IPRB_SAGSA
ID IPRB_SAGSA Reviewed; 181 AA.
AC P07479;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Proteinase inhibitor B;
DE AltName: Full=Double-headed proteinase inhibitor B;
DE Short=API-B;
DE Flags: Precursor;
OS Sagittaria sagittifolia (Arrowhead).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Alismataceae; Sagittaria.
OX NCBI_TaxID=4451;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8468321; DOI=10.1093/oxfordjournals.jbchem.a124019;
RA Xu W., Tao W., Gong Z., Chi C.-W.;
RT "cDNA and genomic structures of arrowhead proteinase inhibitors.";
RL J. Biochem. 113:153-158(1993).
RN [2]
RP PROTEIN SEQUENCE OF 25-174.
RX PubMed=1618743; DOI=10.1093/oxfordjournals.jbchem.a123792;
RA Yang H.-L., Luo R.-S., Wang L.-X., Zhu D.-X., Chi C.-W.;
RT "Primary structure and disulfide bridge location of arrowhead double-headed
RT proteinase inhibitors.";
RL J. Biochem. 111:537-545(1992).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 25-174.
RC TISSUE=Root;
RX PubMed=3907662; DOI=10.1515/bchm3.1985.366.2.879;
RA Chi C.-W., Zhu D.-X., Lin N.-Q., Xu L.-X., Tan F.-L., Wang L.-X.;
RT "The complete amino-acid sequence of the proteinase inhibitor B from the
RT root of the arrowhead (Sagittaria sagittifolia L.).";
RL Biol. Chem. Hoppe-Seyler 366:879-885(1985).
RN [4]
RP PRELIMINARY PROTEIN SEQUENCE OF 25-174.
RC TISSUE=Root;
RA Chi C.-W., Zhu D.-X., Lin N.-Q., Xu L.-X., Tan F.-L., Wang L.-X.;
RT "The complete amino-acid sequence of the arrowhead proteinase inhibitor
RT B.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 18:156-163(1986).
CC -!- FUNCTION: Possesses two reactive sites. Inhibits two molecules of
CC trypsin simultaneously. Inhibits efficiently kallikrein, but
CC chymotrypsin weakly.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.2; Type=Miscellaneous discrepancy; Note=Very different preliminary sequence.; Evidence={ECO:0000305};
CC Sequence=Ref.3; Type=Miscellaneous discrepancy; Note=Very different preliminary sequence.; Evidence={ECO:0000305};
CC Sequence=Ref.4; Type=Miscellaneous discrepancy; Note=Very different preliminary sequence.; Evidence={ECO:0000305};
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DR EMBL; D13820; BAA02973.1; -; Genomic_DNA.
DR PIR; JX0247; JX0247.
DR AlphaFoldDB; P07479; -.
DR SMR; P07479; -.
DR MEROPS; I03.007; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR016308; Prot_inh_API-A/B.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 2.
DR Pfam; PF00197; Kunitz_legume; 1.
DR PIRSF; PIRSF001653; API-B; 1.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:1618743"
FT CHAIN 25..181
FT /note="Proteinase inhibitor B"
FT /id="PRO_0000016898"
FT SITE 68..69
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000305"
FT SITE 100..101
FT /note="Reactive bond"
FT /evidence="ECO:0000305"
FT DISULFID 67..113
FT DISULFID 134..143
FT DISULFID 136..139
FT CONFLICT 61
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="S -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 19174 MW; D21AB5C7BB3412DF CRC64;
MAASNALLLI SGALLISLAV LCQGDPVVDS DGDAVQLNLG GRYPLYTIES AAIGFHGGLS
TLHKDVCKSY VYEAPETDRG LPVSFSASAT SEPVMQLGSR YKFSFLMPVP RICDTAWSVG
KSTEETGVYK LAACSCEFCK IACPEVGSFN VNGKTLLGIG GEHFTVRFHK SDALAMKTAP
Q