VSPH2_MACLB
ID VSPH2_MACLB Reviewed; 260 AA.
AC Q9PT40;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Snake venom serine protease homolog 2;
DE AltName: Full=Venom serine proteinase-like protein 2;
DE Short=VLP2;
DE Flags: Precursor;
OS Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX NCBI_TaxID=8709;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=11223258; DOI=10.1016/s0378-1119(00)00571-0;
RA Siigur E., Aaspollu A., Siigur J.;
RT "Sequence diversity of Vipera lebetina snake venom gland serine proteinase
RT homologs -- result of alternative-splicing or genome alteration.";
RL Gene 263:199-203(2001).
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|PubMed:11223258}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:11223258}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ251153; CAB62591.1; -; mRNA.
DR AlphaFoldDB; Q9PT40; -.
DR SMR; Q9PT40; -.
DR MEROPS; S01.509; -.
DR PRIDE; Q9PT40; -.
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 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; Secreted;
KW Serine protease homolog; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /evidence="ECO:0000250"
FT /id="PRO_0000028425"
FT CHAIN 25..260
FT /note="Snake venom serine protease homolog 2"
FT /id="PRO_0000028426"
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 253
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; 28894 MW; C4E22A96F47BA90B CRC64;
MVLIRVLANL LVLQLSYAQK SSELVIGGDE CNINEHPFPV ALHTARSKRF YCAGTLINQE
WVLTAARCDR KNIRIILGVH SKNVPNEDQQ IRVPKEKFFC LSSKTYTRWD KDIMLIRLKK
PVNDSTHIVP LSLPSSPPSV GSVCRIMGWG TITTTKVTYP DVPHCANINM FDYSVCRKVY
RKLPEKSRTL CAGILQGGID SCKVDNGGPL ICNGQIQGIV SWGGHPCAQP HKPALYTNVF
DYTDWIQSII AGNITATCPP
