ACP2_ENTHI
ID ACP2_ENTHI Reviewed; 310 AA.
AC P36185;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Cysteine proteinase ACP2;
DE EC=3.4.22.-;
DE Flags: Precursor; Fragment;
GN Name=ACP2;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 90-97.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=8473498; DOI=10.1172/jci116359;
RA Reed S., Bouvier J., Pollack A.S., Engel J.C., Brown M., Hirata K., Que X.,
RA Eakin A., Hagblom P., Gillin F., McKerrow J.H.;
RT "Cloning of a virulence factor of Entamoeba histolytica. Pathogenic strains
RT possess a unique cysteine proteinase gene.";
RL J. Clin. Invest. 91:1532-1540(1993).
CC -!- FUNCTION: Cysteine proteinase present in pathogenic and in
CC nonpathogenic isolates.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; S58670; AAB26210.1; -; Genomic_DNA.
DR AlphaFoldDB; P36185; -.
DR SMR; P36185; -.
DR MEROPS; C01.050; -.
DR VEuPathDB; AmoebaDB:EHI5A_081530; -.
DR VEuPathDB; AmoebaDB:EHI7A_106950; -.
DR VEuPathDB; AmoebaDB:EHI8A_050360; -.
DR VEuPathDB; AmoebaDB:EHI_033710; -.
DR VEuPathDB; AmoebaDB:KM1_098010; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL <1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..89
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8473498"
FT /id="PRO_0000026184"
FT CHAIN 90..310
FT /note="Cysteine proteinase ACP2"
FT /id="PRO_0000026185"
FT ACT_SITE 114
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /evidence="ECO:0000250"
FT ACT_SITE 274
FT /evidence="ECO:0000250"
FT DISULFID 111..156
FT /evidence="ECO:0000250"
FT DISULFID 147..188
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 310 AA; 34204 MW; EC063B7B96D101BA CRC64;
AAGIRIASAI DFNTWASKNN KHFTAIEKLR RRAIFNMNAK FVDSFNKIGS FKLSVDGPFA
AMTNEEYRTL LKSKRTTEEN GQVKYLNIQA PESVDWRKEG KVTPLRDQAQ CGSCYTFGSL
AALEGRLLIE KGGDANTLDL SEEHMQCTRD NGNNGCNGGL GSNVYDYIIE HGVAKESDYP
YTGSDSTCKT NVKSFRKITG YTKVPRNNEA ELKAALSQGL LDVSIDVSSA KFQLYKSGAY
TDTKCKNNYF ALNHEVCAVG YGVVDGKECW IVRNSWGTSW GDKGYINMVI EGNTCGVATD
PLYPTGVQYL
