ID   VSPAF_TRIAB             Reviewed;         258 AA.
AC   P0CJ41;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Alpha-fibrinogenase albofibrase;
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Precursor;
OS   Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops
OS   albolabris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=8765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16373075; DOI=10.1016/j.toxicon.2005.11.003;
RA   Rojnuckarin P., Muanpasitporn C., Chanhome L., Arpijuntarangkoon J.,
RA   Intragumtornchai T.;
RT   "Molecular cloning of novel serine proteases and phospholipases A2 from
RT   green pit viper (Trimeresurus albolabris) venom gland cDNA library.";
RL   Toxicon 47:279-287(2006).
RN   [2]
RP   FUNCTION.
RX   PubMed=17346761; DOI=10.1016/j.toxicon.2007.01.015;
RA   Muanpasitporn C., Rojnuckarin P.;
RT   "Expression and characterization of a recombinant fibrinogenolytic serine
RT   protease from green pit viper (Trimeresurus albolabris) venom.";
RL   Toxicon 49:1083-1089(2007).
CC   -!- FUNCTION: The recombinant protein has fibrinogenolytic activity against
CC       the Aalpha chain (FGA) of fibrinogen. Activates plasminogen (PLG) (is
CC       4-fold less active than urokinase). Has weak thrombin-like enzyme
CC       activity. Has enzymatic activity against a trypsin-like substrate (S-
CC       3013) and shows a weaker activity on an activated protein C substrate
CC       (S-3125). {ECO:0000269|PubMed:17346761}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Has no enzymatic activity against a chymotrypsin
CC       substrate (S-3015). Does not show fibrinolytic activity against Bbeta
CC       (FGB) and gamma chains (FGG) of fibrinogen. Does not show activity on
CC       prothrombin (F2), factor V (F5) and factor X (F10). Does not induce
CC       platelet aggregation (PubMed:17346761). {ECO:0000305|PubMed:17346761}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0CJ41; -.
DR   SMR; P0CJ41; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Fibrinogenolytic toxin; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Plasminogen activation; Protease;
KW   Secreted; Serine protease; Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000416390"
FT   CHAIN           25..258
FT                   /note="Alpha-fibrinogenase albofibrase"
FT                   /id="PRO_0000416391"
FT   DOMAIN          25..249
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        98..256
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        142..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        174..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        200..225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   VARIANT         60
FT                   /note="V -> A (in albofibrase-2)"
SQ   SEQUENCE   258 AA;  28001 MW;  2F0C9E37514F66FD CRC64;
     MVLIRVLANL LILQLSYAQK SSELVVGGDE CNINEHHSLV AIFNSTGFFC SGTLINQEWV
     VTAAHCDSKN FKMKFGAHSK KLLNEDEQIR NPKEKFICPN KKSNEILDKD IMLIKLDSPV
     SNSAHIAPLS LPSSPPSVGS VCRIMGWGST TPIEVTYPDV PYCANINLLD DAECKPGYPE
     LLPEYRTLCA GIVQGGKDTC GGDSGGPLIC NEKLHGIVSY GGHPCGQSHK PGIYTNVFDY
     NDWIQSIIAG NTDATCLS