ID   PHIG1_PHIGI             Reviewed;          23 AA.
AC   P84789;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Philibertain g 1;
DE            EC=3.4.22.-;
DE   AltName: Full=Philibertain g I;
DE   Flags: Fragment;
OS   Philibertia gilliesii (Milkweed) (Sarcostemma gilliesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Asclepiadoideae; Asclepiadeae;
OC   MOOG clade; Oxypetalinae; Philibertia.
OX   NCBI_TaxID=126767;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC   TISSUE=Fruit {ECO:0000269|PubMed:16328737};
RX   PubMed=16328737; DOI=10.1007/s10930-005-7640-0;
RA   Sequeiros C., Torres M.J., Trejo S.A., Esteves J.L., Natalucci C.L.,
RA   Lopez L.M.I.;
RT   "Philibertain g I, the most basic cysteine endopeptidase purified from the
RT   latex of Philibertia gilliesii Hook. et Arn. (Apocynaceae).";
RL   Protein J. 24:445-453(2005).
CC   -!- FUNCTION: Thiol protease.
CC   -!- ACTIVITY REGULATION: Strongly inhibited by the cysteine protease
CC       inhibitor E-64. Not inhibited by the serine protease inhibitor PMSF,
CC       the aspartic protease inhibitor pepstatin A, or by the metal ion
CC       chelator 1,10-phenanthroline. {ECO:0000269|PubMed:16328737}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.15 mM for PFLNA {ECO:0000269|PubMed:16328737};
CC       pH dependence:
CC         Optimum pH for casein is 7.6 and philibertain g 1 retains more than
CC         80% of maximum activity between pH 6.7 and pH 8.7, and 50% of maximum
CC         activity between pH 6.1 and pH 9.8. Optimum pH for PFLNA is 6.2-7.2
CC         and philibertain g I retains more than 80% of maximum activity
CC         between pH 5.8 and pH 7.8, and 50% of maximum activity between pH 5.2
CC         and pH 8.6. {ECO:0000269|PubMed:16328737};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P10056}.
CC   -!- MASS SPECTROMETRY: Mass=23530; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16328737};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P84789; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Thiol protease.
FT   CHAIN           1..>23
FT                   /note="Philibertain g 1"
FT                   /id="PRO_0000227534"
FT   DISULFID        22..?
FT                   /evidence="ECO:0000250|UniProtKB:P10056"
FT   NON_TER         23
FT                   /evidence="ECO:0000303|PubMed:16328737"
SQ   SEQUENCE   23 AA;  2518 MW;  CFCA161F65E3D98A CRC64;
     LPASVDWRKE GAVLPIRHQG QCG