Descriptions

Formins are conserved actin nucleators responsible for the assembly of diverse actin structures. The autoinhibition mechanism involves the intramolecular interaction between N-terminal DID domain and C-terminal DAD domain. Autoinhibition is relieved by GTP-bound Rho proteins, which bind to the DID and an adjacent GTPase binding (G) element, and consequently displace the DAD.

Autoinhibitory domains (AIDs)

Target domain

140-387 (DID domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for F1M775

Entry ID Method Resolution Chain Position Source

No variants for F1M775

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for F1M775

2 associated diseases with F1M775

Without disease ID

3 regional properties for F1M775

Type Name Position InterPro Accession
domain Protein kinase domain 102 - 367 IPR000719
active_site Serine/threonine-protein kinase, active site 225 - 237 IPR008271
binding_site Protein kinase, ATP binding site 108 - 131 IPR017441

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane
  • Cell projection, ruffle membrane
  • Cytoplasm, cytoskeleton
  • Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
  • Cytoplasm, cytoskeleton, spindle
  • Cytoplasm
  • Nucleus
  • Membrane ruffles, especially at the tip of ruffles, of motile cells
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
brush border The dense covering of microvilli on the apical surface of an epithelial cell in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
microtubule organizing center An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides.
mitotic spindle A spindle that forms as part of mitosis. Mitotic and meiotic spindles contain distinctive complements of proteins associated with microtubules.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
ruffle membrane The portion of the plasma membrane surrounding a ruffle.

5 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
identical protein binding Binding to an identical protein or proteins.
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.
transmembrane transporter binding Binding to a transmembrane transporter, a protein or protein complex that enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.

13 GO annotations of biological process

Name Definition
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 cytoskeletal structures comprising actin filaments and their associated proteins.
actin filament polymerization Assembly of actin filaments by the addition of actin monomers to a filament.
brain development The process whose specific outcome is the progression of the brain over time, from its formation to the mature structure. Brain development begins with patterning events in the neural tube and ends with the mature structure that is the center of thought and emotion. The brain is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.).
cellular response to histamine Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a histamine stimulus. Histamine, the biogenic amine 2-(1H-imidazol-4-yl)ethanamine, is involved in local immune responses as well as regulating physiological function in the gut and acting as a neurotransmitter.
cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures.
neuron projection development The process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
positive regulation of cell migration Any process that activates or increases the frequency, rate or extent of cell migration.
protein localization to microtubule A process in which a protein is transported to, or maintained at, a microtubule.
regulation of cell shape Any process that modulates the surface configuration of a cell.
regulation of cytoskeleton organization Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures.
regulation of microtubule-based process Any process that modulates the frequency, rate or extent of any cellular process that depends upon or alters the microtubule cytoskeleton.
regulation of release of sequestered calcium ion into cytosol Any process that modulates the frequency, rate or extent of the release into the cytosolic compartment of calcium ions sequestered in the endoplasmic reticulum or mitochondria.
sensory perception of sound The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P48608 dia Protein diaphanous Drosophila melanogaster (Fruit fly) EV
O60879 DIAPH2 Protein diaphanous homolog 2 Homo sapiens (Human) SS
Q9NSV4 DIAPH3 Protein diaphanous homolog 3 Homo sapiens (Human) SS
O60610 DIAPH1 Protein diaphanous homolog 1 Homo sapiens (Human) SS
Q9Z207 Diaph3 Protein diaphanous homolog 3 Mus musculus (Mouse) SS
O70566 Diaph2 Protein diaphanous homolog 2 Mus musculus (Mouse) SS
O08808 Diaph1 Protein diaphanous homolog 1 Mus musculus (Mouse) EV
F1LVW7 Diaph3 Protein diaphanous homolog 3 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFT LKRLMADELE RFTSMRIKKE
70 80 90 100 110 120
KEKPNSAHRN SSASYGDDPT AQSLQDISDD QVLVLFEQML VDMNLNEEKQ QPLREKDIVI
130 140 150 160 170 180
KREMVSQYLH TSKAGMNQKE SSRSAMMYIQ ELRSGLRDMH LLSCLESLRV SLNNNPVSWV
190 200 210 220 230 240
QTFGAEGLAS LLDILKRLHD EKEETSGNYD SRNQHEIIRC LKAFMNNKFG IKTMLETEEG
250 260 270 280 290 300
ILLLVRAMDP AVPNMMIDAA KLLSALCILP QPEDMNERVL EAMTERAEME EVERFQPLLD
310 320 330 340 350 360
GLKSGTSIAL KVGCLQLINA LITPAEELDF RVHIRSELMR LGLHQVLQEL REIDNDDMRV
370 380 390 400 410 420
QLNVFDEQGD EDFFDLKGRL DDIRMEMDDF GEVFQIILNT VKDSKAEPHF LSILQHLLLV
430 440 450 460 470 480
RNDYEARPQY YKLIEECVSQ IVLHKNGTDP DFKCRHLQID IEGLVDQMID KTKVEKSEAK
490 500 510 520 530 540
ATELEKKLDS ELTARHELQV EMKKMENDFE QKLQDLQGEK DALDSEKQQI TTQKQDLEAE
550 560 570 580 590 600
VSKLTGEVAK LSKELEDAKK EMASLSAVAV APSVSSSAAV PQAPPLPGTS GTVIPPPPPP
610 620 630 640 650 660
PLPGGAVPPP PPPPLPAGTG IPPPPPLPGG ACISSSPQLF GSTAIPPPPP LPGATAIPPP
670 680 690 700 710 720
PPLPGDTAIP PPPPLPGXTA IPPPPPLPGA TGVPPPPPPL PGSVGVPPPP PLPGGPGLPP
730 740 750 760 770 780
PPPPFPGAPG IPPPPPGMGV PPPPPFGFGI PAAPVLPFGL TPKKVYKPEV QLRRPNWSKF
790 800 810 820 830 840
VAEDLSQDCF WTKVKEDRFE NNELFAKLTL AFSAQTKTSL AKKDQEGGEE KKSVQKKKVK
850 860 870 880 890 900
ELKVLDSKTA QNLSIFLGSF RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML
910 920 930 940 950 960
SELKEEYDDL AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL
970 980 990 1000 1010 1020
RKSENFSSLL ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM TLLHFLAELC
1030 1040 1050 1060 1070 1080
ETDHPDVLKF PDELAHVEKA SRVSAENLQK NLDQMKKQIA DVERDVQNFP AATDEKDKFV
1090 1100 1110 1120 1130 1140
EKMTSFVKDA QEQYNKLRMM HSNMETLYKE LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ
1150 1160 1170 1180 1190 1200
AVKENQKRRE TEEKMRRAKL AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ
1210 1220 1230 1240 1250 1260
SGAAFRRKRG PRQVNRKAGC AVTSLLASEL TKDDAVAASS AKVPKKSEGV TTILEEAKEL
VGRAS