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Protein

Basic phospholipase A2 homolog Tx-beta

Gene
N/A
Organism
Micrurus tener tener (Texas coral snake)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Heterodimer: snake venom phospholipase that potently activates mouse H+-gated sodium channel ASIC1/ACCN2 (acid-sensitive ion channel 1) expressed in Xenopus oocytes. Both alternatively spliced isoforms ASIC1a and ASIC1b are activated, with a higher potency for ASIC1a (EC(50)=9.4 nM) vs ASIC1b (EC(50)=23 nM). The ASIC3/ACCN3 subtype is also sensitive to the heterodimer, but with a lower potency (EC(50)=830 nM). On ASIC2a/ACCN1, the toxin shows a very weak activation, but produces a remarkable potentiation (>100-fold) of protons when the extracellular pH drops below neutrality. The toxin interacts with the extracellular region of the channel, since responses are only observed in the outside-out configuration. In vivo, the heterodimer elicits robust pain-related behavior in mice by activation of ASIC1/ACCN2 channels on capsaicin-sensitive nerve fibers.1 Publication
Monomer: does not have phospholipase A2 activity but may maintain some lipid-binding character from its PLA2 lineage, which could aid in effecting neuronal depolarization.1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phospholipase A2 activity Source: InterPro

GO - Biological processi

  1. lipid catabolic process Source: InterPro
  2. phospholipid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Basic phospholipase A2 homolog Tx-beta
Short name:
svPLA2 homolog
Alternative name(s):
MitTx-beta
OrganismiMicrurus tener tener (Texas coral snake)
Taxonomic identifieri1114302 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeMicrurus

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 – 30301 PublicationAdd
BLAST
Chaini31 – 149119Basic phospholipase A2 homolog Tx-betaPRO_5000828218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 100By similarity
Disulfide bondi55 ↔ 148By similarity
Disulfide bondi57 ↔ 73By similarity
Disulfide bondi72 ↔ 130By similarity
Disulfide bondi79 ↔ 123By similarity
Disulfide bondi89 ↔ 116By similarity
Disulfide bondi109 ↔ 121By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chains.1 Publication

Structurei

Secondary structure

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 409Combined sources
Helixi47 – 493Combined sources
Turni50 – 523Combined sources
Turni54 – 563Combined sources
Helixi68 – 8720Combined sources
Turni91 – 933Combined sources
Helixi104 – 1063Combined sources
Helixi115 – 13319Combined sources
Helixi138 – 1403Combined sources
Helixi145 – 1473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NTWX-ray2.07C31-149[»]
4NTXX-ray2.27C31-149[»]
4NTYX-ray2.65C31-149[»]
ProteinModelPortaliG9I930.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

G9I930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKMNPAHLL VLAAVCVSLL GASSIPPQAL NLNQFRLMIK CTNDRVWADF
60 70 80 90 100
VDYGCYCVAR DSNTPVDDLD RCCQAQKQCY DEAVKVHGCK PLVMFYSFEC
110 120 130 140
RYLASDLDCS GNNTKCRNFV CNCDRTATLC ILTATYNRNN HKIDPSRCQ
Length:149
Mass (Da):16,793
Last modified:February 22, 2012 - v1
Checksum:i4CF027CBCA751BE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JN613326 mRNA. Translation: AET85560.1.

Cross-referencesi

Web resourcesi

Protein Spotlight

The poison in pain - Issue 140 of July 2012

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JN613326 mRNA. Translation: AET85560.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NTWX-ray2.07C31-149[»]
4NTXX-ray2.27C31-149[»]
4NTYX-ray2.65C31-149[»]
ProteinModelPortaliG9I930.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A heteromeric Texas coral snake toxin targets acid-sensing ion channels to produce pain."
    Bohlen C.J., Chesler A.T., Sharif-Naeini R., Medzihradszky K.F., Zhou S., King D., Sanchez E.E., Burlingame A.L., Basbaum A.I., Julius D.
    Nature 479:410-414(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBUNIT.
    Tissue: Venom and Venom gland.

Entry informationi

Entry nameiPA2HB_MICTN
AccessioniPrimary (citable) accession number: G9I930
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: February 22, 2012
Last modified: January 7, 2015
This is version 20 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

This toxin has been studied to probe molecular mechanisms underlying pain sensation. By targeting ASIC1/ACCN2, it reveals an unexpected contribution of this channel to nociception.
The heterodimeric toxin does not affect ASIC2b/ACCN1, ASIC4/ACCN4, Kv2.1/KCNB1, Cav3.3/CACNA1I, ENaC/SCNN1A, TRPA1, TRPV1, TRPV3, TRPM8, P2X2/P2RX2, and 5-HT3/HTR3A channels.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.