Protein Name:
Microtubule-actin cross-linking factor 1
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UniprotKB/SwissProt ID: D3ZHV2 (D3ZHV2)
Gene Name:
Macf1
Organism: Rattus norvegicus (Rat)
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)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Cytoplasm, cytoskeleton. Cytoplasm. Golgi apparatus. Cell membrane. Cell projection, ruffle membrane. Membrane
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of D3ZHV2
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
3798 |
QKAVLQEKTE C LIQQYEAVSL |
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| 2 |
666 |
ETLGKLETQY C KLKETSSFRM |
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