VSPI_GLOHA
ID VSPI_GLOHA Reviewed; 238 AA.
AC I4CHP3;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Thrombin-like enzyme AhV_TL-I {ECO:0000303|PubMed:23052203};
DE Short=SVTLE AhV_TL-I {ECO:0000303|PubMed:23052203};
DE EC=3.4.21.-;
OS Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=8714;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-20, X-RAY CRYSTALLOGRAPHY
RP (1.75 ANGSTROMS) OF 1-238, MASS SPECTROMETRY, GLYCOSYLATION AT ASN-81, AND
RP DISULFIDE BOND.
RC TISSUE=Venom;
RX PubMed=23052203; DOI=10.1007/s00204-012-0957-5;
RA Zeng F., Shen B., Zhu Z., Zhang P., Ji Y., Niu L., Li X., Teng M.;
RT "Crystal structure and activating effect on RyRs of AhV_TL-I, a
RT glycosylated thrombin-like enzyme from Agkistrodon halys snake venom.";
RL Arch. Toxicol. 87:535-545(2013).
CC -!- FUNCTION: Thrombin-like enzyme that shows fibrinogenolytic activity
CC against both the Aalpha (FGA) and Bbeta (FGB) chains of bovine
CC fibrinogen. This enzyme has poor esterolytic activity upon BAEE
CC substrate. It induces mouse thoracic aortic ring contraction with
CC EC(50)=147 nmol/L. It shows vasoconstrictor effects that are
CC independent of the enzymatic activity, but related to the release of
CC calcium ions form the calcium store, potentially through the activation
CC of ryanodine receptors. {ECO:0000269|PubMed:23052203}.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF, L-cysteine and partially by
CC SBTI and leupeptin. {ECO:0000269|PubMed:23052203}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23052203}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23052203}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23052203}.
CC -!- PTM: N-glycosylated at Asn-81 by a disaccharide composed of two N-
CC acetylglucosamine (NAG). The presence of this N-glycan deforms the
CC enzyme and Removing the carbohydrate moiety increases the esterase
CC activity, but induces a complete loss of contractile response on mouse
CC thoracic aorta. {ECO:0000269|PubMed:23052203}.
CC -!- MASS SPECTROMETRY: Mass=29389.53; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23052203};
CC -!- MISCELLANEOUS: Does not have effect on potassium channels and L-type
CC calcium channels in vascular smooth muscle cells.
CC {ECO:0000269|PubMed:23052203}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFM29142.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; JQ965747; AFM29142.1; ALT_INIT; mRNA.
DR PDB; 4E7N; X-ray; 1.75 A; A=1-238.
DR PDBsum; 4E7N; -.
DR AlphaFoldDB; I4CHP3; -.
DR SMR; I4CHP3; -.
DR MEROPS; S01.253; -.
DR iPTMnet; I4CHP3; -.
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 InterPro; IPR033116; TRYPSIN_SER.
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.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Fibrinogenolytic toxin; Glycoprotein; Hemostasis impairing toxin;
KW Hydrolase; Protease; Secreted; Serine protease; Toxin.
FT CHAIN 1..238
FT /note="Thrombin-like enzyme AhV_TL-I"
FT /id="PRO_0000445810"
FT DOMAIN 1..229
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 184
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23052203,
FT ECO:0000312|PDB:4E7N"
FT DISULFID 7..141
FT /evidence="ECO:0000269|PubMed:23052203,
FT ECO:0007744|PDB:4E7N"
FT DISULFID 28..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:23052203, ECO:0007744|PDB:4E7N"
FT DISULFID 76..236
FT /evidence="ECO:0000269|PubMed:23052203,
FT ECO:0007744|PDB:4E7N"
FT DISULFID 120..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:23052203, ECO:0007744|PDB:4E7N"
FT DISULFID 152..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:23052203, ECO:0007744|PDB:4E7N"
FT DISULFID 180..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:23052203, ECO:0007744|PDB:4E7N"
SQ SEQUENCE 238 AA; 26387 MW; 51504479642D256B CRC64;
IIGGDECNIN EHRFLVALYT SRSRTLFCGG TLINQEWVLT AAHCDRKNFR IKLGMHSKKV
PNEDEQTRVP KEKFFCLSSK NYTLWDKDIM LIRLDSPVKN SKHIAPFSLP SSPPSVGSVC
RIMGWGRISP TEGTYPDVPH CVNINLLEYE MCRAPYPEFE LPATSRTLCA GILEGGKDTC
KGDSGGPLIC NGQFQGIASW GDDPCAQPHK PAAYTKVFDH LDWIENIIAG NTDASCPP
