ID   BMTIA_RHIMP             Reviewed;         121 AA.
AC   P83609;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Kunitz-type serine protease inhibitor A;
DE            Short=BmTI-A;
DE   Flags: Fragments;
OS   Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC   Rhipicephalus; Boophilus.
OX   NCBI_TaxID=6941;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Larva;
RX   PubMed=10615008; DOI=10.1016/s0162-3109(99)00074-0;
RA   Tanaka A.S., Andreotti R., Gomes A., Torquato R.J.S., Sampaio M.U.,
RA   Sampaio C.A.M.;
RT   "A double headed serine proteinase inhibitor-human plasma kallikrein and
RT   elastase inhibitor-from Boophilus microplus larvae.";
RL   Immunopharmacology 45:171-177(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-43, AND FUNCTION.
RC   TISSUE=Larva;
RX   PubMed=15556274; DOI=10.1016/j.biochi.2004.09.010;
RA   Sasaki S.D., Azzolini S.S., Hirata I.Y., Andreotti R., Tanaka A.S.;
RT   "Boophilus microplus tick larvae, a rich source of Kunitz type serine
RT   proteinase inhibitors.";
RL   Biochimie 86:643-649(2004).
CC   -!- FUNCTION: Inhibits bovine trypsin, bovine chymotrypsin, human plasmin,
CC       human plasma kallikrein and human neutrophil elastase, but not bovine
CC       thrombin, human factor Xa or porcine pancreatic kallikrein. May play a
CC       role in blocking blood coagulation during the larvae fixation on
CC       cattle. {ECO:0000269|PubMed:10615008, ECO:0000269|PubMed:15556274}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   VEuPathDB; VectorBase:LOC119167311; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0044562; P:envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism; IEA:UniProt.
DR   CDD; cd00109; KU; 2.
DR   Gene3D; 4.10.410.10; -; 2.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 2.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 2.
DR   SUPFAM; SSF57362; SSF57362; 2.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Repeat;
KW   Secreted; Serine protease inhibitor.
FT   CHAIN           1..>121
FT                   /note="Kunitz-type serine protease inhibitor A"
FT                   /id="PRO_0000155450"
FT   DOMAIN          10..59
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          61..111
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            20..21
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   SITE            70..71
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        10..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        19..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        34..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        70..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        79..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        95..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   NON_CONS        68..69
FT                   /evidence="ECO:0000305"
FT   NON_TER         121
SQ   SEQUENCE   121 AA;  13592 MW;  65DCB397AA2973E2 CRC64;
     SQPHVNPFAC YVAPDQGPCR AILRYYFDDD TQTCQRFTYG GCEGNANNXX XXEQCKASCK
     PETEYEAKKC LARPESGPCL AYMPMWGYDS KLGQCVEFIY GGCDGNDNKY TTEEECLKSC
     K