LACC1
entrez
144811
canonical
uniprot
Q8IV20
canonical
ensembl
ENSG00000179630
resolver
ensp
ENSP00000317619
resolver
ensp
ENSP00000391747
resolver
ensp
ENSP00000521350
resolver
ensp
ENSP00000521351
resolver
ensp
ENSP00000521352
resolver
ensp
ENSP00000521353
resolver
ensp
ENSP00000521354
resolver
ensp
ENSP00000521355
resolver
ensp
ENSP00000521356
resolver
ensp
ENSP00000521357
resolver
ensp
ENSP00000521358
resolver
ensp
ENSP00000521359
resolver
ensp
ENSP00000521360
resolver
ensp
ENSP00000521362
resolver
ensp
ENSP00000521363
resolver
ensp
ENSP00000590149
resolver
ensp
ENSP00000632541
resolver
ensp
ENSP00000632542
resolver
ensp
ENSP00000632545
resolver
ensp
ENSP00000632546
resolver
ensp
ENSP00000632547
resolver
ensp
ENSP00000632548
resolver
ensp
ENSP00000632549
resolver
ensp
ENSP00000632550
resolver
ensp
ENSP00000787308
resolver
ensp
ENSP00000787310
resolver
enst
ENST00000325686
resolver
enst
ENST00000441843
resolver
enst
ENST00000851291
resolver
enst
ENST00000851292
resolver
enst
ENST00000851293
resolver
enst
ENST00000851294
resolver
enst
ENST00000851295
resolver
enst
ENST00000851296
resolver
enst
ENST00000851297
resolver
enst
ENST00000851298
resolver
enst
ENST00000851299
resolver
enst
ENST00000851300
resolver
enst
ENST00000851301
resolver
enst
ENST00000851303
resolver
enst
ENST00000851304
resolver
enst
ENST00000920090
resolver
enst
ENST00000962482
resolver
enst
ENST00000962483
resolver
enst
ENST00000962486
resolver
enst
ENST00000962487
resolver
enst
ENST00000962488
resolver
enst
ENST00000962489
resolver
enst
ENST00000962490
resolver
enst
ENST00000962491
resolver
genesymbol
LACC1
resolver
genesymbol_syn
C13orf31
resolver
genesymbol_syn
FAMIN
resolver
hgnc
HGNC:26789
resolver
uniprot
A2A3Z6
resolver
uniprot
Q8N8X5
resolver
uniprot_entry
LACC1_HUMAN
resolver
uniprot_sec
A2A3Z6
resolver
uniprot_sec
Q8N8X5
resolver
amino_acid_sequence
MAEAVLIDLFGLKLNSQKNCHQTLLKTLNAVQYHHAAKAKFLCIMCCSNISYERDGEQDNCEIETSNGLSALLEEFEIVSCPSMAATLYTIKQKIDEKNLSSIKVIVPRHRKTLMKAFIDQLFTDVYNFEFEDLQVTFRGGLFKQSIEINVITAQELRGIQNEIETFLRSLPALRGKLTIITSSLIPDIFIHGFTTRTGGISYIPTLSSFNLFSSSKRRDPKVVVQENLRRLANAAGFNVEKFYRIKTHHSNDIWIMGRKEPDSYDGITTNQRGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEYGCSLEDIVVVLGPSVGPCCFTLPRESAEAFHNLHPACVQLFDSPNPCIDIRKATRILLEQGGILPQNIQDQNQDLNLCTSCHPDKFFSHVRDGLNFGTQIGFISIKE
uniprot
proteins
disease_involvement
DISEASE: Juvenile arthritis (JUVAR) [MIM:618795]: A rare, familial form of juvenile arthritis characterized by autosomal recessive inheritance and onset in early childhood of symmetric, chronic joint inflammation. It causes joint swelling, pain, stiffness and restricted joint movement. JUVAR has high clinical variability. Some patients exhibit systemic symptoms, including quotidian fever, erythematous rash, generalized lymphadenopathy, hepatomegaly, and/or splenomegaly. Others display polyarthritis without systemic inflammation. {ECO:0000269|PubMed:25220867, ECO:0000269|PubMed:27881174, ECO:0000269|PubMed:29717096, ECO:0000269|PubMed:30872671, ECO:0000269|PubMed:31811059, ECO:0000269|PubMed:31875558, ECO:0000269|PubMed:33606008, ECO:0000269|PubMed:35978195}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.4.2.1
uniprot
proteins
ec_number
2.4.2.28
uniprot
proteins
ec_number
3.5.4.4
uniprot
proteins
ec_number
4.3.3.-
uniprot
proteins
function
FUNCTION: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine, guanosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine, guanine and hypoxanthine (PubMed:31978345). Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (PubMed:31978345). Also has adenosine deaminase activity (PubMed:31978345). Acts as a regulator of innate immunity in macrophages by modulating the purine nucleotide metabolism, thereby regulating the metabolic function and bioenergetic state of macrophages (PubMed:31978345). Enables a purine nucleotide cycle between adenosine and inosine monophosphate and adenylosuccinate that prevents cytoplasmic acidification and balances the cytoplasmic-mitochondrial redox interface (PubMed:31978345). The purine nucleotide cycle consumes aspartate and releases fumarate in a manner involving fatty acid oxidation and ATP-citrate lyase activity (PubMed:31978345). Participates in pattern recognition receptor (PRR)-induced cytokines in macrophages: associates with the NOD2-signaling complex and promotes optimal NOD2-induced signaling, cytokine secretion and bacterial clearance (PubMed:28593945, PubMed:31875558). Localizes to the endoplasmic reticulum upon PRR stimulation of macrophages and associates with endoplasmic reticulum-stress sensors, promoting the endoplasmic reticulum unfolded protein response (UPR) (PubMed:31875558). Component of L-arginine metabolism in activated macrophages supporting anti-inflammatory and antibacterial macrophage effector functions. Cleaves L-citrulline, a product of L-arginine metabolized via NOS2, to yield isocyanate, a reactive carbonyl species-like cytotoxin, and L-ornithine, a precursor in polyamine biosynthesis. Through L-ornithine controls cellular polyamine pools likely triggering polyamine-mediated proinflammatory cytokine suppression and autophagy stimulation (PubMed:35978195). Directly interacts with components of autophagy machinery to regulate macrophage metabolism and bacterial phagocytosis. Acts downstream of the energy sensor AMP-activated protein kinase (AMPK) to promote autophagy associated to lipid droplets generation providing fatty acids for mitochondrial respiration (PubMed:33606008). Does not show laccase activity (PubMed:27959965, PubMed:31978345). {ECO:0000269|PubMed:27959965, ECO:0000269|PubMed:28593945, ECO:0000269|PubMed:31875558, ECO:0000269|PubMed:31978345, ECO:0000269|PubMed:33606008, ECO:0000269|PubMed:35978195}.
uniprot
proteins
mass_dalton
47780
uniprot
proteins
mutagenesis
MUTAGEN 52; /note="Y->A: Does not affect ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages; when associated with A-89 and A-265."; /evidence="ECO:0000269|PubMed:28593945"; MUTAGEN 89; /note="Y->A: Does not affect ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages; when associated with A-52 and A-265."; /evidence="ECO:0000269|PubMed:28593945"; MUTAGEN 247; /note="K->A: Decreased acetylation; does not affect ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages."; /evidence="ECO:0000269|PubMed:28593945"; MUTAGEN 249..250; /note="HH->AA: Impaired ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages."; /evidence="ECO:0000269|PubMed:28593945"; MUTAGEN 265; /note="Y->A: Does not affect ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages; when associated with A-52 and A-89."; /evidence="ECO:0000269|PubMed:28593945
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:28593945}.
uniprot
proteins
protein_family
PgeF/LACC1 family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
25220867
uniprot
proteins
pubmed
27478939
uniprot
proteins
pubmed
27881174
uniprot
proteins
pubmed
27959965
uniprot
proteins
pubmed
28593945
uniprot
proteins
pubmed
29717096
uniprot
proteins
pubmed
30872671
uniprot
proteins
pubmed
31811059
uniprot
proteins
pubmed
31875558
uniprot
proteins
pubmed
31978345
uniprot
proteins
pubmed
33606008
uniprot
proteins
pubmed
35978195
uniprot
proteins
sequence_length
430
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BZT9}. Nucleus {ECO:0000250|UniProtKB:Q8BZT9}. Endoplasmic reticulum {ECO:0000269|PubMed:31875558}. Peroxisome {ECO:0000269|PubMed:27478939, ECO:0000269|PubMed:27959965}. Note=Upon stimulation of the pattern-recognition receptor (PRR) NOD2, localizes to the endoplasmic reticulum. {ECO:0000269|PubMed:31875558}.
uniprot
proteins