VSPH7_TRIST
ID VSPH7_TRIST Reviewed; 260 AA.
AC Q71QI0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Snake venom serine protease homolog KN7;
DE AltName: Full=Serine proteinase-like protein KN7;
DE Flags: Precursor;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Tsai I.-H., Wang Y.-M.;
RT "Identification of geographic variations and cloning of venom proteins of
RT Trimeresurus stejnegeri: serine proteases and phospholipases.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Snake venom serine protease homolog that may act in the
CC hemostasis system of the prey. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved His at position 67, which is expected to
CC be an active site residue. {ECO:0000305}.
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DR EMBL; AF395777; AAQ02907.1; -; mRNA.
DR AlphaFoldDB; Q71QI0; -.
DR SMR; Q71QI0; -.
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:InterPro.
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; 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; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Secreted;
KW Serine protease homolog; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250"
FT /id="PRO_0000295832"
FT CHAIN 25..260
FT /note="Snake venom serine protease homolog KN7"
FT /id="PRO_5000061229"
FT DOMAIN 25..251
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 28721 MW; 38C639F9214F791C CRC64;
MVLIRVLANL LILQLSYAQK SSELIIGGDE CNINEHRFLV ALYTFRSRRF HCGGTLINQE
WVLSAARCDR KNIRIKLGMH STNVTNEDVQ TRVPKEKFFC LSSKTYTKWN KDIMLIRLKR
PVNNSTHIAP VSLPSNPPSL GLVCRVMGWG TISATKETHP DVPHCANINI LDYSVCRAAY
ARLPATSRTL CAGILEGGKD TCHGDSGGPL ICNGQVQGIV SWGGHPCGQP RKPGLYTKVF
DHLDWIKSII AGNKDATCPP
