VKT_ERIMA
ID VKT_ERIMA Reviewed; 62 AA.
AC P24541;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Kunitz-type serine protease inhibitor {ECO:0000303|PubMed:1743283};
DE AltName: Full=Venom trypsin inhibitor {ECO:0000303|PubMed:1743283, ECO:0000305};
OS Eristicophis macmahoni (Leaf-nosed viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Eristicophis.
OX NCBI_TaxID=110227;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=1743283; DOI=10.1016/0014-5793(91)81361-b;
RA Siddiqi A.R., Zaidi Z.H., Joernvall H.;
RT "Purification and characterization of a Kunitz-type trypsin inhibitor from
RT Leaf-nosed viper venom.";
RL FEBS Lett. 294:141-143(1991).
RN [2]
RP FUNCTION, AND RECOMBINANT EXPRESSION.
RX PubMed=30648553; DOI=10.1016/j.bbrc.2019.01.014;
RA Liu Y., Zhang J., Wang R., Wu Y., Wang W., Xin X., Du M., Cao Y., Zhang H.;
RT "Identification of novel Kv1.3 targeting venom peptides by a single round
RT of autocrine-based selection.";
RL Biochem. Biophys. Res. Commun. 509:954-959(2019).
CC -!- FUNCTION: Serine protease inhibitor that inhibits trypsin
CC (PubMed:1743283). The recombinant protein also barely blocks voltage-
CC gated potassium channel Kv1.3/KCNA3 (3.70% inhibition at 60 nM of
CC toxin) (PubMed:30648553). {ECO:0000269|PubMed:1743283,
CC ECO:0000269|PubMed:30648553}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1743283}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:1743283}.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR PIR; S19327; S19327.
DR AlphaFoldDB; P24541; -.
DR SMR; P24541; -.
DR MEROPS; I02.062; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin 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; Ion channel impairing toxin;
KW Potassium channel impairing toxin; Protease inhibitor; Secreted;
KW Serine protease inhibitor; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT CHAIN 1..62
FT /note="Kunitz-type serine protease inhibitor"
FT /evidence="ECO:0000269|PubMed:1743283"
FT /id="PRO_0000155437"
FT DOMAIN 2..52
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 12..13
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250"
FT DISULFID 2..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 11..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 27..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 62 AA; 6772 MW; 0A2ED0ADB20DF938 CRC64;
FCYLPDDPGV CKAHIPRFYY NPASNKCKNF IYGGCGGNAN NFETRAECRH TCVASGKGGP
RP
