P79729 · DHH_DANRE

Function

function

Intercellular signal essential for a variety of patterning events during development.

Features

Showing features for binding site.

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QRCKDCLYKLAIAVMNQWPGVRLRVTEAWDEDGHHPPGSLHYEGRAVDITTSDRDTKKYGLLAQLAVEAGFDWVHYESKYHVHCSVKA
TypeIDPosition(s)Description
Binding site26Ca2+ 1 (UniProtKB | ChEBI)
Binding site27Ca2+ 1 (UniProtKB | ChEBI)
Binding site27Ca2+ 2 (UniProtKB | ChEBI)
Binding site30Ca2+ 2 (UniProtKB | ChEBI)
Binding site32Ca2+ 2 (UniProtKB | ChEBI)
Binding site41Zn2+ (UniProtKB | ChEBI)
Binding site48Zn2+ (UniProtKB | ChEBI)
Binding site83Zn2+ (UniProtKB | ChEBI)

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 Componentextracellular region
Cellular Componentplasma membrane
Molecular Functionmetal ion binding
Molecular Functionpeptidase activity
Biological Processcell-cell signaling
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Desert hedgehog protein
  • Short names
    DHH

Gene names

    • Name
      dhh

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    P79729
  • Secondary accessions
    • Q9YGU3

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
Note: Desert hedgehog protein N-product: Cell membrane; Lipid-anchor; Extracellular side. The N-terminal peptide remains associated with the cell surface. Desert hedgehog protein C-product: Secreted, extracellular space. The C-terminal peptide diffuses from the cell.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000587501-88Desert hedgehog protein

Post-translational modification

The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-terminal fragment (N-product). This covalent modification appears to play an essential role in restricting the spatial distribution of the protein activity to the cell surface. The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity).

Keywords

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Domain

The desert hedgehog protein N-product binds calcium and zinc ions; this stabilizes the protein fold and is essential for protein-protein interactions mediated by this domain.

Sequence similarities

Belongs to the hedgehog family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    88
  • Mass (Da)
    10,069
  • Last updated
    2002-04-03 v2
  • Checksum
    E3D34A0C36677FA6
QRCKDCLYKLAIAVMNQWPGVRLRVTEAWDEDGHHPPGSLHYEGRAVDITTSDRDTKKYGLLAQLAVEAGFDWVHYESKYHVHCSVKA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
Q4PLX3Q4PLX3_DANREdhh447

Features

Showing features for non-terminal residue, sequence conflict.

TypeIDPosition(s)Description
Non-terminal residue1
Sequence conflict17in Ref. 2; AAB38613
Sequence conflict22in Ref. 2; AAB38613
Sequence conflict28in Ref. 2; AAB38613
Sequence conflict34-38in Ref. 2; AAB38613
Sequence conflict56-57in Ref. 2; AAB38613
Sequence conflict61in Ref. 2; AAB38613
Sequence conflict64in Ref. 2; AAB38613
Non-terminal residue88

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF071236
EMBL· GenBank· DDBJ
AAD15931.1
EMBL· GenBank· DDBJ
Genomic DNA
U51388
EMBL· GenBank· DDBJ
AAB38613.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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