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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) (PubMed:8071987), voltage-gated calcium channels (L-, N-, and P-type) (Cav) (PubMed:8817251) and ryanodine receptors (RyR) (PubMed:7647234). 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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 242223Cysteine-rich venom protein helotherminePRO_0000006272Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

3D structure databases

ProteinModelPortaliQ91055.
SMRiQ91055. Positions 34-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 169129SCPAdd
BLAST
Domaini205 – 23733ShKTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the CRISP family.Curated
Contains 1 SCP domain.Curated
Contains 1 ShKT domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MILLSLYLCL AAMLHQSEGE ASPKLPGLMT SNPDQQTEIT DKHNNLRRIV
60 70 80 90 100
EPTASNMLKM TWSNKIAQNA QRSANQCTLE HTSKEERTID GVECGENLFF
110 120 130 140 150
SSAPYTWSYA IQNWFDERKY FRFNYGPTAQ NVMIGHYTQV VWYRSYELGC
160 170 180 190 200
AIAYCPDQPT YKYYQVCQYC PGGNIRSRKY TPYSIGPPCG DCPDACDNGL
210 220 230 240
CTNPCKQNDV YNNCPDLKKQ VGCGHPIMKD CMATCKCLTE IK
Length:242
Mass (Da):27,493
Last modified:November 1, 1996 - v1
Checksum:i0E183FC2F925DF3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13619 mRNA. Translation: AAC59730.1.
PIRiA34859.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13619 mRNA. Translation: AAC59730.1 .
PIRi A34859.

3D structure databases

ProteinModelPortali Q91055.
SMRi Q91055. Positions 34-241.
ModBasei Search...
MobiDBi 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: October 29, 2014
This is version 75 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