VKT19_ANOSM
ID VKT19_ANOSM Reviewed; 75 AA.
AC Q589G4;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Kunitz-type serine protease inhibitor As-fr-19 {ECO:0000303|PubMed:15823549};
DE Short=Asfr19 {ECO:0000303|PubMed:15823549};
DE Flags: Precursor;
OS Anoplius samariensis (Solitary wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Pompiloidea;
OC Pompilidae; Pompilinae; Anoplius.
OX NCBI_TaxID=200614;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-39, MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15823549; DOI=10.1016/j.bbrc.2005.03.087;
RA Hisada M., Satake H., Masuda K., Aoyama M., Murata K., Shinada T.,
RA Iwashita T., Ohfune Y., Nakajima T.;
RT "Molecular components and toxicity of the venom of the solitary wasp,
RT Anoplius samariensis.";
RL Biochem. Biophys. Res. Commun. 330:1048-1054(2005).
RN [2]
RP REVIEW.
RX PubMed=27096870; DOI=10.3390/toxins8040114;
RA Konno K., Kazuma K., Nihei K.;
RT "Peptide toxins in solitary wasp venoms.";
RL Toxins 8:114-114(2016).
CC -!- FUNCTION: May exert inhibitory effects on serine proteases and on
CC potassium and/or calcium channels and then participate in the long-term
CC non-lethal paralysis on the prey. {ECO:0000305|PubMed:15823549}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15823549}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15823549}.
CC -!- MASS SPECTROMETRY: Mass=6663.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15823549};
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR EMBL; AB186137; BAD93276.1; -; mRNA.
DR AlphaFoldDB; Q589G4; -.
DR SMR; Q589G4; -.
DR MEROPS; I02.964; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin 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 Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW Protease inhibitor; Secreted; Serine protease inhibitor; Signal; Toxin.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:15823549"
FT CHAIN 18..75
FT /note="Kunitz-type serine protease inhibitor As-fr-19"
FT /evidence="ECO:0000269|PubMed:15823549"
FT /id="PRO_0000223994"
FT DOMAIN 21..71
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 21..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 30..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 46..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 75 AA; 8494 MW; F84CB20EDBDDE64B CRC64;
MMLLVLSISA ILQVSHSVSF CLLPIVPGPC TQYVIRYAFQ PSISACRRFT FGGCEGNDNN
FMTRRDCEHY CEELL
