Descriptions

The diaphanous-related formin, Frl, the single fly member of the FMNL (formin related in leukocytes/formin-like) formin subfamily affects ommatidial rotation in the Drosophila eye and is controlled by the Rho family GTPase Cdc42. Full-length Frl is autoinhibited by the interaction between DAD domain and N-terminal region (probably DID domain as identified in other Flamins). Binding of Cdc42 to the GBD domain alleviates autoinhibition.

Autoinhibitory domains (AIDs)

Target domain

687-1132 (FH2 domain)

Relief mechanism

Partner binding

Assay

Deletion assay, Mutagenesis experiment

Target domain

687-1132 (FH2 domain)

Relief mechanism

Partner binding

Assay

Deletion assay, Mutagenesis experiment

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9VUC6

Entry ID Method Resolution Chain Position Source
AF-Q9VUC6-F1 Predicted AlphaFoldDB

No variants for Q9VUC6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VUC6

No associated diseases with Q9VUC6

5 regional properties for Q9VUC6

Type Name Position InterPro Accession
domain Formin, FH3 domain 374 - 573 IPR010472
domain Formin, GTPase-binding domain 76 - 371 IPR010473
domain Diaphanous autoregulatory (DAD) domain 1136 - 1169 IPR014767
domain Rho GTPase-binding/formin homology 3 (GBD/FH3) domain 76 - 559 IPR014768
domain Formin, FH2 domain 687 - 1132 IPR015425

Functions

Description
EC Number
Subcellular Localization
PANTHER Family PTHR45857 FORMIN-LIKE PROTEIN
PANTHER Subfamily PTHR45857:SF4 FORMIN-LIKE PROTEIN
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein 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.
GTPase binding Binding to a GTPase, any enzyme that catalyzes the hydrolysis of GTP.
small GTPase binding Binding to a small monomeric GTPase.

6 GO annotations of biological process

Name Definition
axon extension Long distance growth of a single axon process involved in cellular development.
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.
mushroom body development The process whose specific outcome is the progression of the mushroom body over time, from its formation to the mature structure. The mushroom body is composed of the prominent neuropil structures of the insect central brain, thought to be crucial for olfactory associated learning. These consist mainly of a bulbous calyx and tightly packaged arrays of thin parallel fibers of the Kenyon cells.
ommatidial rotation The process in which photoreceptors are arranged in ommatidia in the dorsal and ventral fields to be mirror images. The polarity is established in the imaginal discs concurrently with cell fate specification.
regulation of cell shape Any process that modulates the surface configuration of a cell.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8IVF7 FMNL3 Formin-like protein 3 Homo sapiens (Human) SS
O95466 FMNL1 Formin-like protein 1 Homo sapiens (Human) SS
Q96PY5 FMNL2 Formin-like protein 2 Homo sapiens (Human) SS
Q6ZPF4 Fmnl3 Formin-like protein 3 Mus musculus (Mouse) SS
Q9JL26 Fmnl1 Formin-like protein 1 Mus musculus (Mouse) SS
A2APV2 Fmnl2 Formin-like protein 2 Mus musculus (Mouse) SS
10 20 30 40 50 60
MGAVKSRTIT SADVDADEQL QHPHSHAHHH SMRNGHQHNG SISSGTLQKQ DLRYDIGCSS
70 80 90 100 110 120
QYQHVRQPSL RSRSQQPMPT TDELDRRFAK VLASMDLPPD KAKLLRNYDD EKKWDMICDQ
130 140 150 160 170 180
EMVQAKDPPS HYLSKLRTYL DPKASRSHRL YLFYFLCQKR KMVGESTSTQ VLRDLEISLR
190 200 210 220 230 240
TNHIEWVKEF LDDTNQGLDA LVDYLSFRLQ MMRHEQRLQG VLCASEERLN LTNGGDGGEI
250 260 270 280 290 300
VMGNSSSVSP GGGGGLLSHG NSTGHGLANG TLDSRQQHTM SYGFLRPTIA DALDSPSLKR
310 320 330 340 350 360
RSRHIAKLNM GAATDDIHVS IMCLRAIMNN KYGFNMVIQH REAINCIALS LIHKSLRTKA
370 380 390 400 410 420
LVLELLAAIC LVKGGHEIIL GSFDNFKDVC QEKRRFQTLM EYFMNFEAFN IDFMVACMQF
430 440 450 460 470 480
MNIVVHSVED MNYRVHLQYE FTALGLDKYL ERIRLTESEE LKVQISAYLD NVFDVAALME
490 500 510 520 530 540
DSETKTSALE RVQELEDQLE REIDRNSEFL YKYAELESES LTLKTEREQL AMIRQKLEEE
550 560 570 580 590 600
LTVMQRMLQH NEQELKKRDT LLHTKNMELQ TLSRSLPRSA SSGDGSLANG GLMAGSTSGA
610 620 630 640 650 660
ASLTLPPPPP PMPASPTASS AAPPPPPPPA PPAPPPPPGF SPLGSPSGSL ASTAPSPPHA
670 680 690 700 710 720
PPMLSSFQPP PPPVAGFMPA PDGAMTIKRK VPTKYKLPTL NWIALKPNQV RGTIFNELDD
730 740 750 760 770 780
EKIFKQIDFN EFEERFKIGI GGALRNGSNG TEVDGSLQSS KRFKRPDNVS LLEHTRLRNI
790 800 810 820 830 840
AISRRKLGMP IDDVIAAIHS LDLKKLSLEN VELLQKMVPT DAEVKSYKEY IIERKDQQLL
850 860 870 880 890 900
TEEDKFMLQL SRVERISSKL AIMNYMGNFV DSVHLISPQV QSIAGASTSL KQSRKFKAVL
910 920 930 940 950 960
EIVLAFGNYL NSNKRGPAYG FKLQSLDTLI DTKSTDKRSS LLHYIVATIR AKFPELLNFE
970 980 990 1000 1010 1020
SELYGTDKAA SVALENVVAD VQELEKGMDL VRKEAELRVK GAQTHILRDF LNNSEDKLKK
1030 1040 1050 1060 1070 1080
IKSDLRHAQE AFKECVEYFG DSSRNADAAA FFALIVRFTR AFKQHDQENE QRLRLEKAAA
1090 1100 1110 1120 1130 1140
LAASKKENDQ VLMRNKVNQK KQQLPSNGAL SLQEAVINEL KSKAHSVREK KLLQQDEVYN
1150 1160 1170 1180
GALEDILLGL KSEPYRRADA VRRSQRRRID NNRLSRTLEE MDC