Q54WH2

SS
Gene name
forA
Protein name
Formin-A
Names
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0279607
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. A Formin-3 DAD mutant expressed at endogenous levels produces more robust actin cables, which appear to have normal organization and dynamics.

Autoinhibitory domains (AIDs)

320-369 (DID domain) SS

Target domain

759-1199 (FH2 domain)

Relief mechanism

Partner binding

Assay

1174-1209 (DAD domain) SS

Target domain

759-1199 (FH2 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q54WH2

Entry ID Method Resolution Chain Position Source
AF-Q54WH2-F1 Predicted AlphaFoldDB

No variants for Q54WH2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54WH2

No associated diseases with Q54WH2

6 regional properties for Q54WH2

Type Name Position InterPro Accession
domain C2 domain 1 - 108 IPR000008
domain Formin, FH3 domain 352 - 553 IPR010472
domain Formin, GTPase-binding domain 139 - 347 IPR010473
domain Diaphanous autoregulatory (DAD) domain 1174 - 1209 IPR014767
domain Rho GTPase-binding/formin homology 3 (GBD/FH3) domain 139 - 539 IPR014768
domain Formin, FH2 domain 759 - 1199 IPR015425

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 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.
cleavage furrow The cleavage furrow is a plasma membrane invagination at the cell division site. The cleavage furrow begins as a shallow groove and eventually deepens to divide the cytoplasm.

4 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.
phosphatidylinositol binding Binding to an inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
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.

6 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.
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms.
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.
negative regulation of bleb assembly Any process that stops, prevents or reduces the frequency, rate or extent of bleb assembly.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MADKLYQIKL DIKKGKNIVG SDGSVCSPYL RVTWGGKKQQ KTKVITKSAE PEWNFSCLLE
70 80 90 100 110 120
IKKEKNPQKP GLEFELIEHK QFSEKEISST TYQLPESLIL GEACNYSVPM SIATSKGDQK
130 140 150 160 170 180
CEILIAITAI NFGKDKQDEE KKRHDEIQKK FAQLVEQLAT DSKAREGMMK LPYEARAQLV
190 200 210 220 230 240
EQHRDKLANE KHPDEYVVLL IKEITRKNIQ LAGGLQKSHS ASNASLGSLS PVTPRVDDGL
250 260 270 280 290 300
SVAELKNISV ALRSRGLDWI HQFHKLGATT RLVELLSLYV NKKSHTEESL QKQLECLNCI
310 320 330 340 350 360
KNLMNNNVGI GYIFGIKDSF KTIVLCLGSE YEKVNELAIG LLNTICFLPK INGHKLLIEL
370 380 390 400 410 420
LNYFKEEKKE SRRFISIVKS LKSKAGVIET KETLKTKSIY LSFINIIVNT PAEIDLRLAL
430 440 450 460 470 480
RQEFYWLGIK EILVKLSNYT YDESPELDTQ ITVFEEEESK DNKEMSERFQ EFKGLNLDNV
490 500 510 520 530 540
DDVLKTLMDR IRPKGLVDCM REISKDLLLL PIDDDVGIRN WVLASRIIKQ ISLRDKNIGI
550 560 570 580 590 600
DEDILPLENL LLMCEQEAKE VPLKSQIESL KKDAQDLAKK ITTQDIELKE KVEIIKKNEE
610 620 630 640 650 660
LTTKQLEEQI NIAKKKDEEI NQLKALVEQL KLTQGTAKPD SAAASTSVAP PPPPPPMTGG
670 680 690 700 710 720
GAPPPPPPPP PMTGGGGPPP PPPPPPMTGG GPPPPPPPPP MTGGGPPPPP PPPGGGPPPP
730 740 750 760 770 780
PPPPGAKAGG PPPPPPPFGK GPPPPPGGFG MKKAAAPPRK EVPVPALKMK GLQWVSLNDK
790 800 810 820 830 840
KIQGTIFSKF NLDTSKDINL DYKDIEGVFA AKVIEKKEST APKKTGPVSI IDPKTSQNLS
850 860 870 880 890 900
IFLSQFKGKS YDDICGAISK GDETVFQPNH IDALIGFLPS EDDINNINEF LREEKDITKL
910 920 930 940 950 960
GPPEQFSMKI HSVPQVKARL QAMKFKYAYE SKKSDLKVDI DNFKQGTQEI KGSEKIPKLL
970 980 990 1000 1010 1020
EVILILGNFI NGGTARGNAY GFKLNTITKL ADTKSTDNKL SLVNYLTRVV IKDFPHLNSF
1030 1040 1050 1060 1070 1080
AQDLGHVEAA GRVSLSQVQA EVATLRKEFV QVQKSIETLN SGTGEEAVDP FKVKYEEFCT
1090 1100 1110 1120 1130 1140
QTAEDIDLIT SSSQQIETDY KDLLAMFGED SKSEPSEFFG MFTKFMDQYD KATKENEQLS
1150 1160 1170 1180 1190 1200
IQAEKIAKRE AAKKLKEEED AKKKQLAEER KQKGETVEVK ESVVDDLLDT IASGDAFKNR
1210
RRRARKTDQD STIEPIDL