SASDB32: Human Filamin A Ig-like domains 16-17 truncation (1782-1956)

基本情報

• 登録情報: データベース: SASBDB / ID: SASDB32

試料

Human Filamin A Ig-like domains 16-17 truncation (1782-1956)

• Human Filamin A Ig-like domains 16-17 (protein), FilaminA, Homo sapiens

機能・相同性

分子機能:

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

ドメイン・相同性:

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

構成要素:

Filamin-A

• 生物種: Homo sapiens (ヒト)
• 引用: 日付: 2017 Dec; タイトル: Skeletal Dysplasia Mutations Effect on Human Filamins’ Structure and Mechanosensing; 著者: Seppälä J / Bernardi R / Haataja T / Hellman M / Pentikäinen O / Schulten K / Permi P / Ylänne J

登録者

• Jonne Seppälä (University of Jyväskylä, Jyväskylän, Finland)

モデル

• モデル #382: ; タイプ: dummy / ダミー原子の半径: 1.75 A / カイ2乗値: 1.096; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: Human Filamin A Ig-like domains 16-17 truncation (1782-1956); 試料濃度: 1.00-5.00
• バッファ: 名称: 20 mM Tris 50 mM NaCl 10 mM DTT / 濃度: 20.00 mM / 組成: 50mM NaCl, 10mM DTT

要素 #246

名称: FilaminA / タイプ: protein / 記述: Human Filamin A Ig-like domains 16-17 / 分子量: 18.7 / 分子数: 1 / 由来: Homo sapiens / 参照: UniProt: P21333
配列:

GLDVTSLRPF DLVIPFTIKK GEITGEVRMP SGKVAQPTIT DNKDGTVTVR YAPSEAGLHE MDIRYDNMHI PGSPLQFYVD YVNCGHVTAY GPGLTHGVVN KPATFTVNTK DAGEGGLSLA IEGPSKAEIS CTDNQDGTCS VSYLPVLPGD YSILVKYNEQ HVPGSPFTAR VTGDD

実験情報

• ビーム: 設備名称: ESRF BM29 / 地域: Grenoble / 国: France / 線源: X-ray synchrotron / 波長: 0.93 Å / スペクトロメータ・検出器間距離: 2.43 mm
• 検出器: 名称: Pilatus 1M

スキャン

タイトル: Human Filamin A Ig-like domains 16-17 / 測定日: 2013年9月30日 / 保管温度: 20 °C / セル温度: 20 °C / 照射時間: 1 sec. / フレーム数: 10 / 単位: 1/nm /

	Min	Max
Q	0.0366	4.4631

距離分布関数 P(R)

ソフトウェア P(R): GNOM 4.6 / ポイント数: 374 /

	Min	Max
Q	0.267	3.477
P(R) point	54	427
R	0	6.24

結果

カーブのタイプ: merged

	実験値	Standard	Porod	Estimated	Estimated method
分子量	20 kDa	20 kDa	18.1 kDa	-	-
体積	-	-	30.7 nm3	37.8	DAMMIN

	P(R)	Guinier
前方散乱 I0	30.32	30.33
慣性半径, Rg	1.83 nm	1.83 nm

	Min	Max
D	-	6.2
Guinier point	26	115