Asl
entrez
59085
canonical
uniprot
P20673
canonical
ensembl
ENSRNOG00000000903
resolver
ensp
ENSRNOP00000089055
resolver
genesymbol
Asl
resolver
uniprot
A6J0N5
resolver
uniprot
Q4QRB8
resolver
uniprot
Q6AZ85
resolver
uniprot
Z4YND9
resolver
uniprot_entry
A6J0N5_RAT
resolver
uniprot_entry
ARLY_RAT
resolver
uniprot_sec
Q4QRB8
resolver
uniprot_sec
Q6AZ85
resolver
uniprot_sec
Z4YND9
resolver
activity_regulation
ACTIVITY REGULATION: Enzyme activity is regulated by acetylation. {ECO:0000250|UniProtKB:P04424}.
uniprot
proteins
amino_acid_sequence
MASESGKLWGGRFAGSVDPTMDKFNSSIAYDRHLWNVDLQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGIFKLYPNDEDIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTYSKLSTFLKVLIEAMVDRAEAECEVLFPGYTHLQRAQPIRWSHWILSHAVALTRDLERLKEVQKRINVLPLGSGAIAGNPLGVDREFLCAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYGTKEFNFVQLSDAYSTGSSLMPQKKNPDSLELIRSKARRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMTAVLQVATGVISTLQIHRENMAQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAVVVAEMKGVALNQLSLQELQTVSPLFSSDVNLVWDYSHSVEQYTALGGTAQSSVEWQISQVRALLQM
uniprot
proteins
ec_number
4.3.2.1
uniprot
proteins
function
FUNCTION: Catalyzes the reversible cleavage of L-argininosuccinate to fumarate and L-arginine, an intermediate step reaction in the urea cycle mostly providing for hepatic nitrogen detoxification into excretable urea as well as de novo L-arginine synthesis in nonhepatic tissues (By similarity). Essential regulator of intracellular and extracellular L-arginine pools. As part of citrulline-nitric oxide cycle, forms tissue-specific multiprotein complexes with argininosuccinate synthase ASS1, transport protein SLC7A1 and nitric oxide synthase NOS1, NOS2 or NOS3, allowing for cell-autonomous L-arginine synthesis while channeling extracellular L-arginine to nitric oxide synthesis pathway (By similarity). {ECO:0000250|UniProtKB:P04424}.
uniprot
proteins
mass_dalton
51550
uniprot
proteins
pathway_participation
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000250|UniProtKB:P04424}.; PATHWAY: Nitrogen metabolism; urea cycle; L-arginine and fumarate from (N(omega)-L-arginino)succinate: step 1/1. {ECO:0000250|UniProtKB:P04424}.
uniprot
proteins
post_translational_modification
PTM: Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TSA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity. {ECO:0000250|UniProtKB:P04424}.
uniprot
proteins
protein_family
Argininosuccinate lyase subfamily
uniprot
proteins
protein_family
Lyase 1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
2725197
uniprot
proteins
pubmed
2789519
uniprot
proteins
pubmed
2834354
uniprot
proteins
pubmed
8485149
uniprot
proteins
sequence_length
461
uniprot
proteins