| General information | | DisProt: | DP00448 | | Name: | FH1/FH2 domain-containing protein 1 | | Synonym(s): | FHOD1_HUMAN
Formin homolog overexpressed in spleen 1
FHOS
Formin homology 2 domain-containing protein 1
FHOD1
| | First appeared in release: | Release 3.1 (03/31/2006) | | UniProt: | Q9Y613 | | UniGene: | Hs.95231 | | SwissProt: | FHOD1_HUMAN | | TrEMBL: | | | NCBI (GI): | 62512187 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 1164 | | Percent disordered: | 5% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MAGGEDRGDG EPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP LGAQIPAVHR - 60
LLGAPLKLED CALQVSPSGY YLDTELSLEE QREMLEGFYE EISKGRKPTL ILRTQLSVRV - 120
NAILEKLYSS SGPELRRSLF SLKQIFQEDK DLVPEFVHSE GLSCLIRVGA AADHNYQSYI - 180
LRALGQLMLF VDGMLGVVAH SDTIQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF - 240
IRAVNSVAST TGAPPWANLV SILEEKNGAD PELLVYTVTL INKTLAALPD QDSFYDVTDA - 300
LEQQGMEALV QRHLGTAGTD VDLRTQLVLY ENALKLEDGD IEEAPGAGGR RERRKPSSEE - 360
GKRSRRSLEG GGCPARAPEP GPTGPASPVG PTSSTGPALL TGPASSPVGP PSGLQASVNL - 420
FPTISVAPSA DTSSERSIYK ARFLENVAAA ETEKQVALAQ GRAETLAGAM PNEAGGHPDA - 480
RQLWDSPETA PAARTPQSPA PCVLLRAQRS LAPEPKEPLI PASPKAEPIW ELPTRAPRLS - 540
IGDLDFSDLG EDEDQDMLNV ESVEAGKDIP APSPPLPLLS GVPPPPPLPP PPPIKGPFPP - 600
PPPLPLAAPL PHSVPDSSAL PTKRKTVKLF WRELKLAGGH GVSASRFGPC ATLWASLDPV - 660
SVDTARLEHL FESRAKEVLP SKKAGEGRRT MTTVLDPKRS NAINIGLTTL PPVHVIKAAL - 720
LNFDEFAVSK DGIEKLLTMM PTEEERQKIE EAQLANPDIP LGPAENFLMT LASIGGLAAR - 780
LQLWAFKLDY DSMEREIAEP LFDLKVGMEQ LVQNATFRCI LATLLAVGNF LNGSQSSGFE - 840
LSYLEKVSEV KDTVRRQSLL HHLCSLVLQT RPESSDLYSE IPALTRCAKV DFEQLTENLG - 900
QLERRSRAAE ESLRSLAKHE LAPALRARLT HFLDQCARRV AMLRIVHRRV CNRFHAFLLY - 960
LGYTPQAARE VRIMQFCHTL REFALEYRTC RERVLQQQQK QATYRERNKT RGRMITETEK - 1020
FSGVAGEAPS NPSVPVAVSS GPGRGDADSH ASMKSLLTSR PEDTTHNRRS RGMVQSSSPI - 1080
MPTVGPSTAS PEEPPGSSLP SDTSDEIMDL LVQSVTKSSP RALAARERKR SRGNRKSLRR - 1140
TLKSGLGDDL VQALGLSKGP GLEV
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| Functional narrative |
Formins are large proteins of typically more than 1000 amino acids that are defined by the presence of two conserved regions, namely the formin
homology 1 and 2 (FH1 and FH2) domains. Additional conserved domains such as a N-terminal GTPase-binding domain (GBD) and a C-terminal Diaphanous-autoregulation domain (DAD) were found to constitute a formin
subfamily, the diaphanous-related formins (DRFs). DRFs are cytoskeleton
remodelling proteins that mediate specific upstream GTPase signals to regulate cellular processes such as cytokinesis, actin cable and stress fiber
formation, cell polarity, neurite outgrowth, and organelle motility. The biological activity of DRFs is regulated by an autoinhibitory interaction
of the C-terminal DAD with the DRF N-terminus. This autoinhibition is released upon competitive binding of an activated GTPase to the DRF’s
N-terminus. FHOD1 is required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Self-associates via the FH2 domain. Binds to F-actin via its N-terminus. Binds to the cytoplasmic domain of CD21 via its C-terminus. Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Diaphanous autoregulatory domain (DAD) | | Location: | 1104 - 1164 | | Length: | 61 | | Region sequence: |
SDEIMDLLVQSVTKSSPRALAARERKRSRGNRKSLRRTLKSGLGDDLVQALGLSKGPGLE
V | | Modification type: | Fragment
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Autoregulatory
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; 0.6 mM pdotein; 20 mM KPi, 100 mM NaCl, 1 mM TCEP; uniformly 15N-labelled DAD)
- Size exclusion/gel filtration chromatography (298 K; pH: 7.2; 1 mg/ml protein, 90microl; 50 mM Hepes, 100 mM NaCl, 1 mM DTE; Superdex 75 column)
| References:
- Schonichen A, Alexander M, Gasteier JE, Cuesta FE, Fackler OT, Geyer M. "Biochemical characterization of the diaphanous auto-regulatory interaction in the Formin-homology protein FHOD1." J Biol Chem. 2006; 281(8): 5084-5093. PubMed: 16361249
| Comments:NMR structural analysis and size exclusion
chromatography experiments revealed that
the FHOD1 DAD is intrinsically unstructured
with a tendency for a helical conformation in
the hydrophobic autoregulation motif.
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| References |
- Westendorf JJ, Koka S. "Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated actin dynamics." J Cell Biochem. 2004; 92(1): 29-41. PubMed: 15095401
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