ID   KAZL2_DOLGE             Reviewed;         202 AA.
AC   A0A3G5BID2;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=U-Kazal-Dg21.2 {ECO:0000303|PubMed:30400621};
DE   Flags: Precursor;
OS   Dolopus genitalis (Giant Australian assassin fly) (Asilus genitalis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC   Asilidae; Asilinae; Dolopus.
OX   NCBI_TaxID=2488630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DETECTION IN VENOM.
RC   TISSUE=Venom gland;
RX   PubMed=30400621; DOI=10.3390/toxins10110456;
RA   Walker A.A., Dobson J., Jin J., Robinson S.D., Herzig V., Vetter I.,
RA   King G.F., Fry B.G.;
RT   "Buzz kill: function and proteomic composition of venom from the giant
RT   assassin fly Dolopus genitalis (Diptera: Asilidae).";
RL   Toxins 10:E456-E456(2018).
RN   [2]
RP   FUNCTION, MASS SPECTROMETRY, RECOMBINANT EXPRESSION, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=31870846; DOI=10.1016/j.ibmb.2019.103310;
RA   Jin J., Agwa A.J., Szanto T.G., Csoti A., Panyi G., Schroeder C.I.,
RA   Walker A.A., King G.F.;
RT   "Weaponisation 'on the fly': convergent recruitment of knottin and defensin
RT   peptide scaffolds into the venom of predatory assassin flies.";
RL   Insect Biochem. Mol. Biol. 118:103310-103310(2020).
CC   -!- FUNCTION: May act as a serine protease inhibitor, since it possess the
CC       kazal serine protease inhibitor signature (Probable). The recombinant
CC       peptide does not produce toxic effects on insects (PubMed:31870846).
CC       {ECO:0000269|PubMed:31870846, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31870846}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31870846}.
CC   -!- MASS SPECTROMETRY: Mass=6306.38; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:31870846};
CC   -!- MISCELLANEOUS: The peptide presented here consists of a single Kazal
CC       domain but is suggested to be derived from a multidomain Kazal protein
CC       after proteolytic cleavage. {ECO:0000305|PubMed:30400621}.
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DR   EMBL; MK075139; AYV99542.1; -; mRNA.
DR   AlphaFoldDB; A0A3G5BID2; -.
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; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   Pfam; PF07648; Kazal_2; 3.
DR   SMART; SM00280; KAZAL; 3.
DR   SUPFAM; SSF100895; SSF100895; 3.
DR   PROSITE; PS51465; KAZAL_2; 3.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Repeat; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..87
FT                   /evidence="ECO:0000305|PubMed:30400621"
FT                   /id="PRO_0000452539"
FT   CHAIN           88..142
FT                   /note="U-Kazal-Dg21.2"
FT                   /evidence="ECO:0000269|PubMed:30400621"
FT                   /id="PRO_5018055760"
FT   PROPEP          142..202
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000452540"
FT   DOMAIN          23..77
FT                   /note="Kazal-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          85..140
FT                   /note="Kazal-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          148..202
FT                   /note="Kazal-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            35..36
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            97..98
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            160..161
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        29..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        33..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        91..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        95..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        103..138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        154..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        158..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        166..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   202 AA;  23371 MW;  CA59B1AF01E1DBB7 CRC64;
     MKYFLWSAVT IFAIVNVVGA KNSDFDPRCL RACTAIYRPV CGFDGKQYRI FASECVMAFE
     NCNLLLKSQK AFQKTLMSFC QVEEDFDSDF CPEVCPLLYK PVCGSYGDIK KIFPNECELK
     RANCKFGEAW EKINMDICRN ISFKSELIDP KKKCLKPCNL NWDPICAFDG EKYFTFGNRC
     DMEIQTCLRS EKNWTLIRKG EC