SASDFD3: Filamin A Ig-like domains 4-6 (FLNa4-6) (Filamin A Ig-like domain...

Basic information

• Entry: Database: SASBDB / ID: SASDFD3

Sample

Filamin A Ig-like domains 4-6 (FLNa4-6)

• Filamin A Ig-like domains 4-6 (protein), FLNa4-6, Homo sapiens

Function / homology

Function:

regulation of membrane repolarization during atrial cardiac muscle cell action potential / regulation of membrane repolarization during cardiac muscle cell action potential / establishment of Sertoli cell barrier / Myb complex / formation of radial glial scaffolds / glycoprotein Ib-IX-V complex / adenylate cyclase-inhibiting dopamine receptor signaling pathway / positive regulation of integrin-mediated signaling pathway / cytoplasmic sequestering of protein / tubulin deacetylation / actin crosslink formation / blood coagulation, intrinsic pathway / protein localization to bicellular tight junction / OAS antiviral response / positive regulation of actin filament bundle assembly / positive regulation of neuron migration / positive regulation of potassium ion transmembrane transport / Cell-extracellular matrix interactions / early endosome to late endosome transport / apical dendrite / positive regulation of neural precursor cell proliferation / cell-cell junction organization / positive regulation of platelet activation / protein localization to cell surface / Fc-gamma receptor I complex binding / negative regulation of transcription by RNA polymerase I / wound healing, spreading of cells / megakaryocyte development / GP1b-IX-V activation signalling / cortical cytoskeleton / positive regulation of axon regeneration / receptor clustering / SMAD binding / RHO GTPases activate PAKs / actin filament bundle / brush border / semaphorin-plexin signaling pathway / cilium assembly / mitotic spindle assembly / potassium channel regulator activity / epithelial to mesenchymal transition / blood vessel remodeling / axonal growth cone / heart morphogenesis / positive regulation of substrate adhesion-dependent cell spreading / regulation of cell migration / release of sequestered calcium ion into cytosol / dendritic shaft / protein kinase C binding / protein localization to plasma membrane / G protein-coupled receptor binding / actin filament / synapse organization / mRNA transcription by RNA polymerase II / trans-Golgi network / establishment of protein localization / negative regulation of DNA-binding transcription factor activity / negative regulation of protein catabolic process / cerebral cortex development / Z disc / small GTPase binding / platelet aggregation / kinase binding / positive regulation of protein import into nucleus / actin filament binding / cell-cell junction / actin cytoskeleton / Platelet degranulation / negative regulation of neuron projection development / GTPase binding / perikaryon / actin cytoskeleton organization / postsynapse / angiogenesis / positive regulation of canonical NF-kappaB signal transduction / DNA-binding transcription factor binding / transmembrane transporter binding / protein stabilization / cadherin binding / focal adhesion / glutamatergic synapse / nucleolus / negative regulation of apoptotic process / perinuclear region of cytoplasm / protein homodimerization activity / RNA binding / extracellular exosome / extracellular region / membrane / nucleus / plasma membrane / cytosol / cytoplasm

Domain/homology:

Filamin family / Filamin/ABP280 repeat / Filamin-type immunoglobulin domains / Filamin/ABP280 repeat / Filamin/ABP280 repeat profile. / Filamin/ABP280 repeat-like / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Immunoglobulin E-set / Immunoglobulin-like fold

Component:

Filamin-A

• Biological species: Homo sapiens (human)
• Citation: Date: 2019 Aug; Title: Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia; Authors: Haataja T / Capoulade R / Lecointe S / Hellman M / Merot J / Permi P

Contact author

• Tatu Haataja (University of Jyväskylä, Jyväskylän, Finland)

Models

• Model #2833: ; Type: dummy / Software: (DAMFILT 5) / Radius of dummy atoms: 2.00 A / Symmetry: P1 / Chi-square value: 0.855 / P-value: 0.426529; Search similar-shape structures of this assembly by Omokage search (details)
• Model #2834: ; Type: atomic / Symmetry: P1; Comment: Range 574-766 of 4m9p and homology model of FLNa6 used for generating the SASREF model; Chi-square value: 0.92 / P-value: 0.000009; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Filamin A Ig-like domains 4-6 (FLNa4-6) / Specimen concentration: 2.00-4.00
• Buffer: Name: 20 mM Tris, 100 mM NaCl, 1 mM DTT / pH: 8

Entity #1499

Name: FLNa4-6 / Type: protein / Description: Filamin A Ig-like domains 4-6 / Formula weight: 31.52 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P21333
Sequence:

MSCGNQKVRA WGPGLEGGVV GKSADFVVEA IGDDVGTLGF SVEGPSQAKI ECDDKGDGSC DVRYWPQEAG EYAVHVLCNS EDIRLSPFMA DIRDAPQDFH PDRVKARGPG LEKTGVAVNK PAEFTVDAKH GGKAPLRVQV QDNEGCPVEA LVKDNGNGTY SCSYVPRKPV KHTAMVSWGG VSIPNSPFRV NVGAGSHPNK VKVYGPGVAK TGLKAHEPTY FTVDCAEAGQ GDVSIGIKCA PGVVGPAEAD IDFDIIRNDN DTFTVKYTPR GAGSYTIMVL FADQATPTSP IRVKVEPS

Experimental information

• Beam: Instrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 2.9 mm
• Detector: Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm

Scan

Title: Filamin A Ig-like domains 4-6 (FLNa4-6) / Measurement date: Feb 10, 2017 / Cell temperature: 20 °C / Unit: 1/nm /

	Min	Max
Q	0.0741	3.1293

Distance distribution function P(R)

Sofotware P(R): GNOM 4.6 / Number of points: 287 /

	Min	Max
Q	0.1565	2.849
P(R) point	18	304
R	0	9.5

Result

Type of curve: merged
Comments: Wild type three-domain fragment of human Filamin A Ig-like domains 4-6 (FLNa4-6). There are two extra amino acids, Met and Ser, in the very N-terminus of the polypeptide that have resulted from TEV-cleavage of the GST fusion tag during the protein purification.

	Experimental	Porod
MW	23.4 kDa	25 kDa
Volume	-	41 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	23.91	0.03	23.72	0.03
Radius of gyration, Rg	2.82 nm	0.005	2.73 nm	0.03

	Min	Max
D	-	9.5
Guinier point	18	80