UniProt functional annotation for Q16658



	UniProt functional annotation for Q16658

UniProt code: Q16658.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Actin-binding protein that contains 2 major actin binding sites (PubMed:21685497, PubMed:23184945). Organizes filamentous actin into parallel bundles (PubMed:20393565, PubMed:21685497, PubMed:23184945). Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (PubMed:22155786). Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (PubMed:20393565, PubMed:21685497, PubMed:23184945). Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (PubMed:22155786). {ECO:0000269|PubMed:20137952, ECO:0000269|PubMed:20393565, ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:23184945, ECO:0000269|PubMed:9362073, ECO:0000269|PubMed:9571235}.

Subunit: Interacts with RUFY3 (via N-terminus); the interaction induces neuron axon development (By similarity). Interacts with NGFR (By similarity). Associates with CTNNB1 (By similarity). Interacts with PLXNB3 (PubMed:21706053). {ECO:0000250|UniProtKB:P85845, ECO:0000250|UniProtKB:Q61553, ECO:0000269|PubMed:21706053}.

Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21706053, ECO:0000269|PubMed:9571235}. Cytoplasm, cell cortex {ECO:0000269|PubMed:21685497}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:3525578, ECO:0000269|PubMed:9571235}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:21706053}. Cell projection, filopodium {ECO:0000269|PubMed:20137952, ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:3525578}. Cell projection, invadopodium {ECO:0000269|PubMed:20137952}. Cell projection, microvillus {ECO:0000269|PubMed:9571235}. Cell junction {ECO:0000269|PubMed:9571235}. Note=Colocalized with RUFY3 and F-actin at filipodia of the axonal growth cone. Colocalized with DBN1 and F- actin at the transitional domain of the axonal growth cone (By similarity). {ECO:0000250|UniProtKB:Q61553, ECO:0000269|PubMed:21706053}.

Tissue specificity: Ubiquitous.

Domain: Composed of four fascin beta-trefoil domains. {ECO:0000269|PubMed:20393565, ECO:0000269|PubMed:20434460, ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:23184945}.

Ptm: Phosphorylation at Ser-39 inhibits actin-binding (PubMed:8647875, PubMed:8999969). Phosphorylation is required for the reorganization of the actin cytoskeleton in response to NGF (PubMed:22155786). {ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:8647875, ECO:0000269|PubMed:8999969}.

Similarity: Belongs to the fascin family. {ECO:0000305}.

Sequence caution: Sequence=AAH07539.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Actin-binding protein that contains 2 major actin binding sites (PubMed:21685497, PubMed:23184945). Organizes filamentous actin into parallel bundles (PubMed:20393565, PubMed:21685497, PubMed:23184945). Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (PubMed:22155786). Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (PubMed:20393565, PubMed:21685497, PubMed:23184945). Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (PubMed:22155786). {ECO:0000269\|PubMed:20137952, ECO:0000269\|PubMed:20393565, ECO:0000269\|PubMed:21685497, ECO:0000269\|PubMed:22155786, ECO:0000269\|PubMed:23184945, ECO:0000269\|PubMed:9362073, ECO:0000269\|PubMed:9571235}.


Subunit:		Interacts with RUFY3 (via N-terminus); the interaction induces neuron axon development (By similarity). Interacts with NGFR (By similarity). Associates with CTNNB1 (By similarity). Interacts with PLXNB3 (PubMed:21706053). {ECO:0000250\|UniProtKB:P85845, ECO:0000250\|UniProtKB:Q61553, ECO:0000269\|PubMed:21706053}.
Subcellular location:		Cytoplasm, cytosol {ECO:0000269\|PubMed:21706053, ECO:0000269\|PubMed:9571235}. Cytoplasm, cell cortex {ECO:0000269\|PubMed:21685497}. Cytoplasm, cytoskeleton {ECO:0000269\|PubMed:21685497, ECO:0000269\|PubMed:3525578, ECO:0000269\|PubMed:9571235}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269\|PubMed:21706053}. Cell projection, filopodium {ECO:0000269\|PubMed:20137952, ECO:0000269\|PubMed:21685497, ECO:0000269\|PubMed:3525578}. Cell projection, invadopodium {ECO:0000269\|PubMed:20137952}. Cell projection, microvillus {ECO:0000269\|PubMed:9571235}. Cell junction {ECO:0000269\|PubMed:9571235}. Note=Colocalized with RUFY3 and F-actin at filipodia of the axonal growth cone. Colocalized with DBN1 and F- actin at the transitional domain of the axonal growth cone (By similarity). {ECO:0000250\|UniProtKB:Q61553, ECO:0000269\|PubMed:21706053}.
Tissue specificity:		Ubiquitous.
Domain:		Composed of four fascin beta-trefoil domains. {ECO:0000269\|PubMed:20393565, ECO:0000269\|PubMed:20434460, ECO:0000269\|PubMed:21685497, ECO:0000269\|PubMed:23184945}.
Ptm:		Phosphorylation at Ser-39 inhibits actin-binding (PubMed:8647875, PubMed:8999969). Phosphorylation is required for the reorganization of the actin cytoskeleton in response to NGF (PubMed:22155786). {ECO:0000269\|PubMed:22155786, ECO:0000269\|PubMed:8647875, ECO:0000269\|PubMed:8999969}.
Similarity:		Belongs to the fascin family. {ECO:0000305}.
Sequence caution:		Sequence=AAH07539.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};