VKT1_TRILK
ID VKT1_TRILK Reviewed; 176 AA.
AC W4VSH9;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Kunitz-type U19-barytoxin-Tl1a;
DE Short=U19-BATX-Tl1a;
DE AltName: Full=Kunitz-type serine protease inhibitor Kunitz-1;
DE Flags: Precursor;
OS Trittame loki (Brush-footed trapdoor spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Barychelidae; Trittame.
OX NCBI_TaxID=1295018;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=24351713; DOI=10.3390/toxins5122488;
RA Undheim E.A., Sunagar K., Herzig V., Kely L., Low D.H., Jackson T.N.,
RA Jones A., Kurniawan N., King G.F., Ali S.A., Antunes A., Ruder T.,
RA Fry B.G.;
RT "A proteomics and transcriptomics investigation of the venom from the
RT barychelid spider Trittame loki (brush-foot trapdoor).";
RL Toxins 5:2488-2503(2013).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: This protein was not detected in the venom by mass
CC spectrometry. {ECO:0000305|PubMed:24351713}.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=JAB84508.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GAQE01000046; JAB84508.1; ALT_INIT; Transcribed_RNA.
DR AlphaFoldDB; W4VSH9; -.
DR SMR; W4VSH9; -.
DR ArachnoServer; AS001862; U19-barytoxin-Tl1a.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0044562; P:envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism; IEA:UniProt.
DR CDD; cd00109; KU; 2.
DR Gene3D; 4.10.410.10; -; 2.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 2.
DR SUPFAM; SSF57362; SSF57362; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Repeat; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..176
FT /note="Kunitz-type U19-barytoxin-Tl1a"
FT /id="PRO_0000429204"
FT DOMAIN 28..78
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 106..156
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT REGION 155..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 38..39
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250"
FT SITE 116..117
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250"
FT DISULFID 28..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 37..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 53..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 106..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 115..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 131..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 176 AA; 19275 MW; CD7A7103DD0131B2 CRC64;
MNFELIYVSS LLLGICLANQ ADVVPSDCNL PADAGMCYAY FPMFFYDASS RKCLNFIYGG
CGGNANRFWS EAECMEKCGG GGGGGGSSDG SQKTAKMLNL DLGDICSLEK KVGPCKAHMP
RYYFNRETGL CEEFIYGGCS GNHNNFQTKE QCESFCAPGN SPRPEEETRK RTKQSY
