D3ZHV2 · MACF1_RAT

  • Protein
    Microtubule-actin cross-linking factor 1
  • Gene
    Macf1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity).
Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity).
Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity).
Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity).
May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity).
Plays a key role in wound healing and epidermal cell migration (By similarity).
Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity).
As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity).

Features

Showing features for binding site.

154305001,0001,5002,0002,5003,0003,5004,0004,5005,000
TypeIDPosition(s)Description
Binding site5096Ca2+ 1 (UniProtKB | ChEBI)
Binding site5098Ca2+ 1 (UniProtKB | ChEBI)
Binding site5100Ca2+ 1 (UniProtKB | ChEBI)
Binding site5102Ca2+ 1 (UniProtKB | ChEBI)
Binding site5107Ca2+ 1 (UniProtKB | ChEBI)
Binding site5132Ca2+ 2 (UniProtKB | ChEBI)
Binding site5134Ca2+ 2 (UniProtKB | ChEBI)
Binding site5136Ca2+ 2 (UniProtKB | ChEBI)
Binding site5138Ca2+ 2 (UniProtKB | ChEBI)
Binding site5143Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentactin cytoskeleton
Cellular Componentcytoplasm
Cellular ComponentGolgi apparatus
Cellular Componentmembrane
Cellular Componentmicrotubule
Cellular Componentmicrotubule cytoskeleton
Cellular Componentplasma membrane
Cellular Componentpostsynaptic density
Cellular Componentruffle membrane
Molecular Functionactin binding
Molecular Functionactin filament binding
Molecular FunctionATP hydrolysis activity
Molecular Functioncalcium ion binding
Molecular Functionmicrotubule binding
Molecular Functionmicrotubule minus-end binding
Molecular Functionstructural molecule activity
Biological Processcell migration
Biological Processestablishment or maintenance of cell polarity
Biological ProcessGolgi to plasma membrane protein transport
Biological Processintermediate filament cytoskeleton organization
Biological Processmesoderm formation
Biological Processpositive regulation of axon extension
Biological Processpositive regulation of Wnt signaling pathway
Biological Processpost-translational protein targeting to endoplasmic reticulum membrane
Biological Processregulation of cell migration
Biological Processregulation of epithelial cell migration
Biological Processregulation of focal adhesion assembly
Biological Processregulation of microtubule-based process
Biological Processregulation of neuron projection arborization
Biological ProcessWnt signaling pathway
Biological Processwound healing

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Microtubule-actin cross-linking factor 1
  • Alternative names
    • Actin cross-linking family 7

Gene names

    • Name
      Macf1
    • Synonyms
      Acf7, Aclp7, Macf

Organism names

  • Taxonomic identifier
  • Strain
    • Brown Norway
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    D3ZHV2

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Golgi apparatus
Cell membrane
Membrane
Note: The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules (By similarity).
Localizes to the tips of microtubules. Associated with the minus-end of microtubules via interaction with CAMSAP3. APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization (By similarity).

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004097091-5430Microtubule-actin cross-linking factor 1
Modified residue4Phosphoserine
Modified residue35Phosphoserine
Modified residue57Phosphoserine
Modified residue280Phosphoserine
Modified residue1122Phosphoserine
Modified residue1367Phosphoserine
Modified residue1376Phosphoserine
Modified residue1860Phosphoserine
Modified residue2429Phosphoserine
Modified residue2454Phosphoserine
Modified residue2769Phosphoserine
Modified residue2895Phosphoserine
Modified residue3368Phosphothreonine
Modified residue4074Phosphoserine
Modified residue4252N6-acetyllysine
Modified residue5009Phosphoserine
Modified residue5296Phosphothreonine
Modified residue5321Phosphoserine
Modified residue5334Phosphoserine
Modified residue5372Phosphoserine
Modified residue5375Phosphoserine

Post-translational modification

Phosphorylated on serine residues in the C-terminal tail by GSK3B. Phosphorylation inhibits microtubule-binding and this plays a critical role in bulge stem cell migration and skin wound repair. Wnt-signaling can repress phosphorylation (By similarity).

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with MAPRE1, CLASP1, CLASP2 and GOLGA4 (By similarity).
Interacts with AXIN1 and LRP6 (PubMed:16815997).
Found in a complex composed of MACF1, APC; AXIN1, CTNNB1 and GSK3B (PubMed:16815997).
Interacts with CAMSAP3 (By similarity).

Protein-protein interaction databases

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, domain, repeat.

TypeIDPosition(s)Description
Region1-47Disordered
Region1-295Actin-binding
Compositional bias8-28Basic and acidic residues
Domain78-181Calponin-homology (CH) 1
Repeat148-171LRR 1
Domain194-298Calponin-homology (CH) 2
Repeat240-264LRR 2
Repeat377-399LRR 3
Repeat441-464LRR 4
Domain868-925SH3
Repeat1050-1073LRR 5
Repeat1128-1154LRR 6
Repeat1187-1210LRR 7
Repeat1257-1282LRR 8
Repeat1579-1602LRR 9
Repeat1629-1653LRR 10
Repeat1816-1891Spectrin 1
Repeat1869-1891LRR 11
Repeat1933-2041Spectrin 2
Repeat2058-2083LRR 12
Repeat2194-2220LRR 13
Repeat2399-2507Spectrin 3
Repeat2444-2467LRR 14
Repeat2534-2557LRR 15
Repeat2702-2725LRR 16
Repeat2733-2837Spectrin 4
Repeat2842-2945Spectrin 5
Repeat2984-3009LRR 17
Repeat3105-3127LRR 18
Repeat3169-3274Spectrin 6
Repeat3214-3237LRR 19
Repeat3281-3383Spectrin 7
Repeat3388-3491Spectrin 8
Repeat3714-3818Spectrin 9
Repeat3737-3761LRR 20
Repeat3825-3927Spectrin 10
Repeat3846-3870LRR 21
Repeat4047-4152Spectrin 11
Repeat4157-4261Spectrin 12
Repeat4267-4370Spectrin 13
Repeat4375-4481Spectrin 14
Repeat4486-4589Spectrin 15
Repeat4538-4561LRR 22
Repeat4594-4700Spectrin 16
Repeat4707-4808Spectrin 17
Repeat4812-4916Spectrin 18
Region4993-5023Disordered
Domain5083-5118EF-hand 1
Domain5119-5154EF-hand 2
Domain5159-5231GAR
Region5159-5430C-terminal tail
Region5247-5430Disordered
Compositional bias5266-5345Polar residues
Region5355-53704 X 4 AA tandem repeats of [GS]-S-R-[AR]
Compositional bias5377-5430Polar residues

Domain

The C-terminal tail is required for phosphorylation by GSK3B and for microtubule-binding.

Sequence similarities

Belongs to the plakin or cytolinker family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    5,430
  • Mass (Da)
    619,600
  • Last updated
    2010-04-20 v1
  • Checksum
    C15B030F89CD5FBF

Computationally mapped potential isoform sequences

There are 10 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0G2JU82A0A0G2JU82_RATMacf15474
M9MMM9M9MMM9_RATMacf15431
A0A8I6AP57A0A8I6AP57_RATMacf17375
A0A8I6ATL8A0A8I6ATL8_RATMacf17417
A0A0G2K9T4A0A0G2K9T4_RATMacf17382
A0A0G2JWA8A0A0G2JWA8_RATMacf17352
A0A8I6AAP8A0A8I6AAP8_RATMacf17425
A0A8I5ZYF6A0A8I5ZYF6_RATMacf17395
A0A8I5YCC2A0A8I5YCC2_RATMacf17416
A0A8I5ZUE8A0A8I5ZUE8_RATMacf17345

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias8-28Basic and acidic residues
Compositional bias5266-5345Polar residues
Compositional bias5377-5430Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC114512
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC131172
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp