ID   VKT3_ANTAF              Reviewed;          61 AA.
AC   P0DMX0;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=PI-actitoxin-Axm2b {ECO:0000303|PubMed:22683676};
DE            Short=PI-AITX-Axm2b {ECO:0000303|PubMed:22683676};
DE   AltName: Full=AXPI-III {ECO:0000303|Ref.1};
OS   Anthopleura aff. xanthogrammica (Sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anthopleura.
OX   NCBI_TaxID=152178;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RA   Minagawa S., Ishida M., Shimakura K., Nagashima Y., Shiomi K.;
RT   "Amino acid sequence and biological activities of another Kunitz-type
RT   protease inhibitor from the sea anemone Anthopleura aff. xanthogrammica.";
RL   Fish. Sci. 64:155-159(1998).
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).
CC   -!- FUNCTION: Protease inhibitor. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}. Nematocyst
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=6985; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
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; P0DMX0; -.
DR   SMR; P0DMX0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
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   Direct protein sequencing; Disulfide bond; Nematocyst; Protease inhibitor;
KW   Secreted; Serine protease inhibitor.
FT   CHAIN           1..61
FT                   /note="PI-actitoxin-Axm2b"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000433574"
FT   DOMAIN          7..57
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            17..18
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250|UniProtKB:P31713"
FT   DISULFID        7..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        16..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        32..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   61 AA;  6980 MW;  86E847C2EE0BA710 CRC64;
     HSSNDFCYLP AVRGRCRGYF PRYFFSSETG KCERFIYGGC GGNRNNFESA QECGSTCYPR
     E