Q54N00

SS
Gene name
forH
Protein name
Formin-H
Names
Diaphanous-related formin dia2, dDia2
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0285589
EC number
Protein Class

Descriptions

Formins are conserved actin nucleators responsible for the assembly of diverse actin structures. In a study with Formin-3, the autoinhibition mechanism involves the intramolecular interaction between N-terminal DID domain and C-terminal DAD domain. This interaction is disrupted by Rho GTPase that is able to bind to the DID domain.

Autoinhibitory domains (AIDs)

267-307 (DID domain) SS

Target domain

623-1063 (FH2 domain)

Relief mechanism

Partner binding

Assay

1013-1051 (DAD domain) SS

Target domain

623-1063 (FH2 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q54N00

Entry ID Method Resolution Chain Position Source
AF-Q54N00-F1 Predicted AlphaFoldDB

No variants for Q54N00

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54N00

No associated diseases with Q54N00

3 regional properties for Q54N00

Type Name Position InterPro Accession
domain Formin, FH3 domain 222 - 455 IPR010472
domain Rho GTPase-binding/formin homology 3 (GBD/FH3) domain 34 - 394 IPR014768
domain Formin, FH2 domain 623 - 1063 IPR015425

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cell cortex
  • Cytoplasm, cytoskeleton
  • Enriched at the tips of filopodia
  • The N-terminus of the protein targets the protein to the cell cortex and the FH1/FH2 region refines the localization specifically to filopodial tips
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
cell cortex The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
cell trailing edge The area of a motile cell opposite to the direction of movement.
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
filopodium tip The end of a filopodium distal to the body of the cell.

3 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
profilin binding Binding to profilin, an actin-binding protein that forms a complex with G-actin and prevents it from polymerizing to form F-actin.
small GTPase binding Binding to a small monomeric GTPase.

11 GO annotations of biological process

Name Definition
'de novo' actin filament nucleation The actin nucleation process in which actin monomers combine in the absence of any existing actin filaments; elongation of the actin oligomer formed by nucleation leads to the formation of an unbranched filament.
actin filament polymerization Assembly of actin filaments by the addition of actin monomers to a filament.
actin nucleation The initial step in the formation of an actin filament, in which actin monomers combine to form a new filament. Nucleation is slow relative to the subsequent addition of more monomers to extend the filament.
barbed-end actin filament uncapping The removal of capping protein from the barbed (or plus) end of actin filaments to free the ends for addition, exchange or removal of further actin subunits.
cell morphogenesis The developmental process in which the size or shape of a cell is generated and organized.
cell motility Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another.
cell-substrate adhesion The attachment of a cell to the underlying substrate via adhesion molecules.
cortical actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
filopodium assembly The assembly of a filopodium, a thin, stiff protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal growth cone.
positive regulation of actin filament polymerization Any process that activates or increases the frequency, rate or extent of actin polymerization.
pseudopodium organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pseudopodium, a temporary protrusion or retractile process of a cell, associated with cellular movement.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSFDLESNSS GGSTIGRNSS IRLSSGLAPS ESTVSLNEII DLDREFELLL DKLAIEDPIK
70 80 90 100 110 120
RKQMQSLPDI SKRTLLEQNK ADIYRTVKHK GPIESFADVK SVISSINTKH VPIDIIKTLR
130 140 150 160 170 180
IHLNTADRDW IQSFLDNDGV QPILNILKRL ERNKNRKRKE HSILQWECTR CIAALMKIKI
190 200 210 220 230 240
GMEYIASFPQ TTNLMVLCLD TPLIKAKTLV LELLAAIAVT DRGHGAVLTS MIYHKEVKKE
250 260 270 280 290 300
ITRYFNLVQS LKIEKNAEYL TTCMSFINCI ISSPSDLPSR IEIRKAFLNL KILKYIENLR
310 320 330 340 350 360
ADYNEDKNLL TQLDVFEEEL STDEQLNSQQ GTQIGIEDLF SQISSRVTGT PSQQELITLM
370 380 390 400 410 420
THFQRMSSSN LGLGVWTLYN ALANQLEDEL KIHPDLDVTL VSLLFPEVKK SSSGLFGFGS
430 440 450 460 470 480
KSKSPSSSPA LSSMAKTELK KDNEEKQKTI EHLLKQLNKF SGGQNTERWM IEREEKNKLI
490 500 510 520 530 540
AQLMAQTKNG GGGGGGGVGG DSSLSNDEAL KRENQLLRME IENIKNNPSV LLNSGNSING
550 560 570 580 590 600
DVPNLFISSP GSTLSPSPSG EPPIPSTDFG ITSSSIHTST DKLTNSTEPI LGSPPPPPPP
610 620 630 640 650 660
PMSGGGGPPP PPPPPGGKSN KPAKPIIKPS VKMRNFNWIT IPALKVQGTF WDKLDETSFI
670 680 690 700 710 720
QSLDKVELES LFSAKAPTVK VESKQLTRKV VVTVIDMKKA NNCAIMLQHF KIPNEQLKKM
730 740 750 760 770 780
QIMLDEKHFS QENAIYLLQF APTKEDIEAI KEYQGDQMQL GAAEQYMLTV MDIPKLDSRL
790 800 810 820 830 840
KAFIFKQKFE GLVEDLVPDI KAIKAASLEL KKSKRLSDIL KFILAIGNYV NGSTTRGGAF
850 860 870 880 890 900
GFKVLETLPK MRDARSNDNK LSLLHFLAKT LQDRIPEIWN IGAELPHIEH ASEVSLNNII
910 920 930 940 950 960
SDSSEIKRSI DLIERDFVPM INDPLFAHDK HWIHKITEFQ KIAKVQYQRI EKEIDEMNKA
970 980 990 1000 1010 1020
FEEITSYFGE PKSTQPDVFF STINNFLEDL EKAYGEYQAM IRKAELENSK MEDPEKGGLQ
1030 1040 1050 1060 1070 1080
DLSSQIRSGQ LFKDRRVGDS VIAQMQNVDS LRKNLKSTST TTPNTPPTIK IELPSQSILK
PSGQLKK