VSP2_PROFL
ID VSP2_PROFL Reviewed; 260 AA.
AC O13057;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Snake venom serine protease 2;
DE Short=SVSP 2;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=TLF2;
OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=8941719; DOI=10.1016/s0014-5793(96)01144-1;
RA Deshimaru M., Ogawa T., Nakashima K., Nobuhisa I., Chijiwa T.,
RA Shimohigashi Y., Fukumaki Y., Niwa M., Yamashina I., Hattori S., Ohno M.;
RT "Accelerated evolution of crotalinae snake venom gland serine proteases.";
RL FEBS Lett. 397:83-88(1996).
CC -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC system of the prey. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Arg-67 is present instead of the conserved His which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; D67079; BAA19977.1; -; mRNA.
DR AlphaFoldDB; O13057; -.
DR SMR; O13057; -.
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 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW 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_0000028387"
FT CHAIN 25..260
FT /note="Snake venom serine protease 2"
FT /id="PRO_0000028388"
FT DOMAIN 25..251
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
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 100..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 144..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 176..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 202..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 260 AA; 28641 MW; D0D0A5394CBF9B4A CRC64;
MVLIRVLANL LILQLFYAQK SSELIIGGDE CNINEHRFLV ALYTFRSRRL HCGGILINQE
WVLSAARCNR KNIRIQLGMH STNVINEDVQ TRVPKEKFFC LSSKTHTRWN KDIMLIRLNS
PVNNSTHIAP VSLPSNPPSL GSVCRVMGWG TISATKETHP DVPHCANINI LDYSVCRAAY
ARLPATSRTL CAGILEGGKD SCKADSGGPL ICNGEIQGIV SRGGHSCGQP RKPGLYTKVF
DHLDWIKSII AGNKDAICPP