VKT2_WALAE
ID VKT2_WALAE Reviewed; 81 AA.
AC C1IC52;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Kunitz-type serine protease inhibitor spermatin {ECO:0000303|Ref.2};
DE AltName: Full=Kunitz inhibitor KIn-II;
DE AltName: Full=Protease inhibitor 2;
DE Flags: Precursor;
OS Walterinnesia aegyptia (Desert black snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Walterinnesia.
OX NCBI_TaxID=64182;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-40, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland {ECO:0000303|PubMed:18405934};
RX PubMed=18405934; DOI=10.1016/j.toxicon.2008.02.012;
RA Tsai H.-Y., Wang Y.M., Tsai I.-H.;
RT "Cloning, characterization and phylogenetic analyses of members of three
RT major venom families from a single specimen of Walterinnesia aegyptia.";
RL Toxicon 51:1245-1254(2008).
RN [2]
RP PROTEIN SEQUENCE OF 25-81, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|Ref.2};
RA De Waard M.;
RL Submitted (JUN-2017) to UniProtKB.
CC -!- FUNCTION: Snake venom serine protease inhibitor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18405934,
CC ECO:0000269|Ref.2}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:18405934}.
CC -!- MASS SPECTROMETRY: Mass=6394; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18405934};
CC -!- MASS SPECTROMETRY: Mass=6390; Mass_error=1; Method=MALDI;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR EMBL; EU196560; ABX82869.1; -; mRNA.
DR AlphaFoldDB; C1IC52; -.
DR SMR; C1IC52; -.
DR MEROPS; I02.055; -.
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; Secreted;
KW Serine protease inhibitor; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:18405934, ECO:0000269|Ref.2"
FT CHAIN 25..81
FT /note="Kunitz-type serine protease inhibitor spermatin"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000419228"
FT DOMAIN 29..79
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 29..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 38..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 54..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 81 AA; 8870 MW; 9F611182F1B4BC74 CRC64;
MSSGCLLLLL GLLTLWAELT PVSGRPRLCE LPAESGLCNA YIPSFYYNPH SHKCQKFMYG
GCGGNANNFK TIDECHRTCV G
