ID   VSP_NAJNA               Reviewed;          36 AA.
AC   P86545;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Thrombin-like enzyme TLP;
DE            Short=SVTLE;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Fragment;
OS   Naja naja (Indian cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=35670;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom {ECO:0000269|PubMed:20203422};
RX   PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA   Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA   Athauda S.B., Moriyama A.;
RT   "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT   russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL   Biomed. Res. 31:71-81(2010).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease. Shows strong
CC       hydrolytic activity towards Boc-Asp(oBzl)-Pro-Arg-MCA, a synthetic
CC       substrate for thrombin. {ECO:0000269|PubMed:20203422}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:20203422}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   AlphaFoldDB; P86545; -.
DR   SMR; P86545; -.
DR   Proteomes; UP000694559; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Direct protein sequencing;
KW   Disulfide bond; Hemostasis impairing toxin; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Toxin.
FT   CHAIN           1..>36
FT                   /note="Thrombin-like enzyme TLP"
FT                   /id="PRO_0000394692"
FT   DOMAIN          1..>36
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        6..?
FT                   /evidence="ECO:0000250|UniProtKB:Q91516,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        25..?
FT                   /evidence="ECO:0000250|UniProtKB:Q91516,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         36
FT                   /evidence="ECO:0000303|PubMed:20203422"
SQ   SEQUENCE   36 AA;  4114 MW;  53DFFDF02A8D7714 CRC64;
     IGGFECNEHE HRSLVYLYNS AGFFCAGTLL NHEWVV