VKT1_VIPAA
ID VKT1_VIPAA Reviewed; 90 AA.
AC P00991; Q6XPY8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Kunitz-type serine protease inhibitor 1;
DE AltName: Full=Venom basic protease inhibitor 1;
DE AltName: Full=Venom trypsin inhibitor I;
DE Short=cVamTi;
DE Flags: Precursor;
OS Vipera ammodytes ammodytes (Western sand viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=8705;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=12860400; DOI=10.1016/s0014-5793(03)00693-8;
RA Zupunski V., Kordis D., Gubensek F.;
RT "Adaptive evolution in the snake venom Kunitz/BPTI protein family.";
RL FEBS Lett. 547:131-136(2003).
RN [2]
RP PROTEIN SEQUENCE OF 25-85, FUNCTION, DISULFIDE BONDS, AND PYROGLUTAMATE
RP FORMATION AT GLN-25.
RC TISSUE=Venom;
RX PubMed=6639951; DOI=10.1016/0167-4838(83)90189-9;
RA Ritonja A., Meloun B., Gubensek F.;
RT "The primary structure of Vipera ammodytes venom trypsin inhibitor I.";
RL Biochim. Biophys. Acta 748:429-435(1983).
RN [3]
RP AMINO-ACID COMPOSITION, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=6602050; DOI=10.1111/j.1432-1033.1983.tb07481.x;
RA Ritonja A., Turk V., Gubensek F.;
RT "Serine proteinase inhibitors from Vipera ammodytes venom. Isolation and
RT kinetic studies.";
RL Eur. J. Biochem. 133:427-432(1983).
CC -!- FUNCTION: Serine protease inhibitor that principally inhibits trypsin
CC (Ki=0.34 nM). Also inhibits alpha-chymotrypsin (Ki=270 nM), plasmin,
CC plasma and pancreatic kallikrein. {ECO:0000269|PubMed:6602050,
CC ECO:0000269|PubMed:6639951}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR EMBL; AY217781; AAP04484.1; -; mRNA.
DR PIR; A01222; TIVIT1.
DR AlphaFoldDB; P00991; -.
DR SMR; P00991; -.
DR MEROPS; I02.062; -.
DR PRIDE; P00991; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; KU; 1.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Pyrrolidone carboxylic acid; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:6639951"
FT CHAIN 25..85
FT /note="Kunitz-type serine protease inhibitor 1"
FT /id="PRO_0000155444"
FT PROPEP 86..90
FT /id="PRO_0000376930"
FT DOMAIN 31..81
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 41..42
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:6639951"
FT DISULFID 31..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT ECO:0000269|PubMed:6639951"
FT DISULFID 40..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT ECO:0000269|PubMed:6639951"
FT DISULFID 56..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT ECO:0000269|PubMed:6639951"
SQ SEQUENCE 90 AA; 9831 MW; 05C82A7DD4B41EA3 CRC64;
MSSGGLLLLL GLLTLWAELT PVSGQDHPKF CYLPADPGRC KAHIPRFYYD SASNKCNKFI
YGGCPGNANN FKTWDECRQT CGASAMGRPT
