VKT1_STIHL
ID VKT1_STIHL Reviewed; 55 AA.
AC P31713;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=PI-stichotoxin-She2a {ECO:0000303|PubMed:22683676};
DE Short=PI-SHTX-She2a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Kunitz-type protease inhibitor ShPI-I {ECO:0000303|PubMed:9027993};
OS Stichodactyla helianthus (Sun anemone) (Stoichactis helianthus).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Stichodactylidae; Stichodactyla.
OX NCBI_TaxID=6123;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RX PubMed=9027993; DOI=10.1016/s0041-0101(96)00114-6;
RA Delfin J., Martinez I., Antuch W., Morera V., Gonzalez Y., Rodriguez R.,
RA Marquez M., Saroyan A., Larionova N., Diaz J., Padron G., Chavez M.;
RT "Purification, characterization and immobilization of proteinase inhibitors
RT from Stichodactyla helianthus.";
RL Toxicon 34:1367-1376(1996).
RN [2]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
RN [3]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=8462542; DOI=10.1111/j.1432-1033.1993.tb17705.x;
RA Antuch W., Berndt K.D., Chavez M.A., Delfin J., Wuethrich K.;
RT "The NMR solution structure of a Kunitz-type proteinase inhibitor from the
RT sea anemone Stichodactyla helianthus.";
RL Eur. J. Biochem. 212:675-684(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=23143234; DOI=10.1107/s1744309112039085;
RA Garcia-Fernandez R., Pons T., Meyer A., Perbandt M., Gonzalez-Gonzalez Y.,
RA Gil D., de Los Angeles Chavez M., Betzel C., Redecke L.;
RT "Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the
RT marine invertebrate Stichodactyla helianthus.";
RL Acta Crystallogr. F 68:1289-1293(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH TRYPSIN, FUNCTION,
RP REACTIVE BOND, AND DISULFIDE BONDS.
RX PubMed=22975140; DOI=10.1016/j.jsb.2012.08.009;
RA Garcia-Fernandez R., Pons T., Perbandt M., Valiente P.A., Talavera A.,
RA Gonzalez-Gonzalez Y., Rehders D., Chavez M.A., Betzel C., Redecke L.;
RT "Structural insights into serine protease inhibition by a marine
RT invertebrate BPTI Kunitz-type inhibitor.";
RL J. Struct. Biol. 180:271-279(2012).
CC -!- FUNCTION: Active against serine, cysteine, and aspartic proteases. Can
CC bind vertebrate trypsin and chymotrypsin. {ECO:0000269|PubMed:22975140,
CC ECO:0000269|PubMed:9027993}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:9027993}. Nematocyst
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=6110.60; Method=FAB;
CC Evidence={ECO:0000269|PubMed:9027993};
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2
CC potassium channel toxin subfamily. {ECO:0000305}.
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DR PIR; S30332; S30332.
DR PDB; 1SHP; NMR; -; A=1-55.
DR PDB; 3M7Q; X-ray; 1.70 A; B=1-55.
DR PDB; 3OFW; X-ray; 2.50 A; A=1-54.
DR PDB; 3T62; X-ray; 2.00 A; D/E/F=1-54.
DR PDB; 3UOU; X-ray; 2.00 A; B=1-55.
DR PDBsum; 1SHP; -.
DR PDBsum; 3M7Q; -.
DR PDBsum; 3OFW; -.
DR PDBsum; 3T62; -.
DR PDBsum; 3UOU; -.
DR AlphaFoldDB; P31713; -.
DR SMR; P31713; -.
DR EvolutionaryTrace; P31713; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; KU; 1.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartic protease inhibitor; Direct protein sequencing;
KW Disulfide bond; Nematocyst; Protease inhibitor; Secreted;
KW Serine protease inhibitor.
FT CHAIN 1..55
FT /note="PI-stichotoxin-She2a"
FT /evidence="ECO:0000269|PubMed:9027993"
FT /id="PRO_0000155419"
FT DOMAIN 3..53
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 13..14
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000269|PubMed:22975140"
FT DISULFID 3..53
FT /evidence="ECO:0000269|PubMed:22975140,
FT ECO:0000269|PubMed:23143234, ECO:0000269|PubMed:8462542,
FT ECO:0000312|PDB:1SHP, ECO:0000312|PDB:3M7Q,
FT ECO:0000312|PDB:3OFW, ECO:0000312|PDB:3T62,
FT ECO:0000312|PDB:3UOU"
FT DISULFID 12..36
FT /evidence="ECO:0000269|PubMed:22975140,
FT ECO:0000269|PubMed:23143234, ECO:0000269|PubMed:8462542,
FT ECO:0000312|PDB:1SHP, ECO:0000312|PDB:3M7Q,
FT ECO:0000312|PDB:3OFW, ECO:0000312|PDB:3T62,
FT ECO:0000312|PDB:3UOU"
FT DISULFID 28..49
FT /evidence="ECO:0000269|PubMed:22975140,
FT ECO:0000269|PubMed:23143234, ECO:0000269|PubMed:8462542,
FT ECO:0000312|PDB:1SHP, ECO:0000312|PDB:3M7Q,
FT ECO:0000312|PDB:3OFW, ECO:0000312|PDB:3T62,
FT ECO:0000312|PDB:3UOU"
FT HELIX 1..4
FT /evidence="ECO:0007829|PDB:3M7Q"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3M7Q"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:3M7Q"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:3M7Q"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3M7Q"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3M7Q"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:3M7Q"
SQ SEQUENCE 55 AA; 6116 MW; 532B96E3127000D4 CRC64;
SICSEPKKVG RCKGYFPRFY FDSETGKCTP FIYGGCGGNG NNFETLHQCR AICRA
