O94532

EV
Gene name
for3
Protein name
Formin-3
Names
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPCC895.05
EC number
Protein Class
PROTEIN BNI1 (PTHR47102)

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. 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)

353-406 (DID domain) EV

Target domain

759-1199 (FH2 domain)

Relief mechanism

Partner binding

Assay

Deletion assay, Mutagenesis experiment

1391-1419 (DAD domain) EV

Target domain

759-1199 (FH2 domain)

Relief mechanism

Partner binding

Assay

Deletion assay, Mutagenesis experiment

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O94532

Entry ID Method Resolution Chain Position Source
AF-O94532-F1 Predicted AlphaFoldDB

No variants for O94532

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O94532

No associated diseases with O94532

3 regional properties for O94532

Type Name Position InterPro Accession
domain Sec7 domain 736 - 931 IPR000904
domain Pleckstrin homology domain 962 - 1073 IPR001849
domain IQ motif and SEC7 domain-containing protein, PH domain 951 - 1088 IPR033742

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cell cortex
  • Cell tip
  • Found at the cell cortex and the growing tips of interphase cells
  • Localized to the septum region during cell division and upon cell division begins to localize to the new end, with some remaining at the older end
PANTHER Family PTHR47102 PROTEIN BNI1
PANTHER Subfamily PTHR47102:SF3 FORMIN-3
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

9 GO annotations of cellular component

Name Definition
cell cortex of cell tip The region directly beneath the plasma membrane at the cell tip. The cell tip is the region at either end of the longest axis of a cylindrical or elongated cell.
cell cortex of growing cell tip Any cell cortex that is part of a growing cell tip.
cell division site The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mating projection tip The apex of the mating projection in unicellular fungi exposed to mating pheromone; site of polarized growth.
medial cortex A medial cortical band overlaying the nucleus which acts as a landmark for contractile ring positioning and plays a role in cell cycle regulation.
medial cortex septin ring A ring-shaped structure that forms at the medial cortex of a symmetrically dividing cell at the onset of cytokinesis; composed of members of the conserved family of filament forming proteins called septins as well as septin-associated proteins.
mitotic actomyosin contractile ring A cytoskeletal structure composed of actin filaments, myosin, and myosin-associated proteins that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the mitotic spindle, i.e. the cell division plane. Ring contraction is associated with centripetal growth of the membrane that divides the cytoplasm of the two future daughter cells. In animal cells, the mitotic contractile ring is located inside the plasma membrane at the location of the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the mitotic contractile ring forms beneath the plasma membrane at the mother-bud neck before mitosis.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
small GTPase binding Binding to a small monomeric GTPase.

11 GO annotations of biological process

Name Definition
actin filament bundle assembly The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
actin filament bundle organization A process that results in the assembly, arrangement of constituent parts, or disassembly of an actin filament bundle.
actin filament 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. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
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.
barbed-end actin filament capping The binding of a protein or protein complex to the barbed (or plus) end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits.
establishment or maintenance of bipolar cell polarity Any cellular process that results in the specification, formation or maintenance of a bipolar intracellular organization or cell growth patterns.
establishment or maintenance of cell polarity regulating cell shape Any cellular process that results in the specification, formation or maintenance of a polarized intracellular organization or cell growth patterns that regulate the shape of a cell.
microtubule 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 microtubules and their associated proteins.
mitotic actomyosin contractile ring assembly Any actomyosin contractile ring assembly that is involved in mitotic cytokinesis.
mitotic actomyosin contractile ring maintenance Any actomyosin contractile ring maintenance that is involved in mitotic cell cycle.
protein localization to mitotic actomyosin contractile ring Any protein localization to actomyosin contractile ring that is involved in mitotic cytokinesis.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MASKMPEGSP PTSRSIQSRN SSYSTSSNER IGTPSTISLS ENSDLSKLQS TNDFESREDL
70 80 90 100 110 120
SLTSDDNNDP EYVMCYNTVY HQKTKINDKL LSETEQLRKI YPLESRVFPK PTIVKEITNE
130 140 150 160 170 180
RTKRYTFYDD DAPLTNQHTV LDEATYNRIL KRIDFFIEKV VEVPPTYHFL SLLNVQLRIQ
190 200 210 220 230 240
PIWWMDEFAE RNGIESLLSA LRNLGHYPER ASKTPLESQI IQSLFHCLNS ENCRRRYQSS
250 260 270 280 290 300
AKCSVPGFNA LGTIAETVLS KSLNSARMAT FLLKFLCNKK GLSYFKAVIR AFEWLVEQKL
310 320 330 340 350 360
SKTRFSAWMH SFNDVITGVR VCADSSPQAI VHMDEFEDTD CLIDYLVATL ALIRDLCAAP
370 380 390 400 410 420
PDLQLRCALR HELLSAGLQK AIDSLLKWRN RHVRDALQLL IKEHNADARR FRSGSDVNNV
430 440 450 460 470 480
DRKCVKKQMN YREESHTPHG NTTRKTSTPV SNNRPTTPEQ QAVWDVFQRI YTRFTGSEGS
490 500 510 520 530 540
KESFIKLLEY FVTEPDNGKI QKSMQLLTHT LEALEGFKTA KADTNVGLTI LSQRLLDKLG
550 560 570 580 590 600
TAEEIAEYKT KYNGAMLENK HLKEQVESML SQLNVGPRDP MQFLKKQLDE LKAELNLRDN
610 620 630 640 650 660
LLASMQREFE TRYRAQIQAY NKLQSQMEHV QNSNEQHLQP GLLNKVSKSF DSVHRRNLSQ
670 680 690 700 710 720
DSLDAMTEQF SYHVEPNILS GSGIPVRVHT PSKTEDLDES FSGSEISSSP SPLLPDVSDT
730 740 750 760 770 780
VEEQQKLLLK SPPPPPPAVI VPTPAPAPIP VPPPAPIMGG PPPPPPPPGV AGAGPPPPPP
790 800 810 820 830 840
PPPAVSAGGS RYYAPAPQAE PEPKIDETSL TEEQKIQLEE ARKQRKAADD AARAAIEKYT
850 860 870 880 890 900
SIPSLRDLHK PTRPLKRVHW QRVDPLPGPN VFTKFCLNFD ITAKVFIDNG LLDFLDEKFD
910 920 930 940 950 960
NTPREDFVAV EISDQRSSLL PDTVEQNMAI ILRSVSNMPV EDLVQKFLVE PDFLPASILY
970 980 990 1000 1010 1020
FDRASLASTN AYTDPFIPYS TDYTKKNPKE PTADVNSLSY FEKFFVLFVV NLRHYFQERM
1030 1040 1050 1060 1070 1080
KALKFRSTLF GDLEILEVRM KEVIDTSDSI MEDKNFAEFF QVLLIIGNYF NEPYDRASAF
1090 1100 1110 1120 1130 1140
SLYMIYRLET LRDSSSALTL MHYFDEIIRT RFPELLQAES TFKKIQSVSG YNIDAMVAGV
1150 1160 1170 1180 1190 1200
DGAYDEFCDF QTSLKDGALS KCDQHHPDDK AYDILSEWLP EAKERIRNIK KLKTDMLTKL
1210 1220 1230 1240 1250 1260
ENTVKYLCEY DSIDKVRNSF FKNLNSFYEM YSIAKAENEE RFEKEKRRIM SEDRDKLIRG
1270 1280 1290 1300 1310 1320
RQKTSIVAKY RNKRELPEDS DDKQDTASKD KNSLETIDEK MEDASKIEGD AKTGDDNEME
1330 1340 1350 1360 1370 1380
DLDKMEDLEK PDYAEEKDPY ITVMSELRSR IQNVPKRTVT VYSDEGVATL EPGAQGDDVV
1390 1400 1410 1420 1430 1440
DKAKMILEKM EGHSQLLTSS ANPDEEVLRA KLKAAERLQK PAIPRTRRKG HTEPKSAKSL
1450 1460
LAELTNGSNA SNLVENDRQK Q