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 Q24020

Entry ID Method Resolution Chain Position Source
AF-Q24020-F1 Predicted AlphaFoldDB

1 variants for Q24020

Variant ID(s) Position Change Description Diseaes Association Provenance
601 G>S No

No associated diseases with Q24020

22 regional properties for Q24020

Type Name Position InterPro Accession
repeat Leucine-rich repeat 30 - 87 IPR001611-1
repeat Leucine-rich repeat 101 - 169 IPR001611-2
repeat Leucine-rich repeat 171 - 191 IPR001611-3
repeat Leucine-rich repeat 220 - 241 IPR001611-4
repeat Leucine-rich repeat 243 - 300 IPR001611-5
repeat Leucine-rich repeat 337 - 358 IPR001611-6
repeat Leucine-rich repeat, typical subtype 28 - 50 IPR003591-1
repeat Leucine-rich repeat, typical subtype 51 - 70 IPR003591-2
repeat Leucine-rich repeat, typical subtype 74 - 98 IPR003591-3
repeat Leucine-rich repeat, typical subtype 99 - 122 IPR003591-4
repeat Leucine-rich repeat, typical subtype 123 - 145 IPR003591-5
repeat Leucine-rich repeat, typical subtype 146 - 168 IPR003591-6
repeat Leucine-rich repeat, typical subtype 169 - 193 IPR003591-7
repeat Leucine-rich repeat, typical subtype 218 - 240 IPR003591-8
repeat Leucine-rich repeat, typical subtype 241 - 264 IPR003591-9
repeat Leucine-rich repeat, typical subtype 265 - 287 IPR003591-10
repeat Leucine-rich repeat, typical subtype 312 - 335 IPR003591-11
repeat Leucine-rich repeat, typical subtype 336 - 358 IPR003591-12
domain Gelsolin-like domain 510 - 589 IPR007123-1
domain Gelsolin-like domain 633 - 703 IPR007123-2
domain Gelsolin-like domain 749 - 822 IPR007123-3
domain Gelsolin-like domain 1168 - 1242 IPR007123-4

Functions

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

4 GO annotations of cellular component

Name Definition
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
Z disc Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.

4 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
calcium ion binding Binding to a calcium ion (Ca2+).
phosphatidylinositol-4,5-bisphosphate binding Binding to phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.

6 GO annotations of biological process

Name Definition
actin filament severing The process in which an actin filament is broken down into smaller filaments.
actin polymerization or depolymerization Assembly or disassembly of actin filaments by the addition or removal of actin monomers from a filament.
adult somatic muscle development The process whose specific outcome is the progression of the adult somatic muscle over time, from its formation to the mature structure.
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.
gastrulation involving germ band extension A complex and coordinated series of cellular movements, including germ band extension, that occurs at the end of cleavage during embryonic development. An example of this process is found in Drosophila melanogaster.
myofibril assembly Formation of myofibrils, the repeating units of striated muscle.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3SX14 GSN Gelsolin Bos taurus (Bovine) 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
O65570 VLN4 Villin-4 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSVLPFVRGV DFTKNDFSAT FPSSMRQMSR VQWLTLDRTQ LAEIPEELGH LQKLEHLSLN
70 80 90 100 110 120
HNRLEKIFGE LTELSCLRSL DLRHNQLKNS GIPPELFHLE ELTTLDLSHN KLKEVPEGLE
130 140 150 160 170 180
RAKNLIVLNL SNNQIESIPT PLFIHLTDLL FLDLSHNRLE TLPPQTRRLI NLKTLDLSHN
190 200 210 220 230 240
PLELFQLRQL PSLQSLEVLK MSGTQRTLLN FPTSIDSLAN LCELDLSHNS LPKLPDCVYN
250 260 270 280 290 300
VVTLVRLNLS DNELTELTAG VELWQRLESL NLSRNQLVAL PAALCKLPKL RRLLVNDNKL
310 320 330 340 350 360
NFEGIPSGIG KLGALEVFSA ANNLLEMVPE GLCRCGALKQ LNLSCNRLIT LPDAIHLLEG
370 380 390 400 410 420
LDQLDLRNNP ELVMPPKPSE ASKATSLEFY NIDFSLQTQL RLAGAAVPPS MPSSATPKDS
430 440 450 460 470 480
TARKIRLRRG PRSEGDQDAA KVLKGMKDVA KDKDNEAGAV PEDGKPESLK PKRWDESLEK
490 500 510 520 530 540
PQLDYSKFFE KDDGQLPGLT IWEIENFLPN KIEEVVHGKF YEGDCYIVLK TKFDDLGLLD
550 560 570 580 590 600
WEIFFWIGNE ATLDKRACAA IHAVNLRNFL GARCRTVREE QGDESEQFLS LFETEVIYIE
610 620 630 640 650 660
GGRTATGFYT IEEMIHITRL YLVHAYGATI HLEPVAPAIT SLDPRHAFVL DLGTHIYIWM
670 680 690 700 710 720
GERSKNTLNS KARLMAEKIS KTERKNKCEI QLERQGEESA EFWQGLGMTS EEADAAEPPK
730 740 750 760 770 780
EHVPEDYQPV QPRLYQVQLG MGYLELPQVE LPEQKLCHTL LNSKHVYILD CYTDLFVWFG
790 800 810 820 830 840
KKSTRLVRAA AVKLSRELFN MMDRPDYALV MRVPEGNEMQ IFRTKFAGWD EVMAVDFTRT
850 860 870 880 890 900
AKSVAKTGAN LTQWARQQET RTDLAALFMP RQSAMPLAEA EQLEEEWNYD LEMMEAFVLE
910 920 930 940 950 960
NKKFVRLPEE ELGRFYTGEC YVFLCRYCIP IEEPENGSED GANPAADVSK SSANNQPEDE
970 980 990 1000 1010 1020
IQCVVYFWQG RNAGNMGWLT FTFTLQKKFK AMFGEELEVV RIFQQQENLK FMSHFKRKFI
1030 1040 1050 1060 1070 1080
IHTGKRKDKA HTAKGKSPVE FFHLRSNGGA LTTRLIQINP DAVHLNSTFC YILHVPFETE
1090 1100 1110 1120 1130 1140
DDSQSGIVYV WIGSKACNEE AKLVQDIAEQ MFNSPWVSLQ ILNEGDEPEN FFWVALGGRK
1150 1160 1170 1180 1190 1200
PYDTDAEYMN YTRLFRCSNE RGYYTVAEKC ADFCQDDLAD DDIMILDNGE HVFLWMGPRC
1210 1220 1230 1240 1250
SEVEVKLAYK SAQVYIQHMR IKQPERPRKL FLTMKNKESR RFTKCFHGWS AFKVYL