Descriptions

(Annotation from UniProt)
The DAD domain may regulate activation via by an autoinhibitory interaction with the N-terminus. This autoinhibition may be released upon competitive binding of an activated GTPase. The release of DAD may allow the FH2 domain to nucleate and elongate nonbranched actin filaments.

Autoinhibitory domains (AIDs)

Target domain

27-464 (GBD/FH3 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9JL26

Entry ID Method Resolution Chain Position Source
AF-Q9JL26-F1 Predicted AlphaFoldDB

5 variants for Q9JL26

Variant ID(s) Position Change Description Diseaes Association Provenance
rs1134264397 324 A>T No Ensembl
rs214310171 392 T>M No Ensembl
rs13462437 825 S>F No Ensembl
rs226165420 1093 A>S No Ensembl
rs13462438 1095 L>Y No Ensembl

No associated diseases with Q9JL26

5 regional properties for Q9JL26

Type Name Position InterPro Accession
domain Formin, FH3 domain 283 - 632 IPR010472
domain Formin, GTPase-binding domain 27 - 280 IPR010473
domain Diaphanous autoregulatory (DAD) domain 1049 - 1082 IPR014767
domain Rho GTPase-binding/formin homology 3 (GBD/FH3) domain 27 - 464 IPR014768
domain Formin, FH2 domain 627 - 1057 IPR015425

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell membrane; Lipid-anchor
  • Cytoplasmic vesicle, phagosome
  • Recruited to actin-rich phagosomes during phagocytosis
  • Translocates to the plasma membrane upon activation by RAC1
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.
phagocytic vesicle A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

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.
GTPase activating protein binding Binding to a GTPase activating protein.
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.

5 GO annotations of biological process

Name Definition
actin filament severing The process in which an actin filament is broken down into smaller filaments.
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.
regulation of cell shape Any process that modulates the surface configuration of a cell.
substrate-dependent cell migration The orderly movement of a cell from one site to another along a substrate such as the extracellular matrix; the migrating cell forms a protrusion that attaches to the substrate.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9VUC6 Frl Formin-like protein Drosophila melanogaster (Fruit fly) EV
Q8IVF7 FMNL3 Formin-like protein 3 Homo sapiens (Human) SS
Q96PY5 FMNL2 Formin-like protein 2 Homo sapiens (Human) SS
O95466 FMNL1 Formin-like protein 1 Homo sapiens (Human) SS
Q6ZPF4 Fmnl3 Formin-like protein 3 Mus musculus (Mouse) SS
A2APV2 Fmnl2 Formin-like protein 2 Mus musculus (Mouse) SS
10 20 30 40 50 60
MGNAAGSAEQ PAGPTASPPK QPAVPKQPMP AAGELEERFT RVLNCMNLPP DKVQLLSQYD
70 80 90 100 110 120
NEKKWELICD QERFQVKNPP AAYIQKLKSY LDTGGVSRKV ASDWMSNLGF KRRVQESTQV
130 140 150 160 170 180
LRELETSLRT NHIGWVQEFL NEENRGLDVL LEYLAFAQCS VAYDMESTDS VASGAEKSKP
190 200 210 220 230 240
LDQSVEDLSK APPSSVPKSR LTIKLTPAHS RKALRNSRIV SQKDDVHVCI MCLRAIMNYQ
250 260 270 280 290 300
SGFSLVMNHP ACVNEIALSL NNKSPRTKAL VLELLAAVCL VRGGHDIILA AFDNFKEVCG
310 320 330 340 350 360
EQHRFEKLME YFRHEDSNID FMVACMQFIN IVVHSVENMN FRVFLQYEFT HLGLDLYLER
370 380 390 400 410 420
LRLTESDKLQ VQIQAYLDNV FDVGTLLEET ETKNAVLEHM EELQEQVATL TERLRDTEND
430 440 450 460 470 480
SMAKIAELEK QLSQARKELE TLRERFSEST PMGTSRRIPE PEKVPVPTVV RPSALELKVE
490 500 510 520 530 540
ELEEKGLIRI LRGPGDVVSI EILPGAAATP SGDDAQAPRV STDSPSTAES IPEAASPPPP
550 560 570 580 590 600
PPPPPPPLPN LQSQQEAPPS APPLAPPLPG CAEPPPAPPL PGDLPPPPPP PPLGTDGPVP
610 620 630 640 650 660
PPPPPPPGGP PDILGGQGPD IGPGVKAKKP IQTKFRMPLL NWVALKPSQI TGTVFTELND
670 680 690 700 710 720
EKVLQELDMN DFEEHFKTKS QGPCLDISAL KGKASQKAPT KTILIEANRA KNLAITLRKG
730 740 750 760 770 780
NLGADRICQA IETYDLQTLS LDFLELLTRF LPTDYERSLI ARFEKEQRPM EELSEEDRFM
790 800 810 820 830 840
LRFSRIQRLP ERMNTLTFLG NFPDTAQLLM PQLNAIIAAS MSIKSSDKLR QILEIVLAFG
850 860 870 880 890 900
NYMNSSKRGA AYGFRLQSLD ALLEMKSTDR KQTLLHYLVK VIAEKYPQLT GFHSDLHFLD
910 920 930 940 950 960
KAGSVSLDSV LGDVRSLQRG LELTQREFVR QDDCLVLKEF LRANSPTMDK LLADSKTAQE
970 980 990 1000 1010 1020
AYESVVEYFG ENPKTTSPSM FFSLFSRFTK AYKKAEQEVE QWKKEAAADT SGREEPPTPK
1030 1040 1050 1060 1070 1080
SPPKARRQQM DLISELKRKQ QKEPLIYESD RDGAIEDIIT DLRNQPYIRA DTGRRSARRR
1090
PPGPPLPVTT DLAL