Q54SP2

SS
Gene name
forB
Protein name
Formin-B
Names
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0282297
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)

276-317 (DID domain) SS

Target domain

612-1095 (FH2 domain)

Relief mechanism

Partner binding

Assay

1071-1100 (DAD domain) SS

Target domain

612-1095 (FH2 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q54SP2

Entry ID Method Resolution Chain Position Source
AF-Q54SP2-F1 Predicted AlphaFoldDB

No variants for Q54SP2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54SP2

No associated diseases with Q54SP2

4 regional properties for Q54SP2

Type Name Position InterPro Accession
domain Formin, FH3 domain 227 - 662 IPR010472
domain Formin, GTPase-binding domain 38 - 223 IPR010473
domain Diaphanous autoregulatory (DAD) domain 1071 - 1100 IPR014767
domain Formin, FH2 domain 612 - 1095 IPR015425

Functions

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

1 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.

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.

2 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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFFKGKKKDK EKEKSHGNIG NVISVENKTG SQSNLHVEQN LSNEDLKIQF SQLLYELGVP
70 80 90 100 110 120
EAKRVEMELW SNDKKWMLLV QNKDKIKENE EKMKQKGSLY ETPQFYLSLL RENASIQKTI
130 140 150 160 170 180
SDLKVSLASN KLSWIDSFIG LSGFDEILKI FQTFQLKPEK NSIDFLILFD CVNIIKSILN
190 200 210 220 230 240
SQSGVKSVMT TSHTFKVLVL CLDQSYPPEL RNAVLQLTAA LTLLPTVGHS YVLEAIENFK
250 260 270 280 290 300
VSNREKVRFQ TIIEGAKSVS NTQLHYEYLT SFMNLVNSIV NSPADLQVRI GLRSEFTALK
310 320 330 340 350 360
LIELISNSKG VSEDLDTQIN LFFECMEEDN DEVGAHYKEV NIRSPSEVST KIDTLLQSHP
370 380 390 400 410 420
ALHHHFISII KGLYTLASTQ SDLGGSMWNI LDESVGLILK DPSKESQLEK LQNENNNLKL
430 440 450 460 470 480
QLSEIKLNNS NNNNNNNNSN NNNNDSNVST PNINTGSPLL PPQQYQDLEQ KLQLTQNEKN
490 500 510 520 530 540
ESQNKVKQLE SEIKGLNSTL TGLQLKVTKL EADLLSVSVT TPPSDTNGTT SPPIEAPSSP
550 560 570 580 590 600
SLGAPPPPPP PPPAPPVSGG GPPPPPPPPP PSSGGGPPPP PPPPSSGGPP PPPPPPGGMK
610 620 630 640 650 660
KPGAPAVPNL PPKKSSVPSV KMVGLQWKKV NNNVIENSIW MNVKDYNLND QFKQLEELFQ
670 680 690 700 710 720
VKKPTATTPT APVGGASNVA VGGGSGSKSI VSTPTISILD PKRSQAIMIM LSRFKISFPD
730 740 750 760 770 780
LSKAITNLDE SKLNLEDAKS LLKFVPSSEE IELLKEEDPS CFGKPEQFLW ELSKINRISE
790 800 810 820 830 840
KLECFIFKQK LSTQIEELTP DINALLKGSM ETKNNKSFHQ ILEIVLSLGN FINGGTPRGD
850 860 870 880 890 900
IYGFKLDSLS GLLDCRSPSD SKVTLMTWLI QFLENKHPSL LEFHQEFTAI DEAKRVSIQN
910 920 930 940 950 960
LRSEVASLKK GLTLLTNEVE KSEGASKTIL SGFVGKSTDA VTLIEKQFNT ALESFNSTVQ
970 980 990 1000 1010 1020
FYGEDVKTSS PEEFFQHVSK FKNEFKRTIE SIQKERENVQ KLAARKKAAA SGPSVPSASG
1030 1040 1050 1060 1070 1080
SSINIAPKSG VSPITPTSKS SISISQKPPQ STQPSISVQQ QQQQHHGDDD DDIPQNGTFM
1090 1100 1110 1120
DQLMSKMKGG EAIRASRRAS QYVFTQNGAG GVGAIDALNA ALKNKK