Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.1) (EC 3.1.2.11) (EC 3.1.2.2) (EC 3.1.2.3) (EC 3.1.2.5) (Choloyl-coenzyme A thioesterase) (EC 3.1.2.27) (HIV-Nef-associated acyl-CoA thioesterase) (Peroxisomal acyl-CoA thioesterase 2) (PTE-2) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1) (Thioesterase II) (hACTE-III) (hACTEIII) (hTE)
1_MSSPQ 6_ APEDG 11_ QGCGD 16_ RGDPP 21_ GDLRS 26_ VLVTT 31_ VLNLE 36_ PLDED 41_ LFRGR 46_ HYWVP 51_ AKRLF 56_ GGQIV 61_ GQALV 66_ AAAKS 71_ VSEDV 76_ HVHSL 81_ HCYFV 86_ RAGDP 91_ KLPVL 96_ YQVER 101_ TRTGS 106_ SFSVR 111_ SVKAV 116_ QHGKP 121_ IFICQ 126_ ASFQQ 131_ AQPSP 136_ MQHQF 141_ SMPTV 146_ PPPEE 151_ LLDCE 156_ TLIDQ 161_ YLRDP 166_ NLQKR 171_ YPLAL 176_ NRIAA 181_ QEVPI 186_ EIKPV 191_ NPSPL 196_ SQLQR 201_ MEPKQ 206_ MFWVR 211_ ARGYI 216_ GEGDM 221_ KMHCC 226_ VAAYI 231_ SDYAF 236_ LGTAL 241_ LPHQW 246_ QHKVH 251_ FMVSL 256_ DHSMW 261_ FHAPF 266_ RADHW 271_ MLYEC 276_ ESPWA 281_ GGSRG 286_ LVHGR 291_ LWRQD 296_ GVLAV 301_ TCAQE 306_ GVIRV 311_KPQVS
1: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:15194431, PubMed:9153233, PubMed:9299485). 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:9153233, PubMed:9299485). 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 (PubMed:15194431)
2: (Microbial infection) May mediate Nef-induced down-regulation of CD4 cell-surface expression (PubMed:9153233)