentiation and activation.";
RL   J. Immunol. 200:1027-1038(2018).
RN   [14]
RP   FUNCTION.
RX   PubMed=32818467; DOI=10.1016/j.cell.2020.07.038;
RA   Sadik A., Somarribas Patterson L.F., Oeztuerk S., Mohapatra S.R.,
RA   Panitz V., Secker P.F., Pfaender P., Loth S., Salem H., Prentzell M.T.,
RA   Berdel B., Iskar M., Faessler E., Reuter F., Kirst I., Kalter V.,
RA   Foerster K.I., Jaeger E., Guevara C.R., Sobeh M., Hielscher T., Poschet G.,
RA   Reinhardt A., Hassel J.C., Zapatka M., Hahn U., von Deimling A., Hopf C.,
RA   Schlichting R., Escher B.I., Burhenne J., Haefeli W.E., Ishaque N.,
RA   Boehme A., Schaeuble S., Thedieck K., Trump S., Seiffert M., Opitz C.A.;
RT   "IL4I1 is a metabolic immune checkpoint that activates the AHR and promotes
RT   tumor progression.";
RL   Cell 182:1252-1270(2020).
CC   -!- FUNCTION: Secreted L-amino-acid oxidase that acts as a key
CC       immunoregulator (PubMed:32818467). Has preference for L-aromatic amino
CC       acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan
CC       (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and
CC       indole-3-pyruvic acid (I3P), respectively (PubMed:15383589). Also has
CC       weak L-arginine oxidase activity (By similarity). Acts as a negative
CC       regulator of anti-tumor immunity by mediating Trp degradation via an
CC       indole pyruvate pathway that activates the transcription factor AHR
CC       (PubMed:21469114, PubMed:28405502, PubMed:32818467). IL4I1-mediated Trp
CC       catabolism generates I3P, giving rise to indole metabolites (indole-3-
CC       acetic acid (IAA) and indole-3-aldehyde (I3A)) and kynurenic acid,
CC       which act as ligands for AHR, a ligand-activated transcription factor
CC       that plays important roles in immunity and cancer (By similarity). AHR
CC       activation by indoles following IL4I1-mediated Trp degradation enhances
CC       tumor progression by promoting cancer cell motility and suppressing
CC       adaptive immunity (PubMed:32818467). Also has an immunoregulatory
CC       function in some immune cell, probably by mediating Trp degradation and
CC       promoting downstream AHR activation: inhibits T-cell activation and
CC       proliferation, promotes the differentiation of naive CD4(+) T-cells
CC       into FOXP3(+) regulatory T-cells (Treg) and regulates the development
CC       and function of B-cells (PubMed:25778793, PubMed:29288206). Also
CC       regulates M2 macrophage polarization by inhibiting T-cell activation
CC       (PubMed:26599209). Also has antibacterial properties by inhibiting
CC       growth of Gram negative and Gram positive bacteria through the
CC       production of NH4(+) and H2O2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q96RQ9, ECO:0000269|PubMed:15383589,
CC       ECO:0000269|PubMed:21469114, ECO:0000269|PubMed:25778793,
CC       ECO:0000269|PubMed:26599209, ECO:0000269|PubMed:28405502,
CC       ECO:0000269|PubMed:29288206, ECO:0000269|PubMed:32818467}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59869; EC=1.4.3.2;
CC         Evidence={ECO:0000269|PubMed:15383589};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13782;
CC         Evidence={ECO:0000269|PubMed:15383589};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+);
CC         Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57912; Evidence={ECO:0000250|UniProtKB:Q96RQ9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61245;
CC         Evidence={ECO:0000250|UniProtKB:Q96RQ9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:15383589};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61241;
CC         Evidence={ECO:0000269|PubMed:15383589};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242,
CC         ChEBI:CHEBI:58315; Evidence={ECO:0000250|UniProtKB:Q96RQ9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61249;
CC         Evidence={ECO:0000250|UniProtKB:Q96RQ9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:58489; EC=1.4.3.25;
CC         Evidence={ECO:0000250|UniProtKB:Q96RQ9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51405;
CC         Evidence={ECO:0000250|UniProtKB:Q96RQ9};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:15383589};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.5 mM for phenylalanine (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:15383589};
CC         Vmax=0.0099 nmol/min/mg enzyme toward phenylalanine (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:15383589};
CC       pH dependence:
CC         Optimum pH is 4.0. {ECO:0000269|PubMed:15383589};
CC   -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC       pathway. {ECO:0000250|UniProtKB:Q96RQ9}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q96RQ9}.
CC       Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000250|UniProtKB:Q96RQ9}. Note=Secreted at the immunological
CC       synapse. {ECO:0000250|UniProtKB:Q96RQ9}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Lysosome
CC       {ECO:0000269|PubMed:15383589}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Lysosome
CC       {ECO:0000269|PubMed:15383589}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=1;
CC         IsoId=O09046-1; Sequence=Displayed;
CC       Name=2; Synonyms=IL4I1_2 {ECO:0000303|PubMed:16029492};
CC         IsoId=O09046-2; Sequence=VSP_017174;
CC   -!- TISSUE SPECIFICITY: Primarily found in immune tissues.
CC       {ECO:0000269|PubMed:16029492, ECO:0000269|PubMed:9122225}.
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Primarily found in immune tissues,
CC       mostly in B-lymphocytes. {ECO:0000269|PubMed:16029492}.
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: Restricted to the testis,
CC       predominantly in Sertoli cells at the periphery of the ducts, and the
CC       brain, including Purkinje cells, hippocampus and mitral cells in the
CC       olfactory bulb. No isoform 2 expression in fetal tissues.
CC       {ECO:0000269|PubMed:16029492}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases during bone marrow-derived
CC       macrophage (BMDM) differentiation: expression is much higher in primary
CC       macrophages than monocytes. {ECO:0000269|PubMed:26599209}.
CC   -!- INDUCTION: By interleukin-4. {ECO:0000269|PubMed:9122225}.
CC   -!- DISRUPTION PHENOTYPE: Mice display an accelerated B-cell egress from
CC       the bone marrow, resulting in the accumulation of peripheral follicular
CC       B-cells. {ECO:0000269|PubMed:29288206}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Uses the promoter of the upstream NUP62
CC       gene and shares the first 2 non-coding exons with NUP62.
CC       {ECO:0000305|PubMed:16029492}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB29253.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U70429; AAB51353.1; -; mRNA.
DR   EMBL; U70430; AAB51354.1; -; Genomic_RNA.
DR   EMBL; AF538041; AAM15529.1; -; Genomic_DNA.
DR   EMBL; AY442170; AAM15530.2; -; Genomic_DNA.
DR   EMBL; AY157537; AAO17038.1; -; Genomic_DNA.
DR   EMBL; AY157538; AAO17039.1; -; mRNA.
DR   EMBL; AY161348; AAO23118.1; -; Genomic_DNA.
DR   EMBL; AY178834; AAO65453.1; -; Genomic_DNA.
DR   EMBL; AY442343; AAS00457.1; -; Genomic_DNA.
DR   EMBL; AK014297; BAB29253.1; ALT_INIT; mRNA.
DR   EMBL; AK133082; BAE21502.1; -; mRNA.
DR   EMBL; AK150582; BAE29676.1; -; mRNA.
DR   EMBL; AK151030; BAE30047.1; -; mRNA.
DR   EMBL; AK151171; BAE30174.1; -; mRNA.
DR   EMBL; AK152538; BAE31293.1; -; mRNA.
DR   EMBL; AK172393; BAE42981.1; -; mRNA.
DR   EMBL; BC115960; AAI15961.1; -; mRNA.
DR   EMBL; U89428; AAC36534.1; -; Transcribed_RNA.
DR   EMBL; U89429; AAC36535.1; -; mRNA.
DR   CCDS; CCDS21217.1; -. [O09046-1]
DR   RefSeq; NP_001164495.1; NM_001171024.1.
DR   RefSeq; NP_034345.2; NM_010215.3.
DR   AlphaFoldDB; O09046; -.
DR   SMR; O09046; -.
DR   STRING; 10090.ENSMUSP00000113726; -.
DR   GlyCosmos; O09046; 3 sites, No reported glycans.
DR   GlyGen; O09046; 4 sites, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; O09046; -.
DR   MaxQB; O09046; -.
DR   PaxDb; 10090-ENSMUSP00000113726; -.
DR   ProteomicsDB; 294142; -. [O09046-1]
DR   ProteomicsDB; 294143; -. [O09046-2]
DR   DNASU; 14204; -.
DR   GeneID; 100328588; -.
DR   GeneID; 14204; -.
DR   KEGG; mmu:100328588; -.
DR   KEGG; mmu:14204; -.
DR   AGR; MGI:109552; -.
DR   CTD; 100328588; -.
DR   CTD; 259307; -.
DR   MGI; MGI:109552; Il4i1.
DR   eggNOG; KOG0029; Eukaryota.
DR   InParanoid; O09046; -.
DR   OrthoDB; 3597164at2759; -.
DR   BRENDA; 1.4.3.2; 3474.
DR   Reactome; R-MMU-8964208; Phenylalanine metabolism.
DR   UniPathway; UPA00332; -.
DR   BioGRID-ORCS; 100328588; 2 hits in 19 CRISPR screens.
DR   BioGRID-ORCS; 14204; 4 hits in 46 CRISPR screens.
DR   PRO; PR:O09046; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O09046; Protein.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:MGI.
DR   GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR   GO; GO:0046592; F:polyamine oxidase activity; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0009063; P:amino acid catabolic process; IBA:GO_Central.
DR   GO; GO:0009072; P:aromatic amino acid metabolic process; IDA:MGI.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; ISS:UniProtKB.
DR   GO; GO:0050868; P:negative regulation of T cell activation; ISS:UniProtKB.
DR   GO; GO:0002841; P:negative regulation of T cell mediated immune response to tumor cell; IDA:UniProtKB.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0002819; P:regulation of adaptive immune response; ISS:UniProtKB.
DR   GO; GO:0045577; P:regulation of B cell differentiation; IMP:UniProtKB.
DR   GO; GO:0006569; P:tryptophan catabolic process; ISS:UniProtKB.
DR   GO; GO:0019440; P:tryptophan catabolic process to indole-3-acetate; ISS:UniProtKB.
DR   GO; GO:0006572; P:tyrosine catabolic process; ISS:UniProtKB.
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   Adaptive immunity; Alternative promoter usage; Cytoplasmic vesicle;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Immunity; Lysosome;
KW   Oxidoreductase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..630
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000001711"
FT   REGION          532..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68..69
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         88..89
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         96
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         112..115
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         286
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         479
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         486..491
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         486..487
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..198
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   VAR_SEQ         1..5
FT                   /note="MAGLA -> MGARRAPQRPPCT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_017174"
FT   CONFLICT        12
FT                   /note="A -> V (in Ref. 2; AAO17038/AAO17039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="S -> L (in Ref. 2; AAO65453/AAS00457)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="M -> V (in Ref. 3; BAE30174/BAE31293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="R -> Q (in Ref. 2; AAO23118 and 3;
FT                   BAE21502/BAE29676/BAE30047/BAE30174/BAE31293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="Q -> R (in Ref. 3; BAE21502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        537
FT                   /note="E -> Q (in Ref. 3; BAE21502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        551
FT                   /note="P -> L (in Ref. 2; AAO17038/AAO17039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="A -> M (in Ref. 2; AAO17038/AAO17039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        598..630
FT                   /note="PSEHVQVHGEVIPEWHGHGGSGTPQMHRVGDHS -> LRSMYRCMGKSSLSG
FT                   MVMGDLAPRKCTEWGTTPNRKEEVSTQLLSQPSSGQTDHLH (in Ref. 3;
FT                   BAB29253)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   630 AA;  70191 MW;  A674C5D60D89A071 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 FYPARGEGSL LLASYTWSDA AAPFAGLSTD QTLRLVLQDV
     AALHGPVVFR LWDGRGVVKR WAEDPHSQGG FVVQPPLYGR EAEDYDWSAP FGRIYFAGEH
     TALPHGWVET AVKSGLRAAV RINNNYGYGE VDPQMMEHAY AEANYLDQYP EGERPEEQQA
     REEVSPDEQE PSHKHLLVET SPEGQQHAFV EAIPELQGHV FVETVPQEKG HAHQNIYPSE
     HVQVHGEVIP EWHGHGGSGT PQMHRVGDHS
//