ID   VSP3_PROMU              Reviewed;         257 AA.
AC   Q91509;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Beta-fibrinogenase mucrofibrase-3;
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Precursor;
OS   Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=103944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=7811255; DOI=10.1006/bbrc.1994.2865;
RA   Hung C.-C., Huang K.F., Chiou S.-H.;
RT   "Characterization of one novel venom protease with beta-fibrinogenase
RT   activity from the Taiwan habu (Trimeresurus mucrosquamatus): purification
RT   and cDNA sequence analysis.";
RL   Biochem. Biophys. Res. Commun. 205:1707-1715(1994).
CC   -!- FUNCTION: Snake venom serine protease with fibrinogenolytic activities.
CC       Cleaves beta-chain of fibrinogen (FGB) efficiently and shows relatively
CC       lower activity on alpha-chain. {ECO:0000269|PubMed:7811255}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7811255}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not have activity on gamma-chains of fibrinogen
CC       (FGG). {ECO:0000305|PubMed:7811255}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; X83223; CAA58223.1; -; mRNA.
DR   RefSeq; NP_001310175.1; NM_001323246.1.
DR   RefSeq; XP_015671559.1; XM_015816073.1.
DR   AlphaFoldDB; Q91509; -.
DR   SMR; Q91509; -.
DR   MEROPS; S01.343; -.
DR   MEROPS; S01.344; -.
DR   GeneID; 107287552; -.
DR   KEGG; pmur:107287552; -.
DR   OrthoDB; 1314811at2759; -.
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   Disulfide bond; Fibrinogenolytic toxin; Hemostasis impairing toxin;
KW   Hydrolase; Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028411"
FT   CHAIN           25..257
FT                   /note="Beta-fibrinogenase mucrofibrase-3"
FT                   /id="PRO_0000028412"
FT   DOMAIN          25..248
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        64
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        49..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        97..255
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        141..209
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        173..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        199..224
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   257 AA;  28159 MW;  781E8531FB641416 CRC64;
     MVLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHPFLV LVYYDDYQCG GTLLNEEWVL
     TAAHCNGKDM EIYLGVHSKK VPNKDVQRRV PKEKFFCDSS KTYTKWNKDI MLIRLDRPVR
     KSAHIAPLSL PSSPPSVGSV CRVMGWGTIT SPQETYPDVP HCANINLLDY EVCRAAYAGL
     PATSRTLCAG ILEGGKDSCV GDSGGPLICN GQFQGIVSWG GDPCAQPREP GVYTNVFDHL
     DWIKGIIAGN TDVTCPL