IL4I1
entrez
259307
canonical
uniprot
Q96RQ9
canonical
ensembl
ENSG00000104951
resolver
ensp
ENSP00000342557
resolver
ensp
ENSP00000375702
resolver
ensp
ENSP00000472474
resolver
genesymbol
IL4I1
resolver
genesymbol_syn
FIG1
resolver
hgnc
HGNC:19094
resolver
uniprot
Q1WMJ3
resolver
uniprot
Q4GZN1
resolver
uniprot
Q4GZN2
resolver
uniprot
Q6P2Q3
resolver
uniprot
Q8TEM5
resolver
uniprot
Q96RQ8
resolver
uniprot_entry
OXLA_HUMAN
resolver
uniprot_sec
Q1WMJ3
resolver
uniprot_sec
Q4GZN1
resolver
uniprot_sec
Q4GZN2
resolver
uniprot_sec
Q6P2Q3
resolver
uniprot_sec
Q8TEM5
resolver
uniprot_sec
Q96RQ8
resolver
activity_regulation
ACTIVITY REGULATION: L-amino-acid oxidase activity toward phenylalanine (Phe) is specfically inhibited by a number of Phe derivatives, such as Cp3 (ethyl 3-(2,6-dichlorophenyl)-2-(piperidin-1-yl)propanoate) or Cp2-SO4 (PubMed:31812258). Cp3 is a very potent inhibitor for activity toward phenylalanine but is toxic (PubMed:31812258). In contrast, Cp2-SO4 is less efficient but not toxic and is able to reverse immunosuppressive action of IL4I1 in vitro (PubMed:31812258). {ECO:0000269|PubMed:31812258}.
uniprot
proteins
amino_acid_sequence
MAPLALHLLVLVPILLSLVASQDWKAERSQDPFEKCMQDPDYEQLLKVVTWGLNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLGLNLTKFTQYDKNTWTEVHEVKLRNYVVEKVPEKLGYALRPQEKGHSPEDIYQMALNQALKDLKALGCRKAMKKFERHTLLEYLLGEGNLSRPAVQLLGDVMSEDGFFYLSFAEALRAHSCLSDRLQYSRIVGGWDLLPRALLSSLSGLVLLNAPVVAMTQGPHDVHVQIETSPPARNLKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEHIEGGHSNTDRPSRMIFYPPPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALHGPVVRQLWDGTGVVKRWAEDQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTAYPHGWVETAVKSALRAAIKINSRKGPASDTASPEGHASDMEGQGHVHGVASSPSHDLAKEEGSHPPVQGQLSLQNTTHTRTSH
uniprot
proteins
ec_number
1.4.3.2
uniprot
proteins
ec_number
1.4.3.25
uniprot
proteins
function
FUNCTION: Secreted L-amino-acid oxidase that acts as a key immunoregulator (PubMed:17356132, PubMed:32818467, PubMed:32866000). Has preference for L-aromatic amino acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and indole-3-pyruvic acid (I3P), respectively (PubMed:17356132, PubMed:32818467, PubMed:32866000). Also has weak L-arginine oxidase activity (PubMed:26673964). Acts as a negative regulator of anti-tumor immunity by mediating Trp degradation via an indole pyruvate pathway that activates the transcription factor AHR (PubMed:32818467, PubMed:32866000). IL4I1-mediated Trp catabolism generates I3P, giving rise to indole metabolites (indole-3-acetic acid (IAA) and indole-3-aldehyde (I3A)) and kynurenic acid, which act as ligands for AHR, a ligand-activated transcription factor that plays important roles in immunity and cancer (PubMed:32818467, PubMed:32866000). AHR activation by indoles following IL4I1-mediated Trp degradation enhances tumor progression by promoting cancer cell motility and suppressing adaptive immunity (PubMed:32818467). Also has an immunoregulatory function in some immune cells, probably by mediating Trp degradation and promoting downstream AHR activation: inhibits T-cell activation and proliferation, promotes the differentiation of naive CD4(+) T-cells into FOXP3(+) regulatory T-cells (Treg) and regulates the development and function of B-cells (PubMed:17356132, PubMed:25446972, PubMed:25778793, PubMed:28891065). Also regulates M2 macrophage polarization by inhibiting T-cell activation (By similarity). Also has antibacterial properties by inhibiting growth of Gram negative and Gram positive bacteria through the production of NH4(+) and H2O2 (PubMed:23355881). {ECO:0000250|UniProtKB:O09046, ECO:0000269|PubMed:17356132, ECO:0000269|PubMed:23355881, ECO:0000269|PubMed:25446972, ECO:0000269|PubMed:25778793, ECO:0000269|PubMed:26673964, ECO:0000269|PubMed:28891065, ECO:0000269|PubMed:32818467, ECO:0000269|PubMed:32866000}.
uniprot
proteins
mass_dalton
62881
uniprot
proteins
mutagenesis
MUTAGEN 481; /note="E->A: Abolished L-amino-acid oxidase activity."; /evidence="ECO:0000269|PubMed:17356132
uniprot
proteins
pathway_participation
PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate pathway. {ECO:0000269|PubMed:32818467, ECO:0000269|PubMed:32866000}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:17356132}.
uniprot
proteins
protein_family
FIG1 subfamily
uniprot
proteins
protein_family
Flavin monoamine oxidase family
uniprot
proteins
pubmed
12031486
uniprot
proteins
pubmed
12446450
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16029492
uniprot
proteins
pubmed
17356132
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19436310
uniprot
proteins
pubmed
23355881
uniprot
proteins
pubmed
25446972
uniprot
proteins
pubmed
25767141
uniprot
proteins
pubmed
25778793
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26673964
uniprot
proteins
pubmed
28891065
uniprot
proteins
pubmed
31812258
uniprot
proteins
pubmed
32818467
uniprot
proteins
pubmed
32866000
uniprot
proteins
sequence_length
567
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17356132, ECO:0000269|PubMed:28891065, ECO:0000269|PubMed:32818467}. Lysosome {ECO:0000250|UniProtKB:O09046}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:25767141}. Note=Secreted at the immunological synapse. {ECO:0000269|PubMed:28891065}.
uniprot
proteins