HPI_HEVBR
ID HPI_HEVBR Reviewed; 70 AA.
AC Q6XNP7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Protease inhibitor HPI;
DE AltName: Full=HbPI1;
DE AltName: Full=Protease inhibitor 1;
GN Name=PI1 {ECO:0000312|EMBL:AAP46156.1};
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP46156.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Latex {ECO:0000269|PubMed:15010614};
RX PubMed=15010614; DOI=10.1023/b:plan.0000019119.66643.5d;
RA Ko J.-H., Chow K.-S., Han K.-H.;
RT "Transcriptome analysis reveals novel features of the molecular events
RT occurring in the laticifers of Hevea brasiliensis (para rubber tree).";
RL Plant Mol. Biol. 53:479-492(2003).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-70, FUNCTION, MASS SPECTROMETRY, GLUTATHIONYLATION AT
RP CYS-5, DISULFIDE BOND, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT
RP ALA-2.
RC TISSUE=Latex {ECO:0000269|PubMed:16438995};
RX PubMed=16438995; DOI=10.1016/j.phytochem.2005.12.016;
RA Sritanyarat W., Pearce G., Siems W.F., Ryan C.A., Wititsuwannakul R.,
RA Wititsuwannakul D.;
RT "Isolation and characterization of isoinhibitors of the potato protease
RT inhibitor I family from the latex of the rubber trees, Hevea
RT brasiliensis.";
RL Phytochemistry 67:1644-1650(2006).
CC -!- FUNCTION: Inhibitor of serine proteases, strongly inhibits subtilisin A
CC and weakly inhibits trypsin. Does not inhibit chymotrypsin, papain,
CC pepsin, pronase E, protease type XIII and thermolysin. HPI-1 inhibits
CC subtilisin A with an Ki of 0.21 nM. HPI-2a inhibits subtilisin A with
CC an Ki of 0.08 nM. HPI-2b inhibits subtilisin A with an Ki of 0.1 nM.
CC {ECO:0000269|PubMed:16438995}.
CC -!- SUBUNIT: Monomer and homodimer; disulfide-linked.
CC {ECO:0000269|PubMed:16438995}.
CC -!- PTM: Occurs in 3 forms that differ in the modification of Cys-5, HPI-1
CC forms a homodimer through a disulfide bond, HPI-2a is modified by
CC glutathionylation, and HPI-2b is covalently modified by addition of an
CC unidentified adduct but not by a disulfide linkage.
CC {ECO:0000269|PubMed:16438995}.
CC -!- MASS SPECTROMETRY: Mass=14894; Method=MALDI; Note=HPI-1 homodimer.;
CC Evidence={ECO:0000269|PubMed:16438995};
CC -!- MASS SPECTROMETRY: Mass=7758; Method=MALDI; Note=HPI-2a.;
CC Evidence={ECO:0000269|PubMed:16438995};
CC -!- MASS SPECTROMETRY: Mass=7566; Method=MALDI; Note=HPI-2b.;
CC Evidence={ECO:0000269|PubMed:16438995};
CC -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC protease inhibitor) family. {ECO:0000255}.
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DR EMBL; AY221985; AAP46156.1; -; mRNA.
DR AlphaFoldDB; Q6XNP7; -.
DR SMR; Q6XNP7; -.
DR Allergome; 11621; Hev b 15.
DR Allergome; 8756; Hev b SPI.
DR MEROPS; I13.008; -.
DR iPTMnet; Q6XNP7; -.
DR OrthoDB; 1582946at2759; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEA:InterPro.
DR InterPro; IPR000864; Prot_inh_pot1.
DR InterPro; IPR036354; Prot_inh_pot1_sf.
DR PANTHER; PTHR33091; PTHR33091; 1.
DR Pfam; PF00280; potato_inhibit; 1.
DR PRINTS; PR00292; POTATOINHBTR.
DR SUPFAM; SSF54654; SSF54654; 1.
DR PROSITE; PS00285; POTATO_INHIBITOR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Disulfide bond; Glutathionylation;
KW Protease inhibitor; Serine protease inhibitor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16438995"
FT CHAIN 2..70
FT /note="Protease inhibitor HPI"
FT /evidence="ECO:0000269|PubMed:16438995"
FT /id="PRO_0000273520"
FT SITE 46..47
FT /note="Reactive bond"
FT /evidence="ECO:0000250|UniProtKB:P82381"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:16438995"
FT MOD_RES 5
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:16438995"
FT DISULFID 5
FT /note="Interchain; alternate"
FT /evidence="ECO:0000269|PubMed:16438995"
FT CONFLICT 9..10
FT /note="NS -> DA (in Ref. 1; AAP46156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 70 AA; 7547 MW; A79F2ADDE8CD2E81 CRC64;
MASQCPVKNS WPELVGTNGD IAAGIIQTEN ANVKAIVVKE GLPITQDLNF NRVRVFVDEN
RVVTQVPAIG
