ID   KTIL_BOTSC              Reviewed;          54 AA.
AC   C0HL51;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Kazal-type inhibitor-like protein {ECO:0000303|PubMed:26973135};
DE            Short=KTIL {ECO:0000303|PubMed:26973135};
OS   Bothriechis schlegelii (Eyelash palm pitviper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothriechis.
OX   NCBI_TaxID=44725 {ECO:0000303|PubMed:26973135};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-39, FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:26973135}, and
RC   Venom gland {ECO:0000303|PubMed:26973135};
RX   PubMed=26973135; DOI=10.1016/j.biochi.2016.03.004;
RA   Fernandez J., Gutierrez J.M., Calvete J.J., Sanz L., Lomonte B.;
RT   "Characterization of a novel snake venom component: Kazal-type inhibitor-
RT   like protein from the arboreal pitviper Bothriechis schlegelii.";
RL   Biochimie 125:83-90(2016).
CC   -!- FUNCTION: Partially inhibits trypsin in vitro at slightly acidic pH and
CC       concentrations in excess of 0.3 mM. Has no protease inhibitory activity
CC       at neutral or basic pH. Has no antibacterial activity. Shows no
CC       toxicity in vertebrates apart from transient paw edema in mouse.
CC       {ECO:0000269|PubMed:26973135}.
CC   -!- SUBUNIT: May form disulfide-linked dimers or trimers (in vitro).
CC       {ECO:0000305|PubMed:26973135}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26973135}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:26973135}.
CC   -!- MASS SPECTROMETRY: Mass=6171; Mass_error=2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:26973135};
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DR   AlphaFoldDB; C0HL51; -.
DR   SMR; C0HL51; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   Pfam; PF00050; Kazal_1; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   PROSITE; PS00282; KAZAL_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted.
FT   CHAIN           1..54
FT                   /note="Kazal-type inhibitor-like protein"
FT                   /evidence="ECO:0000269|PubMed:26973135"
FT                   /id="PRO_0000443430"
FT   DOMAIN          1..54
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            15..16
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        5..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        13..32
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        21..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   54 AA;  6179 MW;  3B4C558F2FE37E75 CRC64;
     MKVNCKGYPT KFCFGKPLPH CASDGKTYPN RCRFCNAFVK SHGLITLRYY GKCK