KUN2_TABYA
ID KUN2_TABYA Reviewed; 76 AA.
AC C8YJ94;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Tabkunin 2 {ECO:0000303|PubMed:19531497};
DE AltName: Full=Serine protease inhibitor 2 {ECO:0000312|EMBL:ACS72289.1};
DE Flags: Precursor;
OS Tabanus yao (Horsefly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Tabanomorpha; Tabanoidea;
OC Tabanidae; Tabanus.
OX NCBI_TaxID=485572;
RN [1] {ECO:0000312|EMBL:ACS72289.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-45, SUBCELLULAR
RP LOCATION, MASS SPECTROMETRY, AND FUNCTION.
RC TISSUE=Salivary gland;
RX PubMed=19531497; DOI=10.1074/mcp.m900186-mcp200;
RA Ma D., Wang Y., Yang H., Wu J., An S., Gao L., Xu X., Lai R.;
RT "Anti-thrombosis repertoire of blood-feeding horsefly salivary glands.";
RL Mol. Cell. Proteomics 8:2071-2079(2009).
CC -!- FUNCTION: Potent anticoagulant protein that inhibits the hydrolytic
CC activities of all serine proteases tested (trypsin, thrombin, elastase,
CC and chymotrypsin), with the highest efficacy on thrombin.
CC {ECO:0000269|PubMed:19531497}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19531497}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC {ECO:0000305|PubMed:19531497}.
CC -!- MASS SPECTROMETRY: Mass=6063.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19531497};
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DR EMBL; FJ469601; ACS72289.1; -; mRNA.
DR MEROPS; I02.026; -.
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 Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Protease inhibitor; Secreted;
KW Serine protease inhibitor; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000305|PubMed:19531497"
FT CHAIN 21..76
FT /note="Tabkunin 2"
FT /evidence="ECO:0000305|PubMed:19531497"
FT /id="PRO_5002994607"
FT DOMAIN 25..75
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 25..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 34..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 50..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 76 AA; 8245 MW; B76B271CF81DE653 CRC64;
MKVLSLIFVI FSVLVLFASA KDPVCDQPKA VGRCFAAFPK FYYNSSSGQC QAFIYGGCGG
NENNFNTLEE CNAKCA