VSP2_AGKBI
ID VSP2_AGKBI Reviewed; 235 AA.
AC Q9PSN3; Q9PS18;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Thrombin-like enzyme bilineobin;
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 Agkistrodon bilineatus (Cantil) (Tropical moccasin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=8718;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, DISULFIDE BONDS, AND GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=7726578; DOI=10.1006/abbi.1995.1208;
RA Nikai T., Ohara A., Komori Y., Fox J.W., Sugihara H.;
RT "Primary structure of a coagulant enzyme, bilineobin, from Agkistrodon
RT bilineatus venom.";
RL Arch. Biochem. Biophys. 318:89-96(1995).
RN [2]
RP PROTEIN SEQUENCE OF 1-24, FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom;
RX PubMed=8470131; DOI=10.1016/0041-0101(93)90144-8;
RA Komori Y., Nikai T., Ohara A., Yagihashi S., Sugihara H.;
RT "Effect of bilineobin, a thrombin-like proteinase from the venom of common
RT cantil (Agkistrodon bilineatus).";
RL Toxicon 31:257-270(1993).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that has coagulant
CC activity by releasing fibrinopeptides A and B from fibrinogen alpha
CC (FGA) and beta (FGB), with a preference for beta chain.
CC {ECO:0000269|PubMed:8470131}.
CC -!- ACTIVITY REGULATION: Not inhibited by hirudin.
CC {ECO:0000269|PubMed:8470131}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7726578,
CC ECO:0000269|PubMed:8470131}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:7726578, ECO:0000305|PubMed:8470131}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:7726578}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PIR; S65621; S65621.
DR AlphaFoldDB; Q9PSN3; -.
DR SMR; Q9PSN3; -.
DR MEROPS; S01.181; -.
DR iPTMnet; Q9PSN3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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..235
FT /note="Thrombin-like enzyme bilineobin"
FT /id="PRO_0000088725"
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:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 88
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 7..141
FT /evidence="ECO:0000269|PubMed:7726578"
FT DISULFID 28..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:7726578"
FT DISULFID 78..234
FT /evidence="ECO:0000269|PubMed:7726578"
FT DISULFID 120..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:7726578"
FT DISULFID 152..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:7726578"
FT DISULFID 178..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:7726578"
FT CONFLICT 1
FT /note="I -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 26479 MW; 73A98766CA507578 CRC64;
IIGGDECNIN EHRFLVALYD VWSGSFLCGG TLINQEWVLT AAHCNMSNIY IYLGMHNQSV
QFDDEERRYP KEKYLFRCSK NFTKWDKDIM LIRLNKPVRN SEHIAPLSLP SSPPIVGSVC
RVMGWGTITS PNETLPDVPR CVNINLFNYT VCRGVFPRLP ERSRILCAGV LEGGIDTCKR
DSGGPLICNG QFQGIVSWGP KRCAQPRKPA LYSKVFDHLD WIQSIIAGNK TVNCP
