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 Q9FJ70

Entry ID Method Resolution Chain Position Source
AF-Q9FJ70-F1 Predicted AlphaFoldDB

41 variants for Q9FJ70

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_5_22458940_A_G 4 F>S No 1000Genomes
tmp_5_22458901_T_G 17 Q>P No 1000Genomes
tmp_5_22458878_T_G 25 S>R No 1000Genomes
tmp_5_22458752_T_G 39 K>Q No 1000Genomes
ENSVATH03434185 43 E>K No 1000Genomes
ENSVATH03434184 78 D>A No 1000Genomes
ENSVATH07425496 82 D>E No 1000Genomes
ENSVATH07425493 132 L>F No 1000Genomes
ENSVATH14633733 200 T>M No 1000Genomes
tmp_5_22458019_T_A 219 Q>L No 1000Genomes
ENSVATH12782894 243 A>T No 1000Genomes
tmp_5_22457738_C_T 254 V>I No 1000Genomes
tmp_5_22457721_G_T 259 D>E No 1000Genomes
ENSVATH07425488 260 N>D No 1000Genomes
ENSVATH07425486 289 K>N No 1000Genomes
tmp_5_22457531_T_A 294 N>I No 1000Genomes
ENSVATH14633732 316 H>Y No 1000Genomes
ENSVATH07425482 322 L>P No 1000Genomes
ENSVATH00735662 341 M>I No 1000Genomes
ENSVATH07425480 355 G>A No 1000Genomes
ENSVATH07425479 378 G>C No 1000Genomes
tmp_5_22456963_C_G 398 C>S No 1000Genomes
tmp_5_22456962_A_C 398 C>W No 1000Genomes
tmp_5_22456936_C_T 407 G>E No 1000Genomes
ENSVATH07425475 420 R>G No 1000Genomes
ENSVATH07425474 420 R>I No 1000Genomes
ENSVATH12782890 429 V>A No 1000Genomes
ENSVATH07425471 477 N>D No 1000Genomes
ENSVATH07425464 535 S>L No 1000Genomes
ENSVATH07425459 544 S>I No 1000Genomes
ENSVATH07425457 547 S>N No 1000Genomes
tmp_5_22455850_T_C 610 I>M No 1000Genomes
ENSVATH07425431 642 H>Y No 1000Genomes
tmp_5_22455656_T_C 675 E>G No 1000Genomes
tmp_5_22455654_C_T 676 V>I No 1000Genomes
ENSVATH00735654 691 T>P No 1000Genomes
tmp_5_22455598_T_G 694 E>D No 1000Genomes
ENSVATH03434166 698 A>T No 1000Genomes
ENSVATH14633729 699 D>E No 1000Genomes
tmp_5_22455545_G_A 712 A>V No 1000Genomes
ENSVATH07425427 714 E>D No 1000Genomes

No associated diseases with Q9FJ70

5 regional properties for Q9FJ70

Type Name Position InterPro Accession
conserved_site Actinin-type actin-binding domain, conserved site 213 - 237 IPR001589
domain Calponin homology domain 124 - 241 IPR001715-1
domain Calponin homology domain 269 - 372 IPR001715-2
domain Calponin homology domain 393 - 499 IPR001715-3
domain Calponin homology domain 514 - 622 IPR001715-4

Functions

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

4 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.
plant-type vacuole A closed structure that is completely surrounded by a unit membrane, contains liquid, and retains the same shape regardless of cell cycle phase. An example of this structure is found in Arabidopsis thaliana.

2 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.
metal ion binding Binding to a metal ion.

2 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 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.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P13797 PLS3 Plastin-3 Homo sapiens (Human) PR
Q9FKI0 FIM5 Fimbrin-5 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
MSGFVGVIVS DPWLQSQLTQ VELRSLNSKF VALKNQSGKV TLEDLPSVLV KVKSLSSSFK
70 80 90 100 110 120
EKEIKEILGG LGSDYESDDD LDFESFLKVY LNLRDKAADK AGGGLKHSSS FLKAGTTTLH
130 140 150 160 170 180
TINQSEKGSF VLHINRYLGD DPFLKQFLPL DPDSNDLYEL VKDGVLLCKL INIAVPGTID
190 200 210 220 230 240
ERAINTKRVL NPWERNENHT LCLNSAKAVG CSVVNIGTQD LAEGRPHLVL GLISQLIKIQ
250 260 270 280 290 300
LLADLSLKKM PQLVELVEDN EDIEEFLRLP PEKVLLKWMN FHLKKGGYKK TVGNFSSDLK
310 320 330 340 350 360
DAQAYAYLLN VLAPEHCDPA TLNAEDDLER ANMVLEHAER MNCKRYLTAE EIVEGSSYLN
370 380 390 400 410 420
LAFVAQIFHE RNGLSTDGRF SFAEMMTEDL QTCRDERCYR LWINSLGIES YVNNVFEDVR
430 440 450 460 470 480
NGWILLEVVD KVYPGSVNWK QASKPPIKMP FRKVENCNQV VKIGKEMRFS LVNVAGNDIV
490 500 510 520 530 540
QGNKKLILGF LWQLMRTHML QLLKSLRSRT RGKDMTDSEI ISWANRKVRI MGRKSQIESF
550 560 570 580 590 600
KDKSLSSGLF FLDLLWAVEP RVVNWNLVTK GESDDEKRLN ATYIVSVARK LGCSVFLLPE
610 620 630 640 650 660
DIVEVNQKMI LILTASIMYW SLQQQSSSSE SSSSSSDSSS THSTTTTCTS TCTSTDASPA
670 680 690 700 710
PSVTGEDEVS SLNGEVSSLT IEEDNEVSSL TIEEDNDADI LSDITSISEE AANE