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Q91055 (CRVP_HELHO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine-rich venom protein helothermine

Short name=CRVP HLTx
OrganismHeloderma horridum horridum (Mexican beaded lizard)
Taxonomic identifier8552 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaAnguimorphaNeoanguimorphaHelodermatidaeHeloderma

Protein attributes

Sequence length242 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alters a variety of ion channel activities, including voltage-gated potassium channels (Kv) (Ref.3), voltage-gated calcium channels (L-, N-, and P-type) (Cav) (Ref.4) and ryanodine receptors (RyR) (Ref.1). Is toxic to mice (causes lethargy, partial paralysis of rear limbs and lowering of body temperature). Ref.1 Ref.3 Ref.4

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Miscellaneous

IC50=0.52 µM on IA-type current, and 0.86 µM on delayed rectifier current (Ref.3).

Sequence similarities

Belongs to the CRISP family.

Contains 1 SCP domain.

Contains 1 ShKT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2
Chain20 – 242223Cysteine-rich venom protein helothermine
PRO_0000006272

Regions

Domain41 – 169129SCP
Domain205 – 23733ShKT

Amino acid modifications

Disulfide bond77 ↔ 155 By similarity
Disulfide bond94 ↔ 170 By similarity
Disulfide bond150 ↔ 167 By similarity
Disulfide bond189 ↔ 196 By similarity
Disulfide bond192 ↔ 201 By similarity
Disulfide bond205 ↔ 237 By similarity
Disulfide bond214 ↔ 231 By similarity
Disulfide bond223 ↔ 235 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91055 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0E183FC2F925DF3C

FASTA24227,493
        10         20         30         40         50         60 
MILLSLYLCL AAMLHQSEGE ASPKLPGLMT SNPDQQTEIT DKHNNLRRIV EPTASNMLKM 

        70         80         90        100        110        120 
TWSNKIAQNA QRSANQCTLE HTSKEERTID GVECGENLFF SSAPYTWSYA IQNWFDERKY 

       130        140        150        160        170        180 
FRFNYGPTAQ NVMIGHYTQV VWYRSYELGC AIAYCPDQPT YKYYQVCQYC PGGNIRSRKY 

       190        200        210        220        230        240 
TPYSIGPPCG DCPDACDNGL CTNPCKQNDV YNNCPDLKKQ VGCGHPIMKD CMATCKCLTE 


IK 

« Hide

References

[1]"Primary structure and properties of helothermine, a peptide toxin that blocks ryanodine receptors."
Morrissette J., Kraetzschmar J., Haendler B., El-Hayek R., Mochca-Morales J., Martin B.M., Patel J.R., Moss R.L., Schleuning W.-D., Coronado R., Possani L.D.
Biophys. J. 68:2280-2288(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
[2]"Isolation and characterization of helothermine, a novel toxin from Heloderma horridum horridum (Mexican beaded lizard) venom."
Mochca-Morales J., Martin B.M., Possani L.D.
Toxicon 28:299-309(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-39, CHARACTERIZATION.
Tissue: Venom.
[3]"The toxin helothermine affects potassium currents in newborn rat cerebellar granule cells."
Nobile M., Magnelli V., Lagostena L., Mochca-Morales J., Possani L.D., Prestipino G.
J. Membr. Biol. 139:49-55(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Helothermine, a lizard venom toxin, inhibits calcium current in cerebellar granules."
Nobile M., Noceti F., Prestipino G., Possani L.D.
Exp. Brain Res. 110:15-20(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13619 mRNA. Translation: AAC59730.1.
PIRA34859.

3D structure databases

ProteinModelPortalQ91055.
SMRQ91055. Positions 34-241.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004184.

Family and domain databases

Gene3D3.40.33.10. 1 hit.
InterProIPR001283. Allrgn_V5/Tpx1.
IPR018244. Allrgn_V5/Tpx1_CS.
IPR014044. CAP_domain.
IPR013871. Cysteine_rich_secretory.
IPR003582. ShKT_dom.
[Graphical view]
PANTHERPTHR10334. PTHR10334. 1 hit.
PfamPF00188. CAP. 1 hit.
PF08562. Crisp. 1 hit.
[Graphical view]
PRINTSPR00837. V5TPXLIKE.
SMARTSM00198. SCP. 1 hit.
[Graphical view]
SUPFAMSSF55797. SSF55797. 1 hit.
PROSITEPS01009. CRISP_1. 1 hit.
PS51670. SHKT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCRVP_HELHO
AccessionPrimary (citable) accession number: Q91055
Secondary accession number(s): P46693
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families