Q8IID4 · DYHC2_PLAF7

Function

function

Acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (By similarity).

Biotechnology

Possible candidate for an effective malaria vaccine as determined by epitope response in sera.

Features

Showing features for binding site.

152515001,0001,5002,0002,5003,0003,5004,0004,5005,000
TypeIDPosition(s)Description
Binding site1895-1902ATP (UniProtKB | ChEBI)
Binding site2224-2231ATP (UniProtKB | ChEBI)
Binding site2546-2553ATP (UniProtKB | ChEBI)
Binding site2890-2897ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentdynein complex
Cellular Componentmicrotubule
Cellular Componentmicrotubule associated complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functioncytoskeletal motor activity
Molecular Functiondynein intermediate chain binding
Molecular Functiondynein light intermediate chain binding
Molecular Functionmicrotubule motor activity
Molecular Functionminus-end-directed microtubule motor activity
Biological Processmicrotubule-based movement

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Dynein heavy chain-like protein 2

Gene names

    • ORF names
      PF11_0240, PF3D7_1122900

Organism names

Accessions

  • Primary accession
    Q8IID4
  • Secondary accessions
    • A0A143ZYP5

Proteomes

Organism-specific databases

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue (large scale data).

Type
IDPosition(s)Source
Description
ChainPRO_00003707501-5251UniProtDynein heavy chain-like protein 2
Modified residue (large scale data)154PTMeXchangePhosphoserine
Modified residue (large scale data)1043PTMeXchangePhosphoserine
Modified residue (large scale data)4029PTMeXchangePhosphoserine
Modified residue (large scale data)4105PTMeXchangePhosphothreonine
Modified residue (large scale data)4115PTMeXchangePhosphothreonine
Modified residue (large scale data)4195PTMeXchangePhosphothreonine
Modified residue (large scale data)4205PTMeXchangePhosphothreonine
Modified residue (large scale data)4812PTMeXchangePhosphoserine
Modified residue (large scale data)4815PTMeXchangePhosphoserine

Proteomic databases

Expression

Keywords

Interaction

Subunit

Consists of at least two heavy chains and a number of intermediate and light chains.

Protein-protein interaction databases

Structure

3D structure databases

Family & Domains

Features

Showing features for repeat, compositional bias, region, coiled coil.

Type
IDPosition(s)Description
Repeat37-87Kelch 1
Repeat95-143Kelch 2
Compositional bias140-173Polar residues
Region140-188Disordered
Compositional bias174-188Basic and acidic residues
Repeat266-317Kelch 3
Repeat318-367Kelch 4
Repeat372-421Kelch 5
Region686-732Disordered
Coiled coil1155-1225
Coiled coil1544-1610
Region1554-1598Disordered
Repeat1639-1685Kelch 6
Region1802-1825Disordered
Coiled coil2136-2188
Region2152-2171Disordered
Repeat2447-2494Kelch 7
Compositional bias3138-3152Polar residues
Region3138-3163Disordered
Compositional bias3652-3676Polar residues
Region3652-3686Disordered
Compositional bias4042-4060Basic and acidic residues
Region4042-4250Disordered
Compositional bias4061-4091Acidic residues
Compositional bias4092-4250Basic and acidic residues
Region4280-4299Disordered
Compositional bias4773-4800Polar residues
Region4773-4824Disordered
Region4910-4948Disordered

Domain

Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function.

Sequence similarities

Belongs to the dynein heavy chain family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    5,251
  • Mass (Da)
    617,381
  • Last updated
    2003-03-01 v1
  • MD5 Checksum
    CB3AFFDF5C6B8F5EEE634761A3721529

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias140-173Polar residues
Compositional bias174-188Basic and acidic residues
Compositional bias3138-3152Polar residues
Compositional bias3652-3676Polar residues
Compositional bias4042-4060Basic and acidic residues
Compositional bias4061-4091Acidic residues
Compositional bias4092-4250Basic and acidic residues
Compositional bias4773-4800Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LN999945
EMBL· GenBank· DDBJ
CZT98891.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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