ID   KUN1_RHIHE              Reviewed;         164 AA.
AC   D9IFL3;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Anticoagulant protein rhipilin-1;
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:ADJ56344.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY BLOOD FEEDING,
RP   DISRUPTION PHENOTYPE, AND RECOMBINANT EXPRESSION.
RC   TISSUE=Salivary gland;
RX   PubMed=21147114; DOI=10.1016/j.jinsphys.2010.12.001;
RA   Gao X., Shi L., Zhou Y., Cao J., Zhang H., Zhou J.;
RT   "Characterization of the anticoagulant protein Rhipilin-1 from the
RT   Rhipicephalus haemaphysaloides tick.";
RL   J. Insect Physiol. 57:339-343(2011).
CC   -!- FUNCTION: Anticoagulant protein that may inhibit serine proteases. The
CC       anticoagulant effect of this recombinant protein on blood clotting is
CC       found both in the recalcification time (RT) and the activated partial
CC       thromboplastin time (APTT) tests, indicating it acts in the common
CC       pathway of blood coagulation. {ECO:0000269|PubMed:21147114}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands. {ECO:0000305}.
CC   -!- INDUCTION: By blood feeding. {ECO:0000269|PubMed:21147114}.
CC   -!- DISRUPTION PHENOTYPE: The tick attachment time is prolonged and the
CC       engorgement body weight is decreased after gene silencing by RNA
CC       interference. No significant difference is observed in the feeding
CC       period and survival. {ECO:0000269|PubMed:21147114}.
CC   -!- BIOTECHNOLOGY: May be studied for future application as a vaccine,
CC       since it impairs tick attachment time and engorgement body weight.
CC       {ECO:0000305|PubMed:21147114}.
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DR   EMBL; HM140789; ADJ56344.1; -; 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   Pfam; PF00014; Kunitz_BPTI; 1.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..164
FT                   /note="Anticoagulant protein rhipilin-1"
FT                   /id="PRO_5003125512"
FT   DOMAIN          86..138
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        86..138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        95..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        113..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        131..155
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   164 AA;  18044 MW;  2A4B4EDA0704FE3A CRC64;
     MKILQYALLA CLLVSILGDD DDEENEGAAG SDDAGATPTA LSKPAATSAE GNTAAKNSGG
     DIKQPKQELP EPSSKGQKKP RLPKRCLFKP EQGNCAGSRF LPRWWYNPET ESCEPFTYPV
     CNKKNEAFVS CTLCMNMCMR NKRGREKAKW IRKVCRKSPK VKSG