FMNL3

Protein-coding gene in humans
FMNL3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4EAH

Identifiers
AliasesFMNL3, FHOD3, WBP-3, WBP3, FRL2, formin like 3
External IDsOMIM: 616288; MGI: 109569; HomoloGene: 69101; GeneCards: FMNL3; OMA:FMNL3 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for FMNL3
Genomic location for FMNL3
Band12q13.12Start49,636,499 bp[1]
End49,708,165 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for FMNL3
Genomic location for FMNL3
Band15|15 F1Start99,215,106 bp[2]
End99,268,363 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • sural nerve

  • appendix

  • right coronary artery

  • stromal cell of endometrium

  • lymph node

  • Achilles tendon

  • apex of heart

  • granulocyte

  • left coronary artery

  • right lung
Top expressed in
  • primary oocyte

  • granulocyte

  • calvaria

  • internal carotid artery

  • external carotid artery

  • secondary oocyte

  • zygote

  • endocardial cushion

  • semi-lunar valve

  • ankle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • GTPase activating protein binding
  • actin binding
Cellular component
  • cytoplasm
  • membrane
  • Golgi apparatus
  • cytosol
  • plasma membrane
  • intracellular membrane-bounded organelle
Biological process
  • multicellular organism development
  • actin cytoskeleton organization
  • angiogenesis
  • cellular component organization
  • cytoskeleton organization
  • regulation of cell shape
  • cell migration
  • cortical actin cytoskeleton organization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

91010

22379

Ensembl

ENSG00000161791

ENSMUSG00000023008

UniProt

Q8IVF7

Q6ZPF4

RefSeq (mRNA)

NM_175736
NM_198900
NM_001367835

NM_011711
NM_001310622
NM_001310623

RefSeq (protein)

NP_783863
NP_944489
NP_001354764

NP_001297551
NP_001297552
NP_035841

Location (UCSC)Chr 12: 49.64 – 49.71 MbChr 15: 99.22 – 99.27 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Formin-like protein 3 (FMNL3), also known as WW domain-binding protein 3 (WBP-3), is a protein that in humans is encoded by the FMNL3 gene.[5][6]

Function

The protein encoded by this gene contains a formin homology 2 domain and has high sequence identity to the mouse Wbp3 protein. Two alternative transcripts encoding different isoforms have been described.[5] The C-terminus has been shown to accelerate actin polymerization activity of this protein through its WH2-like motif.[7] FMNL3 has been crystallized in complex with actin providing insight into the mechanism of formin-mediated actin nucleation.[8]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000161791 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023008 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: formin-like 3".
  6. ^ Katoh M, Katoh M (May 2003). "Identification and characterization of human FMNL1, FMNL2 and FMNL3 genes in silico". International Journal of Oncology. 22 (5): 1161–8. doi:10.3892/ijo.22.5.1161. PMID 12684686.
  7. ^ Heimsath EG, Higgs HN (Jan 2012). "The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends". The Journal of Biological Chemistry. 287 (5): 3087–98. doi:10.1074/jbc.M111.312207. PMC 3270965. PMID 22094460.
  8. ^ Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ (Jan 2013). "FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation". Nature Structural & Molecular Biology. 20 (1): 111–8. doi:10.1038/nsmb.2462. PMC 3876896. PMID 23222643.

Further reading

  • Bedford MT, Chan DC, Leder P (May 1997). "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands". The EMBO Journal. 16 (9): 2376–83. doi:10.1093/emboj/16.9.2376. PMC 1169838. PMID 9171351.


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