OXLA_MOUSE
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 03-AUG-2022, entry version 163.
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 GlyGen; O09046; 3 sites.
DR PhosphoSitePlus; O09046; -.
DR MaxQB; O09046; -.
DR PaxDb; O09046; -.
DR PRIDE; O09046; -.
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 CTD; 100328588; -.
DR CTD; 259307; -.
DR MGI; MGI:109552; Il4i1.
DR eggNOG; KOG0029; Eukaryota.
DR InParanoid; O09046; -.
DR OrthoDB; 367611at2759; -.
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; 3 hits in 40 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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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:0009072; P:aromatic amino acid family metabolic process; IDA:MGI.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IBA:GO_Central.
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; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 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; BAE21502/
FT 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
