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Q91055

- CRVP_HELHO

UniProt

Q91055 - CRVP_HELHO

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Protein
Cysteine-rich venom protein helothermine
Gene
N/A
Organism
Heloderma horridum horridum (Mexican beaded lizard)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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

Keywords - Molecular functioni

Calcium channel impairing toxin, Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Ryanodine-sensitive calcium-release channel impairing toxin, Toxin, Voltage-gated calcium channel impairing toxin, Voltage-gated potassium channel impairing toxin

Protein family/group databases

TCDBi8.B.9.1.3. the triflin toxin (triflin or crisp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine-rich venom protein helothermine
Short name:
CRVP HLTx
OrganismiHeloderma horridum horridum (Mexican beaded lizard)
Taxonomic identifieri8552 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaAnguimorphaNeoanguimorphaHelodermatidaeHeloderma

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 Publication
Add
BLAST
Chaini20 – 242223Cysteine-rich venom protein helothermine
PRO_0000006272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi77 ↔ 155 By similarity
Disulfide bondi94 ↔ 170 By similarity
Disulfide bondi150 ↔ 167 By similarity
Disulfide bondi189 ↔ 196 By similarity
Disulfide bondi192 ↔ 201 By similarity
Disulfide bondi205 ↔ 237 By similarity
Disulfide bondi214 ↔ 231 By similarity
Disulfide bondi223 ↔ 235 By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

3D structure databases

ProteinModelPortaliQ91055.
SMRiQ91055. Positions 34-241.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 169129SCP
Add
BLAST
Domaini205 – 23733ShKT
Add
BLAST

Sequence similaritiesi

Belongs to the CRISP family.
Contains 1 SCP domain.
Contains 1 ShKT domain.

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG004184.

Family and domain databases

Gene3Di3.40.33.10. 1 hit.
InterProiIPR001283. Allrgn_V5/Tpx1.
IPR018244. Allrgn_V5/Tpx1_CS.
IPR014044. CAP_domain.
IPR013871. Cysteine_rich_secretory.
IPR003582. ShKT_dom.
[Graphical view]
PANTHERiPTHR10334. PTHR10334. 1 hit.
PfamiPF00188. CAP. 1 hit.
PF08562. Crisp. 1 hit.
[Graphical view]
PRINTSiPR00837. V5TPXLIKE.
SMARTiSM00198. SCP. 1 hit.
[Graphical view]
SUPFAMiSSF55797. SSF55797. 1 hit.
PROSITEiPS01009. CRISP_1. 1 hit.
PS51670. SHKT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91055-1 [UniParc]FASTAAdd to Basket

« Hide

MILLSLYLCL AAMLHQSEGE ASPKLPGLMT SNPDQQTEIT DKHNNLRRIV    50
EPTASNMLKM TWSNKIAQNA QRSANQCTLE HTSKEERTID GVECGENLFF 100
SSAPYTWSYA IQNWFDERKY FRFNYGPTAQ NVMIGHYTQV VWYRSYELGC 150
AIAYCPDQPT YKYYQVCQYC PGGNIRSRKY TPYSIGPPCG DCPDACDNGL 200
CTNPCKQNDV YNNCPDLKKQ VGCGHPIMKD CMATCKCLTE IK 242
Length:242
Mass (Da):27,493
Last modified:November 1, 1996 - v1
Checksum:i0E183FC2F925DF3C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13619 mRNA. Translation: AAC59730.1.
PIRiA34859.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13619 mRNA. Translation: AAC59730.1 .
PIRi A34859.

3D structure databases

ProteinModelPortali Q91055.
SMRi Q91055. Positions 34-241.
ModBasei Search...

Protein family/group databases

TCDBi 8.B.9.1.3. the triflin toxin (triflin or crisp) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG004184.

Family and domain databases

Gene3Di 3.40.33.10. 1 hit.
InterProi IPR001283. Allrgn_V5/Tpx1.
IPR018244. Allrgn_V5/Tpx1_CS.
IPR014044. CAP_domain.
IPR013871. Cysteine_rich_secretory.
IPR003582. ShKT_dom.
[Graphical view ]
PANTHERi PTHR10334. PTHR10334. 1 hit.
Pfami PF00188. CAP. 1 hit.
PF08562. Crisp. 1 hit.
[Graphical view ]
PRINTSi PR00837. V5TPXLIKE.
SMARTi SM00198. SCP. 1 hit.
[Graphical view ]
SUPFAMi SSF55797. SSF55797. 1 hit.
PROSITEi PS01009. CRISP_1. 1 hit.
PS51670. SHKT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCRVP_HELHO
AccessioniPrimary (citable) accession number: Q91055
Secondary accession number(s): P46693
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

IC50=0.52 µM on IA-type current, and 0.86 µM on delayed rectifier current (1 Publication).

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi