ID   NIVU2_EUPNI             Reviewed;         157 AA.
AC   P86837;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 2.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Cysteine protease Nivulian-2;
DE   AltName: Full=Nivulian-II {ECO:0000303|Ref.1};
DE            EC=3.4.22.-;
DE   Flags: Fragments;
OS   Euphorbia nivulia (Leafy milk hedge) (Euphorbia varians).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Euphorbioideae; Euphorbieae;
OC   Euphorbia; Euphorbia subgen. Euphorbia; Euphorbia sect. Euphorbia.
OX   NCBI_TaxID=334690;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-12, FUNCTION, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Latex {ECO:0000269|Ref.1};
RA   Badgujar S.B., Mahajan R.T.;
RT   "Characterization of milk clotting cysteine protease of Euphorbia nivulia
RT   Buch.-Ham. latex.";
RL   Green Farming 1:645-648(2010).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Badgujar S.B., Mahajan R.T.;
RT   "Peptide mass fingerprinting and N-terminal amino acid sequencing of
RT   glycosylated cysteine protease of Euphorbia nivulia Buch.-Ham.";
RL   J. Amino Acids 2013:0-0(2013).
CC   -!- FUNCTION: Cysteine protease inducing milk clotting by cleaving casein.
CC       {ECO:0000269|Ref.1}.
CC   -!- ACTIVITY REGULATION: Inhibited by HgCl(2), iodoacetamide (IAA) and, to
CC       a far lesser extent, by PMSF, Pepstatin A and EDTA.
CC       {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.3. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: Mass=43670.848; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 3.4,
CC       its MW is: 43.67 kDa.
CC   -!- SIMILARITY: Belongs to the intron maturase 2 family. MatK subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P86837; -.
DR   GO; GO:0009507; C:chloroplast; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR002866; Maturase_MatK.
DR   InterPro; IPR024942; Maturase_MatK_N.
DR   PANTHER; PTHR34811; PTHR34811; 2.
DR   Pfam; PF01824; MatK_N; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..>157
FT                   /note="Cysteine protease Nivulian-2"
FT                   /id="PRO_0000408761"
FT   NON_CONS        12..13
FT                   /evidence="ECO:0000305"
FT   NON_CONS        36..37
FT                   /evidence="ECO:0000305"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000305"
FT   NON_CONS        74..75
FT                   /evidence="ECO:0000305"
FT   NON_CONS        83..84
FT                   /evidence="ECO:0000305"
FT   NON_CONS        109..110
FT                   /evidence="ECO:0000305"
FT   NON_CONS        125..126
FT                   /evidence="ECO:0000305"
FT   NON_CONS        141..142
FT                   /evidence="ECO:0000305"
FT   NON_TER         157
SQ   SEQUENCE   157 AA;  18436 MW;  03190EDD6BA60F68 CRC64;
     DFPPNTCCCI CCFIDRMYQQ NHFIISSNSN SSNQNKLVSS LEGKVWVQDV PSLHLLRFFL
     YEYRNWNSFI TPKKCESMFV FLRDPFIHYV RYQAKSFLAA RGTPLMMNKS QMLENSFLID
     IAINKAKFCN ALGHPISKPV RVWYLDIIRI NDLVNHD