UniProt functional annotation for Q9Y4D1



	UniProt functional annotation for Q9Y4D1

UniProt code: Q9Y4D1.

Organism: Homo sapiens (Human).

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

Function: Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments. Involved in building functional cilia (PubMed:16630611, PubMed:17482208). Involved in the organization of the subapical actin network in multiciliated epithelial cells (By similarity). Together with DAAM2, required for myocardial maturation and sarcomere assembly (By similarity). {ECO:0000250|UniProtKB:B0DOB5, ECO:0000250|UniProtKB:Q8BPM0, ECO:0000269|PubMed:16630611, ECO:0000269|PubMed:17482208}.

Subunit: Homodimer. Interacts with CIP4, FNBP1 and FNBP1L. Interacts with the SH3 domains of Abl, BTK, endophilin, spectrin and SRC. Binds specifically to GTP-bound CDC42 and RHOA. Interacts with INTU; INTU mediates the indirect interaction between DAAM1 and NPHP4. {ECO:0000269|PubMed:16630611, ECO:0000269|PubMed:17482208}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:16630611}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26644512}. Note=Perinuclear.

Tissue specificity: Expressed in all tissues examined.

Domain: The C-terminal DAD domain may participate in intramolecular interactions with the N-terminus.

Domain: The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250|UniProtKB:O08808}.

Similarity: Belongs to the formin homology family. {ECO:0000305}.

Sequence caution: Sequence=BAA31641.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAC04230.1; Type=Erroneous initiation; 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:		Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments. Involved in building functional cilia (PubMed:16630611, PubMed:17482208). Involved in the organization of the subapical actin network in multiciliated epithelial cells (By similarity). Together with DAAM2, required for myocardial maturation and sarcomere assembly (By similarity). {ECO:0000250\|UniProtKB:B0DOB5, ECO:0000250\|UniProtKB:Q8BPM0, ECO:0000269\|PubMed:16630611, ECO:0000269\|PubMed:17482208}.


Subunit:		Homodimer. Interacts with CIP4, FNBP1 and FNBP1L. Interacts with the SH3 domains of Abl, BTK, endophilin, spectrin and SRC. Binds specifically to GTP-bound CDC42 and RHOA. Interacts with INTU; INTU mediates the indirect interaction between DAAM1 and NPHP4. {ECO:0000269\|PubMed:16630611, ECO:0000269\|PubMed:17482208}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:16630611}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269\|PubMed:26644512}. Note=Perinuclear.
Tissue specificity:		Expressed in all tissues examined.
Domain:		The C-terminal DAD domain may participate in intramolecular interactions with the N-terminus.
Domain:		The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity). {ECO:0000250\|UniProtKB:O08808}.
Similarity:		Belongs to the formin homology family. {ECO:0000305}.
Sequence caution:		Sequence=BAA31641.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAC04230.1; Type=Erroneous initiation; Evidence={ECO:0000305};