Q8VHK0
uniprot
Q8VHK0
canonical
activity_regulation
ACTIVITY REGULATION: Inhibited by CoASH (IC(50)=10-15 uM). Also inhibited by cysteine-reactive agents. {ECO:0000250|UniProtKB:P58137}.
uniprot
proteins
amino_acid_sequence
MSKPEDLGDANGDADRGDLSGDLRSVLVTSVLNLEPLDEDLYRGRHYWVPTSQRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKVPVLYHVERTRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSPLQHQFSMPTVPPPEELLDHEALIDQYLRDPNLHEKYRVGLNRIAAREVPIEIKLVNPPALNQLQTLEPKQMFWVRARGYIGEGDIKMHCCVAAYISDYAFLGTALLPHQSKYKVNFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRSKPRVSESKL
uniprot
proteins
ec_number
3.1.2.1
uniprot
proteins
ec_number
3.1.2.11
uniprot
proteins
ec_number
3.1.2.2
uniprot
proteins
ec_number
3.1.2.27
uniprot
proteins
ec_number
3.1.2.3
uniprot
proteins
ec_number
3.1.2.5
uniprot
proteins
function
FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:11785945). Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains (PubMed:11785945). Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT) (By similarity). Is also able to hydrolyze CoA esters of dicarboxylic acids (By similarity). It is involved in the metabolic regulation of peroxisome proliferation (By similarity). {ECO:0000250|UniProtKB:O14734, ECO:0000250|UniProtKB:P58137, ECO:0000269|PubMed:11785945}.
uniprot
proteins
mass_dalton
36003
uniprot
proteins
protein_family
C/M/P thioester hydrolase family
uniprot
proteins
pubmed
10092594
uniprot
proteins
pubmed
11785945
uniprot
proteins
sequence_length
320
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:11785945}. Note=Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded. {ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:11785945}.
uniprot
proteins