ID   BMTI6_RHIMP             Reviewed;         291 AA.
AC   P83606;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Kunitz-type serine protease inhibitor 6;
DE            Short=BmTI-6;
DE   Flags: Fragment;
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   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, AND FUNCTION.
RX   PubMed=18502587; DOI=10.1016/j.vetpar.2008.03.031;
RA   Sasaki S.D., Tanaka A.S.;
RT   "rBmTI-6, a Kunitz-BPTI domain protease inhibitor from the tick Boophilus
RT   microplus, its cloning, expression and biochemical characterization.";
RL   Vet. Parasitol. 155:133-141(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nene V., Quackenbush J., George J., Guerrero F.;
RT   "An index of genes transcribed in the tick Boophilus microplus.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-35, AND FUNCTION.
RC   TISSUE=Larva;
RA   Sasaki S.D., Hirata I.Y., Tanaka A.S.;
RT   "Molecular studies of serine protease inhibitors from cattle tick Boophilus
RT   microplus (larvae).";
RL   Submitted (JUN-2003) to UniProtKB.
CC   -!- FUNCTION: Inhibits trypsin and plasmin. Does not inhibit human plasma
CC       kallikrein, chymotrypsin, human neutrophil elastase, factor Xa, factor
CC       XIIa or thrombin. {ECO:0000269|PubMed:18502587, ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; CK186726; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P83606; -.
DR   SMR; P83606; -.
DR   VEuPathDB; VectorBase:LOC119167312; -.
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; 3.
DR   Gene3D; 4.10.410.10; -; 3.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 3.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 3.
DR   SUPFAM; SSF57362; SSF57362; 3.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 3.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Repeat; Secreted; Serine protease inhibitor.
FT   CHAIN           1..>291
FT                   /note="Kunitz-type serine protease inhibitor 6"
FT                   /id="PRO_0000155454"
FT   DOMAIN          7..57
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          139..189
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          235..285
FT                   /note="BPTI/Kunitz inhibitor 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            17..18
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   SITE            149..150
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   SITE            245..246
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        7..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        16..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        32..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        139..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        148..172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        164..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        235..285
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        244..268
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        260..281
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   CONFLICT        20
FT                   /note="F -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="F -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        35
FT                   /note="F -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         291
SQ   SEQUENCE   291 AA;  33847 MW;  4E0111354A5781C2 CRC64;
     VDFETYCKPT YDSGPCKGYF PRWWFNVKTG QCEEFIYGGC QGNKNNHVTR KECETRCLRK
     QLSRLHFSPP VDQYPYGDTE RSNEEVPEYP PVHLNDSLEV SAVMNQRPLR NYTKQHKPNV
     TSDFSAISLT SGVDFETYCK PTHDRGPCKA YIPRWWFNVK TGQCEQFIYG GCQGNKNNYE
     TKSICETNCL RRQLSELGVS ADVHYRKHWN ETKYSPNVTV EYPAVHFNVT LNPVCNEPKY
     PELCKGYFPR YYYNSRSKTC KKFIYGGCQS NGNNFLTLEE CENTCLVDLQ V