ID   PRVN_THEPV              Reviewed;          36 AA.
AC   C0HJY2;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Peruvianin-1 {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000269|PubMed:26794967};
DE   AltName: Full=Peruvianin-I {ECO:0000303|PubMed:26794967};
DE   Flags: Fragment;
OS   Thevetia peruviana (Yellow oleander) (Cascabela thevetia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Plumerieae;
OC   Thevetiinae; Thevetia.
OX   NCBI_TaxID=52862;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, GLYCOSYLATION, AND MASS SPECTROMETRY.
RC   TISSUE=Latex {ECO:0000303|PubMed:26794967};
RX   PubMed=26794967; DOI=10.1007/s00425-016-2468-8;
RA   de Freitas C.D., da Cruz W.T., Silva M.Z., Vasconcelos I.M., Moreno F.B.,
RA   Moreira R.A., Monteiro-Moreira A.C., Alencar L.M., Sousa J.S., Rocha B.A.,
RA   Ramos M.V.;
RT   "Proteomic analysis and purification of an unusual germin-like protein with
RT   proteolytic activity in the latex of Thevetia peruviana.";
RL   Planta 243:1115-1128(2016).
CC   -!- FUNCTION: Cysteine protease able to degrade azocasein and benzoyl-
CC       arginine-beta-naphtylamide (BANA) in vitro.
CC       {ECO:0000269|PubMed:26794967}.
CC   -!- ACTIVITY REGULATION: Inhibited by iodoacetamide and trans-
CC       epoxysuccinyl-L-leucylamido(4-guanidino)butane (E-64) but not by
CC       phenylmethylsulfonyl fluoride (PMSF), pepstatin-A, ethylenediamine
CC       tetra acetic acid (EDTA) or ethylene glycol tetraacetic acid (EGTA).
CC       {ECO:0000269|PubMed:26794967}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=17.6 uM for azocasein (at pH 6 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:26794967};
CC         Vmax=46 nmol/sec/ug enzyme toward azocasein (at pH 6 and 37 degrees
CC         Celsius) {ECO:0000269|PubMed:26794967};
CC       pH dependence:
CC         Optimum pH is 5-6. {ECO:0000269|PubMed:26794967};
CC       Temperature dependence:
CC         Optimum temperature is 25-37 degrees Celsius.
CC         {ECO:0000269|PubMed:26794967};
CC   -!- SUBUNIT: Homohexamer, possibly consisting of a trimer of dimers.
CC       {ECO:0000269|PubMed:26794967}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:26794967}.
CC   -!- MASS SPECTROMETRY: Mass=20522; Method=Electrospray; Note=Monomer.;
CC       Evidence={ECO:0000269|PubMed:26794967};
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HJY2; -.
DR   SMR; C0HJY2; -.
DR   SABIO-RK; C0HJY2; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..>36
FT                   /note="Peruvianin-1"
FT                   /evidence="ECO:0000269|PubMed:26794967"
FT                   /id="PRO_0000435962"
FT   NON_TER         36
FT                   /evidence="ECO:0000303|PubMed:26794967"
SQ   SEQUENCE   36 AA;  3881 MW;  5B70B3B0C4392781 CRC64;
     ADPGPLQDFC LADLNSPLFI NGYPCRNPAL AISDDF