VKT2_STIHL
ID VKT2_STIHL Reviewed; 55 AA.
AC P81129;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=PI-stichotoxin-She2b {ECO:0000303|PubMed:22683676};
DE Short=PI-SHTX-She2b {ECO:0000303|PubMed:22683676};
DE AltName: Full=Kunitz-type protease inhibitor SHPI-2 {ECO:0000303|Ref.1};
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, AND FUNCTION.
RA Diaz J., Morera V., Delfin J., Huerta V., Lima G., Rodriguex de la Vega M.,
RA Garcia B., Padron G., Assfalg-Machleidt I., Machleidt W., Chavez M.;
RT "Purification and partial characterization of a novel proteinase inhibitor
RT from the sea anemone Stichodactyla helianthus.";
RL Toxicon 36:1275-1276(1998).
RN [2]
RP MASS SPECTROMETRY.
RX PubMed=22015268; DOI=10.1016/j.peptides.2011.10.011;
RA Rodriguez A.A., Cassoli J.S., Sa F., Dong Z.Q., de Freitas J.C.,
RA Pimenta A.M., de Lima M.E., Konno K., Lee S.M., Garateix A.,
RA Zaharenko A.J.;
RT "Peptide fingerprinting of the neurotoxic fractions isolated from the
RT secretions of sea anemones Stichodactyla helianthus and Bunodosoma
RT granulifera. New members of the APETx-like family identified by a 454
RT pyrosequencing approach.";
RL Peptides 34:26-38(2012).
RN [3]
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).
CC -!- FUNCTION: Inhibitor of serine, cysteine, and aspartic proteinases.
CC {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}. Nematocyst
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=6197.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22015268};
CC -!- MISCELLANEOUS: Does not show effect on crabs.
CC {ECO:0000269|PubMed:22015268}.
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 AlphaFoldDB; P81129; -.
DR SMR; P81129; -.
DR MEROPS; I02.061; -.
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 Aspartic protease inhibitor; Direct protein sequencing; Disulfide bond;
KW Nematocyst; Protease inhibitor; Secreted; Serine protease inhibitor.
FT CHAIN 1..55
FT /note="PI-stichotoxin-She2b"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000155420"
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:0000250|UniProtKB:P31713"
FT DISULFID 3..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 12..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 28..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 55 AA; 6203 MW; 33187E041916C7CF CRC64;
SFCLEPKRVG RCKGYFPRFY FDSKTGKCTP FIYGGCGGNG NNFETLHQCR AICRA
