Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity.
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The study reports constitutive ARG1 expression in human granulocytes and azurophil-granule localization. Phagolysosomal arginine depletion is proposed as the antimicrobial mechanism.
"arginase I is localized in azurophil granules of neutrophils and constitutes a
novel antimicrobial effector pathway, likely through arginine depletion in the
phagolysosome"
Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response.
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The 1.29-A structure reveals the binuclear manganese cluster of human arginase I and the structural basis of catalysis and inhibition.
"The
ultrahigh-resolution structure of the human arginase I-ABH complex yields an
unprecedented view of the binuclear manganese cluster"
Suppression of T-cell functions by human granulocyte arginase.
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Arginase I released from human granulocytes accumulates extracellularly during inflammation and suppresses T-cell proliferation and cytokine synthesis by depleting arginine, downregulating the CD3-zeta chain.
"This T-cell phenotype is due to
arginase-mediated depletion of arginine in the T-cell environment, which leads
to CD3zeta chain down-regulation but does not alter T-cell viability"
Expression, purification, assay, and crystal structure of perdeuterated human arginase I.
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Human arginase I is a manganese metalloenzyme that catalyzes hydrolysis of L-arginine to L-ornithine and urea, confirmed by assay and X-ray structure.
"Arginase is a manganese metalloenzyme that catalyzes the hydrolysis of
l-arginine to yield l-ornithine and urea."
Proteomic characterization of the human sperm nucleus.
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The abstract reports 403 proteins from isolated human sperm nuclei and microscopy-based purity controls. The specific ARG1 protein-table entry has not been inspected.
"403
different proteins have been identified from the isolated sperm nuclei"
Binding of α,α-disubstituted amino acids to arginase suggests new avenues for inhibitor design.
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Arginase is a binuclear manganese metalloenzyme that hydrolyzes L-arginine to L-ornithine and urea; arginase I is cytosolic and predominantly hepatic, whereas arginase II is mitochondrial.
"Arginase I is a cytosolic enzyme found predominantly in the liver, and arginase II is a mitochondrial enzyme found at highest concentrations in the kidney."
Analysis of novel ARG1 mutations causing hyperargininemia and correlation with arginase I activity in erythrocytes.
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Hyperargininemia is caused by deficient arginase I activity encoded by ARG1; the R308 residue is important for assembly of the ARG1 homotrimer.
"Our study reinforced the role of
Arg308 residue for assembly of the ARG1 homotrimer."
CMTM6 maintains the expression of PD-L1 and regulates anti-tumour immunity.
Molecular cloning and nucleotide sequence of cDNA for human liver arginase.
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Human liver arginase (EC 3.5.3.1) catalyzes the last step of the urea cycle; cloned cDNA conferred arginase activity, and inherited deficiency causes argininemia.
"Arginase (EC 3.5.3.1) catalyzes the last step of the urea cycle in the liver of ureotelic animals."
Exocytosis of specific granule lumen proteins
Exocytosis of azurophil granule lumen proteins
arginine + H2O => ornithine + urea [ARG1]
ARG1 variants don't synthesize urea and ornithine