CI2S_ARAAG
ID CI2S_ARAAG Reviewed; 94 AA.
AC C0HLT8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 25-MAY-2022, entry version 4.
DE RecName: Full=2S albumin-like cysteine protease inhibitor {ECO:0000305|PubMed:33266031};
DE Short=AaCI-2S {ECO:0000303|PubMed:33266031};
DE Flags: Fragments;
OS Araucaria angustifolia (Brazilian pine tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Araucariales;
OC Araucariaceae; Araucaria.
OX NCBI_TaxID=56992 {ECO:0000303|PubMed:33266031};
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Seed {ECO:0000303|PubMed:33266031};
RX PubMed=33266031; DOI=10.3390/plants9121676;
RA Sallai R.C., Salu B.R., Silva-Lucca R.A., Alves F.L., Napoleao T.H.,
RA Paiva P.M.G., da Silva Ferreira R., Sampaio M.U., Vilela Oliva M.L.;
RT "Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and
RT the Cysteine Protease Inhibitor AaCI-2S.";
RL Plants (Basel) 9:0-0(2020).
CC -!- FUNCTION: Cysteine protease inhibitor that likely functions in defense
CC against insects by inhibiting cysteine proteases in the midgut of
CC herbivore insects such as C.maculatus (PubMed:33266031). Selectively
CC inhibits cathepsin L, as well as papain, ficin and bromelain with lower
CC efficiency (PubMed:33266031). Shows antitumor activity, inhibiting the
CC growth of prostate cancer cell lines PC3 and DU145, and the gastric
CC cancer cell line Hs746T (PubMed:33266031). No activity against
CC cathepsin B or serine proteases (trypsin, human plasma kallikrein and
CC elastase) (PubMed:33266031). {ECO:0000269|PubMed:33266031}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is around 6. Stable from pH 2 to 10.
CC {ECO:0000269|PubMed:33266031};
CC Temperature dependence:
CC Thermostable. Active from 25 to 100 degrees Celsius. Retains 80% of
CC its maximal activity after heating for 2 hours at 100 degrees and
CC retains around 30% of its maximal activity after heating for 4 hours
CC at 100 degrees. {ECO:0000269|PubMed:33266031};
CC -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level).
CC {ECO:0000269|PubMed:33266031}.
CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC {ECO:0000305}.
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DR AlphaFoldDB; C0HLT8; -.
DR SMR; C0HLT8; -.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0002213; P:defense response to insect; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR CDD; cd00261; AAI_SS; 1.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR044723; AAI_SS_dom.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor.
FT CHAIN 1..94
FT /note="2S albumin-like cysteine protease inhibitor"
FT /id="PRO_0000452814"
FT DISULFID 12..35
FT /note="Interchain (between small and large chains)"
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT DISULFID 36..82
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT DISULFID 48..89
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT NON_CONS 23..24
FT /evidence="ECO:0000303|PubMed:33266031"
FT NON_CONS 61..62
FT /evidence="ECO:0000303|PubMed:33266031"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:33266031"
FT NON_TER 94
FT /evidence="ECO:0000303|PubMed:33266031"
SQ SEQUENCE 94 AA; 11012 MW; 09690E53C3B35F73 CRC64;
ERRCDPRRLS DCEDFVRGRS KGGRGEKECR LSERCCTELQ KMPRECRCEA VEGMYKEAER
KERGEGEQRQ RLERARALPG LCSIEPSYCE IRPS