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TauPI-stichotoxin-Hcr2b (TauPI-SHTX-Hcr2b) (Analgesic polypeptide HC1) (APHC1)

 VKT1_HETCR              Reviewed;          78 AA.
B2G331;
10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
23-MAY-2018, entry version 46.
RecName: Full=TauPI-stichotoxin-Hcr2b {ECO:0000305};
Short=TauPI-SHTX-Hcr2b {ECO:0000303|PubMed:22683676};
AltName: Full=Analgesic polypeptide HC1 {ECO:0000303|PubMed:18579526};
Short=APHC1 {ECO:0000303|PubMed:18579526};
Flags: Precursor;
Heteractis crispa (Leathery sea anemone) (Radianthus macrodactylus).
Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
Stichodactylidae; Heteractis.
NCBI_TaxID=175771;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-37, FUNCTION, MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
TISSUE=Nematoblast;
PubMed=18579526; DOI=10.1074/jbc.M800776200;
Andreev Y.A., Kozlov S.A., Koshelev S.G., Ivanova E.A.,
Monastyrnaya M.M., Kozlovskaya E.P., Grishin E.V.;
"Analgesic compound from sea anemone Heteractis crispa is the first
polypeptide inhibitor of vanilloid receptor 1 (TRPV1).";
J. Biol. Chem. 283:23914-23921(2008).
[2]
FUNCTION.
Andreev Y.A., Mosharova I.V., Kozlov S.A., Korolkova Y.V.,
Grishin E.V.;
"Sea anemone peptides modulate TRPV1 activity and produce analgesia
without hyperthermic effect.";
Submitted (OCT-2013) to UniProtKB.
[3]
FUNCTION.
PubMed=22982418; DOI=10.1016/j.lfs.2012.09.001;
Philyppov I.B., Paduraru O.N., Andreev Y.A., Grishin E.V., Shuba Y.M.;
"Modulation of TRPV1-dependent contractility of normal and diabetic
bladder smooth muscle by analgesic toxins from sea anemone Heteractis
crispa.";
Life Sci. 91:912-920(2012).
[4]
NOMENCLATURE.
PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
Oliveira J.S., Fuentes-Silva D., King G.F.;
"Development of a rational nomenclature for naming peptide and protein
toxins from sea anemones.";
Toxicon 60:539-550(2012).
-!- FUNCTION: This protease inhibitor shows two different activities,
inhibition of the capsaicin receptor and of serine proteases. It
partially (max 50%) and reversibly inhibits mammalian TRPV1
(IC(50)=54 nM), the capsaicin receptor, a non-selective cation
channel expressed by sensory neurons of the pain pathway
(PubMed:18579526). The second activity is a weak inhibition of
trypsin and chymotrypsin activity (Ki are 1 uM and 5 uM,
respectively) (PubMed:18579526). In vivo, it significantly
prolongs tail-flick latency and reduces capsaicin-induced acute
pain (analgesic effect on mammals) (PubMed:18579526).
{ECO:0000269|PubMed:18579526, ECO:0000269|PubMed:22982418,
ECO:0000269|Ref.2}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18579526}.
Nematocyst {ECO:0000269|PubMed:18579526}.
-!- MASS SPECTROMETRY: Mass=6187.0; Method=MALDI; Range=23-78;
Evidence={ECO:0000269|PubMed:18579526};
-!- SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone
type 2 potassium channel toxin subfamily. {ECO:0000305}.
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EMBL; AM933240; CAP69846.1; -; mRNA.
ProteinModelPortal; B2G331; -.
SMR; B2G331; -.
PRIDE; B2G331; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0042151; C:nematocyst; IDA:UniProtKB.
GO; GO:0008200; F:ion channel inhibitor activity; IDA:UniProtKB.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0044465; P:modulation of sensory perception of pain in other organism; IDA:UniProtKB.
CDD; cd00109; KU; 1.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
Pfam; PF00014; Kunitz_BPTI; 1.
PRINTS; PR00759; BASICPTASE.
SMART; SM00131; KU; 1.
SUPFAM; SSF57362; SSF57362; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Nematocyst; Neurotoxin;
Protease inhibitor; Secreted; Serine protease inhibitor; Signal;
Toxin.
SIGNAL 1 22 {ECO:0000269|PubMed:18579526}.
CHAIN 23 78 TauPI-stichotoxin-Hcr2b.
{ECO:0000305|PubMed:18579526}.
/FTId=PRO_5000342888.
DOMAIN 26 76 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
SITE 36 37 Reactive bond for trypsin.
{ECO:0000250|UniProtKB:P31713}.
DISULFID 26 76 {ECO:0000250|UniProtKB:P31713}.
DISULFID 35 59 {ECO:0000250|UniProtKB:P31713}.
DISULFID 51 72 {ECO:0000250|UniProtKB:P31713}.
SEQUENCE 78 AA; 8565 MW; 9F812F0E2471C841 CRC64;
MKGTFLICLI LIAGFSFKST QAGSICLEPK VVGPCTAYFR RFYFDSETGK CTVFIYGGCE
GNGNNFETLR ACRAICRA


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