ID   VKT_VIPRE               Reviewed;          66 AA.
AC   P0DKL8;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Kunitz-type serine protease inhibitor Vur-KIn;
DE   Contains:
DE     RecName: Full=Kunitz-type serine protease inhibitor Vur-KIn, truncated;
DE   Flags: Precursor;
OS   Vipera renardi (Steppe viper) (Vipera ursinii renardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=927686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-27, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=21185324; DOI=10.1016/j.toxicon.2010.12.012;
RA   Tsai I.-H., Wang Y.M., Cheng A.C., Starkov V., Osipov A., Nikitin I.,
RA   Makarova Y., Ziganshin R., Utkin Y.;
RT   "cDNA cloning, structural, and functional analyses of venom phospholipases
RT   A and a Kunitz-type protease inhibitor from steppe viper Vipera ursinii
RT   renardi.";
RL   Toxicon 57:332-341(2011).
CC   -!- FUNCTION: Serine protease inhibitor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: [Kunitz-type serine protease inhibitor Vur-KIn]:
CC       Mass=6824.1; Method=MALDI; Evidence={ECO:0000269|PubMed:21185324};
CC   -!- MASS SPECTROMETRY: [Kunitz-type serine protease inhibitor Vur-KIn,
CC       truncated]: Mass=6695.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21185324};
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
CC   -!- CAUTION: It is unsure if the sequence starts at position 1 or 2.
CC       {ECO:0000305}.
CC   -!- CAUTION: Two N-terminal sequences could be detected after automatic
CC       Edman degradation, one is the sequence AHKPRFYYNP, that corresponds to
CC       the fragment 18-27, and the other is DH., that possibly corresponds to
CC       the fragment 2-17. Vur-KIn possibly was partially degraded into two
CC       fragments which might be kept linked by disulfide bonds during sample
CC       preparation. {ECO:0000305}.
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DR   AlphaFoldDB; P0DKL8; -.
DR   SMR; P0DKL8; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Pyrrolidone carboxylic acid; Secreted; Serine protease inhibitor; Toxin.
FT   CHAIN           1..61
FT                   /note="Kunitz-type serine protease inhibitor Vur-KIn"
FT                   /id="PRO_0000419643"
FT   CHAIN           2..61
FT                   /note="Kunitz-type serine protease inhibitor Vur-KIn,
FT                   truncated"
FT                   /id="PRO_0000419644"
FT   PROPEP          62..66
FT                   /id="PRO_0000419645"
FT   DOMAIN          7..57
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            17..18
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
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"
SQ   SEQUENCE   66 AA;  7370 MW;  38D414BBE39382C5 CRC64;
     QDHPVFCYLP ADPGICKAHK PRFYYNPASN KCKEFFYGGC GGNANNFKTR DECHHTCVAS
     AMGRPT