PR13A_PLARH
ID PR13A_PLARH Reviewed; 73 AA.
AC A0A6B9L1F0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=Kazal peptide Pr13a {ECO:0000303|PubMed:31752210};
DE AltName: Full=Venom Kazal domain peptide Pr13a {ECO:0000312|EMBL:QHB21517.1};
DE Flags: Precursor;
OS Platymeris rhadamanthus (Red spot assassin bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Platymeris.
OX NCBI_TaxID=1134088;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Venom gland;
RX PubMed=31752210; DOI=10.3390/toxins11110673;
RA Walker A.A., Robinson S.D., Undheim E.A.B., Jin J., Han X., Fry B.G.,
RA Vetter I., King G.F.;
RT "Missiles of mass disruption: composition and glandular origin of venom
RT used as a projectile defensive weapon by the assassin bug Platymeris
RT rhadamanthus.";
RL Toxins 11:E673-E673(2019).
CC -!- FUNCTION: May act as a serine protease inhibitor, since it possess the
CC kazal serine protease inhibitor signature. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:31752210}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland (anterior main gland)
CC (at protein level). {ECO:0000269|PubMed:31752210}.
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DR EMBL; MN208328; QHB21517.1; -; mRNA.
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; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..73
FT /note="Kazal peptide Pr13a"
FT /evidence="ECO:0000305"
FT /id="PRO_5025470253"
FT DOMAIN 21..73
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 29..30
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 23..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 27..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 36..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 73 AA; 8200 MW; 46E5FC90C358773E CRC64;
MKYIILFLVL IGLQANLALG SKCKCDCTKY PYSPVCAKEL KTGDTETFNN VCQLQCYNCT
HMKNYVVIYS GSC