P17452 · TOXA_PASMD

  • Protein
    Dermonecrotic toxin
  • Gene
    toxA
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

This is a dermonecrotic toxin. This osteolytic toxin, induces bone resorption. Potent mitogen. This toxin is associated with the severe progressive form of the atrophic rhinitis, a major respiratory disease in pigs.

Miscellaneous

Closely spaced cysteine and histidine residues may provide the toxin with an affinity for metal.
The sequence shown is that of strain NCTC 12178.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentextracellular region
Cellular Componenthost cell plasma membrane
Cellular Componentmembrane
Molecular Functionphospholipase activity
Molecular Functionphospholipid binding
Molecular Functiontoxin activity
Biological Processsymbiont-mediated killing of host cell
Biological Processsymbiont-mediated perturbation of host G protein-coupled receptor signal transduction pathway

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Dermonecrotic toxin
  • Short names
    DNT
  • Alternative names
    • Mitogenic toxin
    • PMT

Gene names

    • Name
      toxA

Organism names

  • Taxonomic identifier
  • Strains
    • NCTC 12178
    • CVI 47459
    • LFB3
    • CH05
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Pasteurella

Accessions

  • Primary accession
    P17452
  • Secondary accessions
    • Q57008

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane402-422Helical

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant853in strain: CVI 47459

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000726351-1285Dermonecrotic toxin

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO P17452Vim P201524EBI-9541048, EBI-299269

Protein-protein interaction databases

Family & Domains

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,285
  • Mass (Da)
    146,383
  • Last updated
    2001-04-27 v2
  • Checksum
    E67A9FCA58C107DA
MKTKHFFNSDFTVKGKSADEIFRRLCTDHPDKQLNNVKWKEVFINRFGQMMLDTPNPRKIVEKIINEGLEKQGLKNIDPETTYFNIFSSSDSSDGNVFHYNSLSESYRVTDACLMNIFVERYFDDWDLLNSLASNGIYSVGKEGAYYPDHDYGPEYNPVWGPNEQIYHSRVIADILYARSVWDEFKKYFMEYWQKYAQLYTEMLSDTFLAMAIQQYTRQTLTDEGFLMVCNTYYGNKEEVQITLLDIYGYPSTDIICIEQKGLPTPKVILYIPGGTQPFVEFLNTDDLKQWIAWHLKDNKHMVAFRKHFSLKQRQEGETFTGIDKALQYIAEESPEWPANKYILYNPTHLETENLFNIMMKRTEQRMLEDSDVQIRSNSEATRDYALSLLETFISQLSAIDMLVPAVGIPINFALSATALGLSSDIVVNGDSYEKRKYGIGSLVQSALFTGINLIPVISETAEILSSFSRTEEDIPAFFTEEQALAQRFEIVEEELHSISPDDPPREITDENLHKIRLVRLNNENQPLVVLRRLGGNKFIRIEPITFQEIKGSLVSEVINPVTNKTYYVSNAKLLGGSPYSPFRIGLEGVWTPEVLKARASVIGKPIGESYKRILAKLQRIHNSNILDERQGLMHELMELIDLYEESQPSSERLNAFRELRTQLEKALYLPEMEALKKQILQIPNKGSGAARFLLRTAMNEMAGKTSESTADLIRFALQDTVISAPFRGYAGAIPEAIDFPVKYVIEDISVFDKIQTNYWELPAYESWNEGSNSALLPGLLRESQSKGMLSKCRIIENSLYIGHSYEEMFYSISPYSNQVGGPYELYPFTFFSMLQEVQGDLGFEQAFATRNFFNTLVSDRLSLMENTMLLTESFDYTPWDAIYGDINYDEQFAAMSINERIEKCMNTYRGVAFQNSSKSIDFFLNNLTTFIDNGLTEIAISDLPYDIVQQEISQFLQGSNEWKTLDAMLFNLDKGDINGAFRKLLQSAKDNNIKFRAIGHSDNSVPPFNNPYKSLYYKGNIIAEAIEKLDREGQKFVVFADSSLLNSTPGTGRPMPGLVQYLKIPATVVDSDGAWQFLPDVASSRVPIEVTELENWQVLTPPQGKILGLKQFKLTAGFPTEQSRLPLLENSVSEDLREELMQKIDAIKNDVKMNSLVCMEAGSCDSVSPKVAARLKDMGLEAGMGASITWWRREGGMEFSHQMHTTASFKFAGKEFAVDASHLQFVHDQLDTTILILPVDDWALEIAQRNRAINPFVEYVSKTGNMLALFMPPLFTKPRLTRAL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict304in Ref. 1; CAA35885
Sequence conflict775in Ref. 1; CAA35885

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X51512
EMBL· GenBank· DDBJ
CAA35885.1
EMBL· GenBank· DDBJ
Genomic DNA
X52478
EMBL· GenBank· DDBJ
CAA36717.1
EMBL· GenBank· DDBJ
Genomic DNA
Z28388
EMBL· GenBank· DDBJ
CAA82233.1
EMBL· GenBank· DDBJ
Genomic DNA
X57775
EMBL· GenBank· DDBJ
CAA40921.1
EMBL· GenBank· DDBJ
Genomic DNA
AF240778
EMBL· GenBank· DDBJ
AAL55665.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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