VKTA1_CYRHA
ID VKTA1_CYRHA Reviewed; 88 AA.
AC D2Y2C2;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Kunitz-type U15-theraphotoxin-Hhn1a;
DE Short=U15-TRTX-Hhn1a;
DE AltName: Full=Kunitz-type serine protease inhibitor hainantoxin-XI;
DE Short=HNTX-XI;
DE Flags: Precursor;
OS Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Haplopelma.
OX NCBI_TaxID=209901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA / MRNA].
RC TISSUE=Venom gland;
RX PubMed=20192277; DOI=10.1021/pr1000016;
RA Tang X., Zhang Y., Hu W., Xu D., Tao H., Yang X., Li Y., Jiang L.,
RA Liang S.;
RT "Molecular diversification of peptide toxins from the tarantula Haplopelma
RT hainanum (Ornithoctonus hainana) venom based on transcriptomic, peptidomic,
RT and genomic analyses.";
RL J. Proteome Res. 9:2550-2564(2010).
CC -!- FUNCTION: Serine protease inhibitor that inhibits chymotrypsin and
CC blocks voltage-gated potassium channels (Kv). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. 03 (sub-Kunitz)
CC subfamily. {ECO:0000305}.
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DR EMBL; GU292999; ADB56815.1; -; mRNA.
DR EMBL; GU293131; ADB56947.1; -; Genomic_DNA.
DR AlphaFoldDB; D2Y2C2; -.
DR SMR; D2Y2C2; -.
DR ArachnoServer; AS002024; U15-theraphotoxin-Hhn1a.
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 GO; GO:0044562; P:envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism; IEA:UniProt.
DR CDD; cd00109; KU; 1.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Ion channel impairing toxin;
KW Potassium channel impairing toxin; Protease inhibitor; Secreted;
KW Serine protease inhibitor; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..33
FT /evidence="ECO:0000250"
FT /id="PRO_0000400978"
FT PEPTIDE 34..88
FT /note="Kunitz-type U15-theraphotoxin-Hhn1a"
FT /id="PRO_0000400979"
FT DOMAIN 37..85
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 47..48
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250"
FT DISULFID 37..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 60..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 88 AA; 9892 MW; 533DAEC17975DE17 CRC64;
MGTARFLRAV LLLSVLLMVT FPALLSAEHH DGRVDICRLP SDSGDCLRFF EMWYFDGTTC
TKFVYGGYGG NDNRFPTEKA CMKRCAKA
