ID   PIP22_PEA               Reviewed;         217 AA.
AC   O82711;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Kunitz-type trypsin inhibitor-like 2 protein;
DE   AltName: Full=Protease inhibitor from pea 2;
DE   Flags: Precursor;
GN   Name=PIP20-2; Synonyms=FUC2;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Martinez I.M.;
RL   Thesis (1998), University of Barcelona, Spain.
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=7559605; DOI=10.1074/jbc.270.42.24839;
RA   Augur C., Stiefel V., Darvill A., Albersheim P., Puigdomenech P.;
RT   "Molecular cloning and pattern of expression of an alpha-L-fucosidase gene
RT   from pea seedlings.";
RL   J. Biol. Chem. 270:24839-24843(1995).
RN   [3]
RP   FUNCTION REVISION.
RX   PubMed=12777048; DOI=10.1023/a:1023053101938;
RA   Tarrago T., Martinez I., Torrent M., Codina A., Giralt E., Puigdomenech P.,
RA   Ludevid D.;
RT   "The fuc1 gene product (20 kDa FUC1) of Pisum sativum has no alpha-L-
RT   fucosidase activity.";
RL   Plant Mol. Biol. 51:877-884(2003).
CC   -!- FUNCTION: Might act as a protease inhibitor involved in plant defense
CC       responses. {ECO:0000250, ECO:0000269|PubMed:12777048}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be an alpha-L-fucosidase.
CC       {ECO:0000305|PubMed:7559605}.
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DR   EMBL; AJ011398; CAA09607.1; -; Genomic_DNA.
DR   AlphaFoldDB; O82711; -.
DR   SMR; O82711; -.
DR   MEROPS; I03.025; -.
DR   PRIDE; O82711; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00178; STI; 1.
DR   InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR   InterPro; IPR002160; Prot_inh_Kunz-lg.
DR   PANTHER; PTHR33107; PTHR33107; 1.
DR   Pfam; PF00197; Kunitz_legume; 1.
DR   PRINTS; PR00291; KUNITZINHBTR.
DR   SMART; SM00452; STI; 1.
DR   SUPFAM; SSF50386; SSF50386; 1.
DR   PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..217
FT                   /note="Kunitz-type trypsin inhibitor-like 2 protein"
FT                   /id="PRO_5000064559"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        70..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        168..175
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  23638 MW;  EAD838A13B18ACA0 CRC64;
     MKPLSPLTLS FLLFVFITTL SLAFSNEDVE QVLDVNGKPI FPGGQYYILP AIRGPPGGGV
     RLGRTGDLTC PVTVLQDRRE VKNGLPVKFV IPGISPGIIF TGTPIEIEYT KKPNCAKSSK
     WLVFVDNVIQ KACVGIGGPE NYPGIQTLSG LFKIEKHESG FGYKLGFCIK GSPTCLDVGR
     FDNDEAGRRL NLTEHESFQV VFVEAEANDA EFIKSVV