ID   KUN2_RHIHE              Reviewed;         195 AA.
AC   I6VXS1;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Anticoagulant protein rhipilin-2 {ECO:0000303|PubMed:25708749};
DE   Flags: Precursor;
OS   Rhipicephalus haemaphysaloides (Tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC   Rhipicephalus; Rhipicephalus.
OX   NCBI_TaxID=237073;
RN   [1] {ECO:0000312|EMBL:AFN22082.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY BLOOD FEEDING, TISSUE
RP   SPECIFICITY, AND RECOMBINANT EXPRESSION.
RC   TISSUE=Salivary gland;
RX   PubMed=25708749; DOI=10.1002/arch.21118;
RA   Cao J., Shi L., Zhou Y., Gao X., Zhang H., Gong H., Zhou J.;
RT   "Characterization of a new Kunitz-type serine protease inhibitor from the
RT   hard tick Rhipicephalus hemaphysaloides.";
RL   Arch. Insect Biochem. Physiol. 84:104-113(2013).
CC   -!- FUNCTION: Anticoagulant protein that inhibits the serine proteases
CC       trypsin and elastase, but not thrombin (PubMed:25708749). The
CC       anticoagulant effect of this recombinant protein on blood clotting is
CC       found only in the activated partial thromboplastin time (APTT) assays,
CC       but not in the prothrombin time (PT) assays (PubMed:25708749).
CC       {ECO:0000269|PubMed:25708749}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Primarily expressed in salivary glands and weakly
CC       expressed in the midgut of fed ticks. {ECO:0000269|PubMed:25708749}.
CC   -!- INDUCTION: By blood feeding. Expression is most important during the
CC       early stage of feeding. {ECO:0000269|PubMed:25708749}.
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DR   EMBL; JQ812616; AFN22082.1; -; mRNA.
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; -; 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   2: Evidence at transcript level;
KW   Blood coagulation cascade inhibiting toxin; Disulfide bond;
KW   Hemostasis impairing toxin; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..195
FT                   /note="Anticoagulant protein rhipilin-2"
FT                   /id="PRO_5003706419"
FT   DOMAIN          26..87
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        26..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        39..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        62..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   195 AA;  22613 MW;  18E4228399181688 CRC64;
     MVLCCFALLI TAVLVASKGA EEKPTCDPDH ENKKVLWTCW TDDYNTTCFE RSFYYNRQTD
     RCEEFLYEGC GGNDNNFPSI EDCLSNCKTN MTDYEIKFFQ RLNKTLSCTS TYEKGSISRY
     ILNETSQECQ RADVKNGDIH FPSFRKCVYD CKPNSTSNPY CNSIKENGTK PRAPWNCYRQ
     DGYKALFCYK PKNSK