ID   VKT2_TROCA              Reviewed;          83 AA.
AC   B5KL33;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Kunitz-type serine protease inhibitor carinatin-2;
DE   Flags: Precursor;
OS   Tropidechis carinatus (Australian rough-scaled snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Notechinae; Tropidechis.
OX   NCBI_TaxID=100989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=18979207; DOI=10.1007/s00018-008-8573-5;
RA   St Pierre L., Earl S.T., Filippovich I., Sorokina N., Masci P.P.,
RA   De Jersey J., Lavin M.F.;
RT   "Common evolution of waprin and Kunitz-like toxin families in Australian
RT   venomous snakes.";
RL   Cell. Mol. Life Sci. 65:4039-4054(2008).
CC   -!- FUNCTION: Serine protease inhibitor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF990741; ABV64395.1; -; mRNA.
DR   EMBL; EU401853; ACC77802.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5KL33; -.
DR   SMR; B5KL33; -.
DR   MEROPS; I02.052; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor 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   2: Evidence at transcript level;
KW   Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..83
FT                   /note="Kunitz-type serine protease inhibitor carinatin-2"
FT                   /id="PRO_5000395592"
FT   DOMAIN          31..81
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            41..42
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        40..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        56..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   83 AA;  9178 MW;  AE4643036FCB7662 CRC64;
     MSSGGLLLLL GLLTLWEILT PVSSKDHPEF CELPADSGPC RGILHAFYYH PVHRTCLEFI
     YGGCYGNANN FKTIDECKRT CAA