ID   KUNI_AMBHE              Reviewed;         166 AA.
AC   Q5VJG2;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Amblin {ECO:0000303|PubMed:15527983};
DE   AltName: Full=Thrombin inhibitor {ECO:0000303|PubMed:15527983};
DE   Flags: Precursor;
OS   Amblyomma hebraeum (South African bont tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Amblyomminae; Amblyomma.
OX   NCBI_TaxID=34608;
RN   [1] {ECO:0000312|EMBL:AAR97367.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-26, AND FUNCTION.
RC   TISSUE=Hemolymph;
RX   PubMed=15527983; DOI=10.1016/j.gene.2004.07.012;
RA   Lai R., Takeuchi H., Jonczy J., Rees H.H., Turner P.C.;
RT   "A thrombin inhibitor from the ixodid tick, Amblyomma hebraeum.";
RL   Gene 342:243-249(2004).
CC   -!- FUNCTION: Thrombin-specific inhibitor from tick hemolymph (Ki=20 nM).
CC       {ECO:0000269|PubMed:15527983}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; AY437082; AAR97367.1; -; mRNA.
DR   MEROPS; I02.039; -.
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; 1.
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   Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Hemostasis impairing toxin; Protease inhibitor; Repeat;
KW   Secreted; Serine protease inhibitor; Signal; Toxin.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..166
FT                   /note="Amblin"
FT                   /evidence="ECO:0000305|PubMed:15527983"
FT                   /id="PRO_5013062386"
FT   DOMAIN          22..72
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          82..132
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        22..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        31..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        47..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        82..132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        91..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        107..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   166 AA;  18882 MW;  85A8E6B0F6D8A138 CRC64;
     MGFLVASAVL VCVTSQRVPG YCKKKPAVGP CKALIEKWYF DYSTQSCKTF YYGGCGGNGN
     KFSSRKKCRE ACLPKRPSVP VCKQMPDPGF CRAYMPHWFF NSKSGYCEGF VYGGCQGNDN
     RFKSCWQCMK KCRTAREANR LCWKLTKEFN KKFLRNVPTA KPLPPK