ID   PFPA_ENTHI              Reviewed;          98 AA.
AC   P34095; Q24839;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Pore-forming peptide ameobapore A;
DE   AltName: Full=EH-APP;
DE   Flags: Precursor;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-46.
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=1396552; DOI=10.1002/j.1460-2075.1992.tb05432.x;
RA   Leippe M., Tannich E., Nickel R., van der Goot G., Pattus F.,
RA   Horstmann R.D., Mueller-Eberhard H.J.;
RT   "Primary and secondary structure of the pore-forming peptide of pathogenic
RT   Entamoeba histolytica.";
RL   EMBO J. 11:3501-3506(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=8274224; DOI=10.1089/dna.1993.12.925;
RA   Bruchhaus I., Leippe M., Lioutas C., Tannich E.;
RT   "Unusual gene organization in the protozoan parasite Entamoeba
RT   histolytica.";
RL   DNA Cell Biol. 12:925-933(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 22-46.
RX   PubMed=1881907; DOI=10.1073/pnas.88.17.7659;
RA   Leippe M., Ebel S., Schoenberger O.L., Horstmann R.D.,
RA   Mueller-Eberhard H.J.;
RT   "Pore-forming peptide of pathogenic Entamoeba histolytica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7659-7663(1991).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=7715451; DOI=10.1111/j.1365-2958.1994.tb01325.x;
RA   Leippe M., Andrae J., Nickel R., Tannich E., Mueller-Eberhard H.J.;
RT   "Amoebapores, a family of membranolytic peptides from cytoplasmic granules
RT   of Entamoeba histolytica: isolation, primary structure, and pore formation
RT   in bacterial cytoplasmic membranes.";
RL   Mol. Microbiol. 14:895-904(1994).
CC   -!- FUNCTION: Forms pores in the cytoplasmic membrane of host cells. Has
CC       antibacterial activity against M.luteus, no activity against E.coli.
CC       Implicated in the cytolytic activity of the parasite.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule.
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DR   EMBL; M83945; AAA29111.1; -; mRNA.
DR   EMBL; X70851; CAA50203.1; -; Genomic_DNA.
DR   PIR; S25283; S25283.
DR   PDB; 1OF9; NMR; -; A=22-98.
DR   PDBsum; 1OF9; -.
DR   AlphaFoldDB; P34095; -.
DR   SMR; P34095; -.
DR   TCDB; 1.C.35.1.1; the amoebapore (amoebapore) family.
DR   VEuPathDB; AmoebaDB:EHI5A_171330; -.
DR   VEuPathDB; AmoebaDB:EHI7A_127390; -.
DR   VEuPathDB; AmoebaDB:EHI8A_138030; -.
DR   VEuPathDB; AmoebaDB:EHI_159480; -.
DR   VEuPathDB; AmoebaDB:KM1_215020; -.
DR   OMA; CAKIHAC; -.
DR   EvolutionaryTrace; P34095; -.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR008138; SapB_2.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB_dom.
DR   Pfam; PF03489; SapB_2; 1.
DR   SMART; SM00741; SapB; 1.
DR   SUPFAM; SSF47862; SSF47862; 1.
DR   PROSITE; PS50015; SAP_B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:1396552,
FT                   ECO:0000269|PubMed:1881907"
FT   PEPTIDE         22..98
FT                   /note="Pore-forming peptide ameobapore A"
FT                   /id="PRO_0000031668"
FT   DOMAIN          22..98
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        26..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        29..92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        56..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   VARIANT         71
FT                   /note="L -> F"
FT   HELIX           26..39
FT                   /evidence="ECO:0007829|PDB:1OF9"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:1OF9"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:1OF9"
FT   HELIX           64..73
FT                   /evidence="ECO:0007829|PDB:1OF9"
FT   HELIX           75..84
FT                   /evidence="ECO:0007829|PDB:1OF9"
FT   HELIX           88..95
FT                   /evidence="ECO:0007829|PDB:1OF9"
SQ   SEQUENCE   98 AA;  10504 MW;  F9592FDC1FAC7FFA CRC64;
     MKAIVFVLIF AVAFAVTATH QGEILCNLCT GLINTLENLL TTKGADKVKD YISSLCNKAS
     GFIATLCTKV LDFGIDKLIQ LIEDKVDANA ICAKIHAC