VSPCR_CROAD
ID VSPCR_CROAD Reviewed; 262 AA.
AC F8S114;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Thrombin-like enzyme crotalase;
DE Short=SVTLE;
DE EC=3.4.21.74;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease 2;
DE Short=SVSP;
DE Flags: Precursor;
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=21255598; DOI=10.1016/j.toxicon.2011.01.008;
RA Rokyta D.R., Wray K.P., Lemmon A.R., Lemmon E.M., Caudle S.B.;
RT "A high-throughput venom-gland transcriptome for the eastern diamondback
RT rattlesnake (Crotalus adamanteus) and evidence for pervasive positive
RT selection across toxin classes.";
RL Toxicon 57:657-671(2011).
RN [2]
RP PROTEIN SEQUENCE OF 25-262, FUNCTION, GLYCOSYLATION, AND 3D-STRUCTURE
RP MODELING.
RC TISSUE=Venom;
RX PubMed=10348716;
RA Henschen-Edman A.H., Theodor I., Edwards B.F., Pirkle H.;
RT "Crotalase, a fibrinogen-clotting snake venom enzyme: primary structure and
RT evidence for a fibrinogen recognition exosite different from thrombin.";
RL Thromb. Haemost. 81:81-86(1999).
RN [3]
RP FUNCTION.
RX PubMed=5132665; DOI=10.1016/s0021-9258(19)34138-9;
RA Markland F.S., Damus P.S.;
RT "Purification and properties of a thrombin-like enzyme from the venom of
RT Crotalus adamanteus (Eastern diamondback rattlesnake).";
RL J. Biol. Chem. 246:6460-6473(1971).
RN [4]
RP FUNCTION.
RX PubMed=1014024; DOI=10.1016/0041-0101(76)90046-5;
RA Markland F.S., Pirkle H.;
RT "Characterization of a thrombin-like enzyme from Crotalus adamanteus
RT (Eastern diamondback rattlesnake).";
RL Toxicon 14:412-413(1976).
RN [5]
RP FUNCTION.
RX PubMed=854881; DOI=10.1016/0049-3848(77)90158-x;
RA Markland F.S., Pirkle H.;
RT "Thrombin-like enzyme from the venom of Crotalus adamanteus (eastern
RT diamondback rattlesnake).";
RL Thromb. Res. 10:487-494(1977).
RN [6]
RP FUNCTION.
RX PubMed=7043462; DOI=10.1073/pnas.79.6.1688;
RA Markland F.S., Kettner C., Schiffman S., Shaw E., Bajwa S.S., Reddy K.N.,
RA Kirakossian H., Patkos G.B., Theodor I., Pirkle H.;
RT "Kallikrein-like activity of crotalase, a snake venom enzyme that clots
RT fibrinogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1688-1692(1982).
CC -!- FUNCTION: Thrombin-like snake venom protein that release fibrinopeptide
CC A from fibrinogen (FGA). Shows both kinin-releasing and coagulant
CC activities. {ECO:0000269|PubMed:1014024, ECO:0000269|PubMed:10348716,
CC ECO:0000269|PubMed:5132665, ECO:0000269|PubMed:7043462,
CC ECO:0000269|PubMed:854881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form
CC fibrin, and release fibrinopeptide A. The specificity of further
CC degradation of fibrinogen varies with species origin of the enzyme.;
CC EC=3.4.21.74;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated: contains mannose, galactose, N-acetylglucosamine,
CC and fucose. {ECO:0000269|PubMed:10348716}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; HQ414118; AEJ31996.1; -; mRNA.
DR AlphaFoldDB; F8S114; -.
DR SMR; F8S114; -.
DR MEROPS; S01.181; -.
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 GO; GO:0008217; P:regulation of blood pressure; 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 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.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Hypotensive agent; Protease; Secreted; Serine protease; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:10348716"
FT /id="PRO_0000416597"
FT CHAIN 25..262
FT /note="Thrombin-like enzyme crotalase"
FT /id="PRO_5000771379"
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:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 52..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 102..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"
FT CONFLICT 49
FT /note="S -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="E -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="K -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 262 AA; 29457 MW; 865DA30A569279A1 CRC64;
MVLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHRFLV ALYDYWSQSF LCGGTLINEE
WVLTAKHCDR THILIYVGVH DRSVQFDKEQ RRFPKEKYFF DCSNNFTKWD KDIMLIRLNK
PVSYSEHIAP LSLPSSPPIV GSVCRAMGWG QTTSPQETLP DVPHCANINL LDYEVCRTAH
PQFRLPATSR TLCAGVLEGG IDTCNRDSGG PLICNGQFQG IVFWGPDPCA QPDKPGLYTK
VFDHLDWIQS IIAGEKTVNC PP
