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

2 structures for O65570

Entry ID Method Resolution Chain Position Source
5VNT NMR - A 912-974 PDB
AF-O65570-F1 Predicted AlphaFoldDB

43 variants for O65570

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_4_14754691_G_C 22 E>Q No 1000Genomes
tmp_4_14754749_A_G 41 K>R No 1000Genomes
ENSVATH02943138 45 G>A No 1000Genomes
ENSVATH06801929 85 T>I No 1000Genomes
ENSVATH00545112 168 Y>F No 1000Genomes
tmp_4_14755387_A_G 169 I>V No 1000Genomes
ENSVATH06801933 248 T>P No 1000Genomes
tmp_4_14755862_T_A 272 L>M No 1000Genomes
ENSVATH12311778 278 D>E No 1000Genomes
ENSVATH02943140 278 D>N No 1000Genomes
tmp_4_14755976_G_A 310 A>T No 1000Genomes
ENSVATH12311779 312 E>D No 1000Genomes
ENSVATH00545114 313 E>K No 1000Genomes
ENSVATH12311780 314 M>I No 1000Genomes
ENSVATH12311781 316 R>C No 1000Genomes
ENSVATH06801939 379 P>S No 1000Genomes
ENSVATH06801939 379 P>T No 1000Genomes
ENSVATH12311782 398 R>L No 1000Genomes
tmp_4_14756561_A_T,G 444 Q>L No 1000Genomes
tmp_4_14756561_A_T,G 444 Q>R No 1000Genomes
ENSVATH12311806 451 G>C No 1000Genomes
tmp_4_14756704_C_T 455 S>F No 1000Genomes
tmp_4_14757087_G_T 510 D>Y No 1000Genomes
tmp_4_14757171_G_A 538 D>N No 1000Genomes
tmp_4_14757319_T_A 559 F>Y No 1000Genomes
ENSVATH12311809 610 S>L No 1000Genomes
ENSVATH14314157 620 R>C No 1000Genomes
ENSVATH12311810 620 R>H No 1000Genomes
ENSVATH12311811 626 S>A No 1000Genomes
ENSVATH06801946 628 T>S No 1000Genomes
tmp_4_14758202_C_T 695 S>F No 1000Genomes
tmp_4_14758242_G_C 708 E>D No 1000Genomes
ENSVATH00545118 725 A>T No 1000Genomes
tmp_4_14758617_T_G 767 S>A No 1000Genomes
tmp_4_14758690_A_G 791 N>S No 1000Genomes
ENSVATH14314161 837 A>T No 1000Genomes
tmp_4_14758893_G_A 859 A>T No 1000Genomes
tmp_4_14759083_C_T 863 T>I No 1000Genomes
ENSVATH12311827 879 K>E No 1000Genomes
ENSVATH14314163 880 K>R No 1000Genomes
tmp_4_14759248_A_G 918 D>G No 1000Genomes
tmp_4_14759417_A_G 944 E>G No 1000Genomes
ENSVATH00545120 947 E>D No 1000Genomes

No associated diseases with O65570

5 regional properties for O65570

Type Name Position InterPro Accession
domain Villin headpiece 909 - 974 IPR003128
domain Gelsolin-like domain 29 - 111 IPR007123-1
domain Gelsolin-like domain 150 - 217 IPR007123-2
domain Gelsolin-like domain 267 - 333 IPR007123-3
domain Gelsolin-like domain 638 - 711 IPR007123-4

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
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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 filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
mRNA binding Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.

7 GO annotations of biological process

Name Definition
actin crosslink formation The process in which two or more actin filaments are connected together by proteins that act as crosslinks between the filaments. The crosslinked filaments may be on the same or differing axes.
actin filament capping The binding of a protein or protein complex to the end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits.
actin filament depolymerization Disassembly of actin filaments by the removal of actin monomers from a filament.
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 filament severing The process in which an actin filament is broken down into smaller filaments.
cytoplasmic streaming The directed flow of cytosol (the liquid component of the cytoplasm) and the organelles it contains.
root hair elongation The process in which the root hair grows longer.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3SX14 GSN Gelsolin Bos taurus (Bovine) PR
Q24020 fliI Protein flightless-1 Drosophila melanogaster (Fruit fly) PR
O75366 AVIL Advillin Homo sapiens (Human) PR
P06396 GSN Gelsolin Homo sapiens (Human) PR
P13020 Gsn Gelsolin Mus musculus (Mouse) PR
Q68FP1 Gsn Gelsolin Rattus norvegicus (Rat) PR
P34268 fli-1 Protein flightless-1 homolog Caenorhabditis elegans PR
10 20 30 40 50 60
MSVSMRDLDP AFQGAGQKAG IEIWRIENFI PTPIPKSSIG KFFTGDSYIV LKTTALKTGA
70 80 90 100 110 120
LRHDIHYWLG KDTSQDEAGT AAVKTVELDA ALGGRAVQYR EVQGHETEKF LSYFKPCIIP
130 140 150 160 170 180
QEGGVASGFK HVVAEEHITR LFVCRGKHVV HVKEVPFARS SLNHDDIYIL DTKSKIFQFN
190 200 210 220 230 240
GSNSSIQERA KALEVVQYIK DTYHDGTCEV ATVEDGKLMA DADSGEFWGF FGGFAPLPRK
250 260 270 280 290 300
TANDEDKTYN SDITRLFCVE KGQANPVEGD TLKREMLDTN KCYILDCGIE VFVWMGRTTS
310 320 330 340 350 360
LDDRKIASKA AEEMIRSSER PKSQMIRIIE GFETVPFRSK FESWTQETNT TVSEDGRGRV
370 380 390 400 410 420
AALLQRQGVN VRGLMKAAPP KEEPQVFIDC TGNLQVWRVN GQAKTLLQAA DHSKFYSGDC
430 440 450 460 470 480
YVFQYSYPGE EKEEVLIGTW FGKQSVEEER GSAVSMASKM VESMKFVPAQ ARIYEGKEPI
490 500 510 520 530 540
QFFVIMQSFI VFKGGISSGY KKYIAEKEVD DDTYNENGVA LFRIQGSGPE NMQAIQVDPV
550 560 570 580 590 600
AASLNSSYYY ILHNDSSVFT WAGNLSTATD QELAERQLDL IKPNQQSRAQ KEGSESEQFW
610 620 630 640 650 660
ELLGGKAEYS SQKLTKEPER DPHLFSCTFT KEVLKVTEIY NFTQDDLMTE DIFIIDCHSE
670 680 690 700 710 720
IFVWVGQEVV PKNKLLALTI GEKFIEKDSL LEKLSPEAPI YVIMEGGEPS FFTRFFTSWD
730 740 750 760 770 780
SSKSAMHGNS FQRKLKIVKN GGTPVADKPK RRTPASYGGR ASVPDKSQQR SRSMSFSPDR
790 800 810 820 830 840
VRVRGRSPAF NALAATFESQ NARNLSTPPP VVRKLYPRSV TPDSSKFAPA PKSSAIASRS
850 860 870 880 890 900
ALFEKIPPQE PSIPKPVKAS PKTPESPAPE SNSKEQEEKK ENDKEEGSMS SRIESLTIQE
910 920 930 940 950 960
DAKEGVEDEE DLPAHPYDRL KTTSTDPVSD IDVTRREAYL SSEEFKEKFG MTKEAFYKLP
970
KWKQNKFKMA VQLF