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Protein

Pardaxin P-4

Gene
N/A
Organism
Pardachirus marmoratus (Finless sole) (Achirus marmoratus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis.2 Publications

GO - Biological processi

Keywordsi

Molecular functionToxin
Biological processIon transport, Transport

Protein family/group databases

TCDBi1.A.66.1.1. the pardaxin (pardaxin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Pardaxin P-4
Alternative name(s):
Pardaxin P1a
Pardaxin Pa4
OrganismiPardachirus marmoratus (Finless sole) (Achirus marmoratus)
Taxonomic identifieri31087 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataCarangariaPleuronectiformesPleuronectoideiSoleidaePardachirus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Membrane, Secreted, Target cell membrane, Target membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000447851 – 33Pardaxin P-4Add BLAST33

Interactioni

Subunit structurei

Monomer. In aqueous solution exists as a tetramer (By similarity).By similarity

Structurei

Secondary structure

133
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi6 – 9Combined sources4
Turni10 – 14Combined sources5
Helixi15 – 25Combined sources11
Turni26 – 31Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XC0NMR-A1-33[»]
2KNSNMR-A1-33[»]
ProteinModelPortaliP81861.
SMRiP81861.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81861.

Family & Domainsi

Domaini

Consists of a C-terminal hydrophilic region and a predominantly hydrophobic remainder.

Sequence similaritiesi

Belongs to the pardaxin family.Curated

Keywords - Domaini

Transmembrane

Family and domain databases

InterProiView protein in InterPro
IPR009990. Pardaxin.
PfamiView protein in Pfam
PF07425. Pardaxin. 1 hit.
PIRSFiPIRSF037561. Pardaxin. 1 hit.

Sequencei

Sequence statusi: Complete.

P81861-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
GFFALIPKII SSPLFKTLLS AVGSALSSSG GQE
Length:33
Mass (Da):3,324
Last modified:May 30, 2000 - v1
Checksum:i5ABFF96A16FC910D
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XC0NMR-A1-33[»]
2KNSNMR-A1-33[»]
ProteinModelPortaliP81861.
SMRiP81861.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.A.66.1.1. the pardaxin (pardaxin) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP81861.

Family and domain databases

InterProiView protein in InterPro
IPR009990. Pardaxin.
PfamiView protein in Pfam
PF07425. Pardaxin. 1 hit.
PIRSFiPIRSF037561. Pardaxin. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPAP4_PARMA
AccessioniPrimary (citable) accession number: P81861
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 63 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.