VSP1_GLOBR
ID VSP1_GLOBR Reviewed; 236 AA.
AC P85109;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Thrombin-like enzyme kangshuanmei;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
OS Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys
OS brevicaudus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=259325;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, AND GLYCOSYLATION AT ASN-81; ASN-99; ASN-148 AND ASN-229.
RC TISSUE=Venom {ECO:0000269|PubMed:16908038};
RX PubMed=16908038; DOI=10.1016/j.toxicon.2006.06.001;
RA Sakai J., Zhang S., Chen H., Atsumi F., Matsui T., Shiono H., Sanada S.,
RA Okada T.;
RT "Primary structure of a thrombin-like serine protease, kangshuanmei, from
RT the venom of Agkistrodon halys brevicaudus stejneger.";
RL Toxicon 48:313-322(2006).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-50, FUNCTION, ACTIVITY REGULATION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom {ECO:0000269|PubMed:11491462};
RX PubMed=11491462;
RA Zhang S., Ma B., Sakai J., Shiono H., Matsui T., Sugie I., Okada T.;
RT "Characterization of a thrombin-like serine protease, Kangshuanmei,
RT isolated from the venom of a Chinese snake, Agkistrodon halys brevicaudus
RT stejneger.";
RL J. Nat. Toxins 10:221-238(2001).
CC -!- FUNCTION: Thrombin-like snake venom serine protease. Cleaves bonds
CC after Arg and Lys, converts fibrinogen (FGA and FGB) to fibrin and
CC releases both fibrinopeptides A and B, and fibrinogen peptide Bbeta1-
CC 42. Has a blood clotting activity. {ECO:0000269|PubMed:11491462,
CC ECO:0000269|PubMed:16908038}.
CC -!- ACTIVITY REGULATION: Inhibited by 4-(2-aminoethyl)-benzensulfonyl
CC fluoride. Not inhibited by antithrombin-III.
CC {ECO:0000269|PubMed:11491462}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11491462}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11491462,
CC ECO:0000269|PubMed:16908038}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:11491462, ECO:0000269|PubMed:16908038}.
CC -!- PTM: N-glycosylated by units composed of Fuc, Man, GlcNAc, Gal and
CC NeuAC residues. {ECO:0000269|PubMed:16908038}.
CC -!- MASS SPECTROMETRY: Mass=26476; Method=MALDI; Note=For the
CC deglycosylated protein.; Evidence={ECO:0000269|PubMed:16908038};
CC -!- MASS SPECTROMETRY: Mass=32278; Method=MALDI; Note=For the glycosylated
CC protein.; Evidence={ECO:0000269|PubMed:16908038};
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR AlphaFoldDB; P85109; -.
DR SMR; P85109; -.
DR MEROPS; S01.524; -.
DR iPTMnet; P85109; -.
DR PRIDE; P85109; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Protease; Secreted; Serine protease; Toxin.
FT CHAIN 1..236
FT /note="Thrombin-like enzyme kangshuanmei"
FT /id="PRO_0000283728"
FT DOMAIN 1..227
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 43
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P33589"
FT ACT_SITE 88
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P33589"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P33589"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16908038"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16908038"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16908038"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16908038"
FT DISULFID 7..141
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 78..234
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 120..188
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 152..167
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 178..203
FT /evidence="ECO:0000250|UniProtKB:Q9PSN3,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 236 AA; 26432 MW; B1579E328A6522E5 CRC64;
VIGGDECNIN EHRFLVALYH SRSRTFLCGG TLINQEWVLT AAHCDRFFMY IRLGMHNKNV
NFDDEQRRSP KEKYFFRCSN NFTKWDKDIM LIRLDSPVNN SAHIAPLSLP SNPPSVGSVC
RVMGWGQTTS PQEDLSDVPR CANINLFNFT VCRAAYPWLP ATSRVLCAGD MEGGIDTCNR
DSGGPLICNG QFQGIVSKGQ NLCAQPRKPA LYTKVFDHLD WIQSIIAGNK TVTCPP
