VSP1_GLOUS
ID VSP1_GLOUS Reviewed; 262 AA.
AC Q91053;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Thrombin-like enzyme calobin-1;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Calobin I;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
OS Gloydius ussuriensis (Ussuri mamushi) (Gloydius blomhoffii ussuriensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=35671;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Venom gland;
RX PubMed=8797081; DOI=10.1093/oxfordjournals.jbchem.a021319;
RA Hahn B.S., Yang K.Y., Park E.M., Chang I.M., Kim Y.S.;
RT "Purification and molecular cloning of calobin, a thrombin-like enzyme from
RT Agkistrodon caliginosus (Korean viper).";
RL J. Biochem. 119:835-843(1996).
CC -!- FUNCTION: Thrombin-like snake venom serine protease. Has a coagulant
CC activity. Acts on alpha-chains of fibrinogen (FGA) generating
CC fibrinopeptide A. {ECO:0000269|PubMed:8797081}.
CC -!- ACTIVITY REGULATION: Strongly inhibited by PMSF, and moderately by
CC benzamidine and soybean trypsin inhibitor.
CC {ECO:0000269|PubMed:8797081}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8797081}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8797081}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:8797081}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8797081}.
CC -!- MISCELLANEOUS: Does not show lysine esterase and caseinolytic activity.
CC {ECO:0000305|PubMed:8797081}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; U32937; AAC59906.1; -; mRNA.
DR PIR; JC4803; JC4803.
DR AlphaFoldDB; Q91053; -.
DR SMR; Q91053; -.
DR MEROPS; S01.335; -.
DR iPTMnet; Q91053; -.
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 Blood coagulation cascade activating toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /id="PRO_0000028369"
FT CHAIN 25..262
FT /note="Thrombin-like enzyme calobin-1"
FT /id="PRO_0000028370"
FT DOMAIN 25..253
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 67
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:8797081"
FT DISULFID 31..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 52..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 100..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 144..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 176..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 204..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 262 AA; 28908 MW; 7F318C933006244D CRC64;
MVLISVLANL LILQLSYAQK SSELVIGGDE CNINEHRFLV ALYNSRSRTL FCGGTLINQE
WVLTAAHCER KNFRIKLGIH SKKVPNEDEQ TRVPKEKFFC LSSKNYTLWD KDIMLIRLDS
PVSNSEHIAP LSLPSSPPSV GSVCRIMGWG RISPTKETYP DVPHCANINL LEYEMCRAPY
PEFGLPATSR TLCAGILEGG KDTCRGDSGG PLICNGQFQG IASWGDDPCA QPHKPAAYTK
VFDHLDWIQS IIAGNTDASC PP
