ID   SER_TABYA               Reviewed;         248 AA.
AC   C1IBY0;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Tabserin {ECO:0000303|PubMed:18087067};
DE            EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274};
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:ABX80068.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RC   TISSUE=Salivary gland;
RX   PubMed=18087067; DOI=10.1074/mcp.m700497-mcp200;
RA   Xu X., Yang H., Ma D., Wu J., Wang Y., Song Y., Wang X., Lu Y., Yang J.,
RA   Lai R.;
RT   "Toward an understanding of the molecular mechanism for successful blood
RT   feeding by coupling proteomics analysis with pharmacological testing of
RT   horsefly salivary glands.";
RL   Mol. Cell. Proteomics 7:582-590(2008).
CC   -!- FUNCTION: Serine protease that inhibits blood coagulation in a dose-
CC       dependent manner. May act by destroying coagulant factors to inhibit
CC       blood coagulation. {ECO:0000269|PubMed:18087067}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18087067}.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC       {ECO:0000305|PubMed:18087067}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; EU147250; ABX80068.1; -; mRNA.
DR   SMR; C1IBY0; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation cascade inhibiting toxin; Disulfide bond;
KW   Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..248
FT                   /note="Tabserin"
FT                   /id="PRO_5002910663"
FT   DOMAIN          24..248
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        64
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        111
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        49..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        175..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        201..226
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   248 AA;  27408 MW;  EEE65662F4F14E53 CRC64;
     MLKYSALFLY LIYVGGSESA HSRIVGGVPV AEEKVPYVVS IRMKEIHVCG GSILSESIVL
     TAAHCFDKSK GYSNYAVFAG SNRLSGGLKV EIQNITIHPK YIGPSDWWKN DLAVVKLKKP
     LNFSKSVRTV KIFPSYVPEN ETVYAYGWGK TIVPFFTLPN VLQKLETKAL NLTACQKSWK
     EHVVESQLCL WTGHGTGVGL CKADSGGPVV YKGKLVGVIS WVQVHCNTKK PDVAVRLSPY
     FENGLRKR