Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9FKI0

Entry ID Method Resolution Chain Position Source
AF-Q9FKI0-F1 Predicted AlphaFoldDB

35 variants for Q9FKI0

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_5_13876350_G_A 28 S>F No 1000Genomes
ENSVATH14518130 39 R>L No 1000Genomes
tmp_5_13876226_A_G 40 F>S No 1000Genomes
ENSVATH00674514 44 D>H No 1000Genomes
ENSVATH07214648 69 D>G No 1000Genomes
ENSVATH14518128 151 A>T No 1000Genomes
ENSVATH07214644 154 A>S No 1000Genomes
ENSVATH03243818 261 A>V No 1000Genomes
tmp_5_13874737_G_A 304 A>V No 1000Genomes
ENSVATH07214630 367 Q>H No 1000Genomes
tmp_5_13874305_A_G 374 V>A No 1000Genomes
tmp_5_13874269_G_A 386 T>I No 1000Genomes
tmp_5_13874266_T_C 387 D>G No 1000Genomes
ENSVATH11957926 400 L>F No 1000Genomes
tmp_5_13874179_T_C 416 E>G No 1000Genomes
ENSVATH07214621 423 V>I No 1000Genomes
ENSVATH11957863 509 S>L No 1000Genomes
tmp_5_13873468_G_T 541 D>E No 1000Genomes
tmp_5_13873425_C_A 556 A>S No 1000Genomes
ENSVATH03243812 569 N>S No 1000Genomes
tmp_5_13873258_C_G 574 E>D No 1000Genomes
tmp_5_13873070_C_T 609 M>I No 1000Genomes
tmp_5_13873060_C_T 613 A>T No 1000Genomes
tmp_5_13872994_C_T 635 A>T No 1000Genomes
tmp_5_13872976_C_T 641 A>T No 1000Genomes
ENSVATH03243799 645 A>S No 1000Genomes
ENSVATH00674498 650 N>S No 1000Genomes
tmp_5_13872930_G_C 656 A>G No 1000Genomes
tmp_5_13872912_G_A 662 T>I No 1000Genomes
ENSVATH03243798 664 Q>E No 1000Genomes
tmp_5_13872901_G_C 666 Q>E No 1000Genomes
ENSVATH07214606 680 D>E No 1000Genomes
ENSVATH07214605 683 N>S No 1000Genomes
ENSVATH07214604 684 N>I No 1000Genomes
tmp_5_13872837_G_A 687 A>V No 1000Genomes

No associated diseases with Q9FKI0

2 regional properties for Q9FKI0

Type Name Position InterPro Accession
domain Far11/STRP, N-terminal 48 - 354 IPR012486
domain Far11/STRP, C-terminal 456 - 812 IPR021819

Functions

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

3 GO annotations of cellular component

Name Definition
actin filament A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
actin filament bundle An assembly of actin filaments that are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

1 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.

5 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 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 network formation The assembly of a network of actin filaments; actin filaments on different axes and with differing orientations are crosslinked together to form a mesh of filaments.
pollen germination The physiological and developmental changes that occur in a heterosporous plant pollen grain, beginning with hydration and terminating with the emergence of the pollen tube through the aperture.
pollen tube growth Growth of pollen via tip extension of the intine wall.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P13797 PLS3 Plastin-3 Homo sapiens (Human) PR
Q9FJ70 FIM3 Fimbrin-3 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SJ84 FIM4 Fimbrin-4 Arabidopsis thaliana (Mouse-ear cress) PR
Q7G188 FIM1 Fimbrin-1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSSYVGVLVS DPWLQSQFTQ VELRTLKSKF VSNKTQLGRF TVGDLPPVFE KLKAFNGTID
70 80 90 100 110 120
EDEIKSVLDK SYPNADDEVD FEFFLRAFLS VQARGVEKSG GSKGASSFLK TSTTTVHHAI
130 140 150 160 170 180
NESEKASYVS HVNNYLRDDP FLKSYLPIDP ATNAFFDLVK DGVLLCKLIN VAVPGTIDER
190 200 210 220 230 240
AINTKKTLNP WERNENLTLG LNSAKAIGCT VVNIGTQDIA EGRPYLVLGL ISQIIKIQML
250 260 270 280 290 300
ADLNFKKTPS LFQLVDDTQD AEELMGLAPE KVLLKWMNFH LKKAGYEKQV TNFSSDLKDG
310 320 330 340 350 360
EAYAYLLNAL APEHSTHVAL ETKDPTERAK KVLEQAEKLD CKRYLSPKDI VDGSANLNLA
370 380 390 400 410 420
FVAQIFQHRN GLTVDDSKTS FAEMMTDDVE TSREERCFRL WINSLGTATY VNNVFEDLRN
430 440 450 460 470 480
GWVLLEVLDK VSPGSVNWKH ANKPPIKMPF KKVENCNEVI KIGKELRFSL VNVAGNDIVQ
490 500 510 520 530 540
GNKKLLLAFL WQLMRYTMLQ LLRNLRSHSQ GKEITDADIL NWANRKVKRG GRTSQADSFR
550 560 570 580 590 600
DKNLSSGMFF LELLSAVEPR VVNWSLVTNG ETEEDKKLNA TYIISVARKL GCSIFLLPED
610 620 630 640 650 660
IIEVNQKMML ILAASIMYWS LQQQSDTEST VSEDATDDGD ANSVAGEISN LSIDGASESS
670 680
PTVQDQELLT KADNDEDEVD GENNKDA