ACP1_ENTHI
ID ACP1_ENTHI Reviewed; 308 AA.
AC P36184; Q24831;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cysteine proteinase ACP1;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=ACP1; Synonyms=CP3;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8825217; DOI=10.1007/s004360050093;
RA Bruchhaus I., Tannich E.;
RT "A gene highly homologous to ACP1 encoding cysteine proteinase 3 in
RT Entamoeba histolytica is present and expressed in E. dispar.";
RL Parasitol. Res. 82:189-192(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-308, AND PROTEIN SEQUENCE OF
RP 93-100.
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-274.
RX PubMed=2406590; DOI=10.1016/0166-6851(90)90002-4;
RA Eakin A.E., Bouvier J., Sakanari J.A., Craik C.S., McKerrow J.H.;
RT "Amplification and sequencing of genomic DNA fragments encoding cysteine
RT proteases from protozoan parasites.";
RL Mol. Biochem. Parasitol. 39:1-8(1990).
CC -!- FUNCTION: Involved in pathogenicity. Its presence correlates with
CC increased proteinase expression and activity in pathogenic isolates.
CC Probably involved in tissue invasion.
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; X87214; CAA60673.1; -; mRNA.
DR EMBL; S58669; AAB26209.2; -; Genomic_DNA.
DR EMBL; M27307; AAA29094.1; -; Genomic_DNA.
DR PIR; C44938; C44938.
DR AlphaFoldDB; P36184; -.
DR SMR; P36184; -.
DR STRING; 5759.rna_EHI_159610-1; -.
DR MEROPS; C01.050; -.
DR MEROPS; I29.003; -.
DR VEuPathDB; AmoebaDB:EHI5A_081680; -.
DR VEuPathDB; AmoebaDB:EHI7A_046640; -.
DR VEuPathDB; AmoebaDB:EHI8A_045840; -.
DR VEuPathDB; AmoebaDB:EHI_159610; -.
DR VEuPathDB; AmoebaDB:KM1_093780; -.
DR eggNOG; KOG1543; Eukaryota.
DR OMA; YGNRGCN; -.
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..13
FT /evidence="ECO:0000255"
FT PROPEP 14..92
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8473498"
FT /id="PRO_0000026182"
FT CHAIN 93..308
FT /note="Cysteine proteinase ACP1"
FT /id="PRO_0000026183"
FT ACT_SITE 115
FT /evidence="ECO:0000250"
FT ACT_SITE 251
FT /evidence="ECO:0000250"
FT ACT_SITE 271
FT /evidence="ECO:0000250"
FT DISULFID 112..153
FT /evidence="ECO:0000250"
FT DISULFID 146..186
FT /evidence="ECO:0000250"
FT CONFLICT 61
FT /note="A -> G (in Ref. 2; AAB26209)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..157
FT /note="GGH -> RG (in Ref. 2; AAB26209)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..270
FT /note="IR -> VK (in Ref. 3; AAA29094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 33851 MW; D08A0F6A84D89316 CRC64;
MFALILFVSL ACANEVAFKQ WAATHNKVFA NRAEYLYRFA VFLDNKKFVE ANANTELNVF
ADMTHEEFIQ THLGMTYEVP ETTSNVKAAV KAAPESVDWR SIMNPAKDQG QCGSCWTFCT
TAVLEGRVNK DLGKLYSFSE QQLVDCDASD NGCEGGHPSN SLKFIQENNG LGLESDYPYK
AVAGTCKKVK NVATVTGSRR VTDGSETGLQ TIIAENGPVA VGMDASRPSF QLYKKGTIYS
DTKCRSRMMN HCVTAVGYGS NSNGKYWIIR NSWGTSWGDA GYFLLARDSN NMCGIGRDSN
YPTGVKLI
