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 Q3SX14

Entry ID Method Resolution Chain Position Source
AF-Q3SX14-F1 Predicted AlphaFoldDB

No variants for Q3SX14

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3SX14

No associated diseases with Q3SX14

6 regional properties for Q3SX14

Type Name Position InterPro Accession
domain Gelsolin-like domain 25 - 107 IPR007123-1
domain Gelsolin-like domain 147 - 219 IPR007123-2
domain Gelsolin-like domain 266 - 338 IPR007123-3
domain Gelsolin-like domain 404 - 485 IPR007123-4
domain Gelsolin-like domain 527 - 591 IPR007123-5
domain Gelsolin-like domain 630 - 705 IPR007123-6

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 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.
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.

3 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.
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.

7 GO annotations of biological process

Name Definition
actin filament severing The process in which an actin filament is broken down into smaller filaments.
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.
actin polymerization or depolymerization Assembly or disassembly of actin filaments by the addition or removal of actin monomers from a 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.
cell projection assembly Formation of a prolongation or process extending from a cell, e.g. a flagellum or axon.
central nervous system development The process whose specific outcome is the progression of the central nervous system over time, from its formation to the mature structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain and spinal cord. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
cilium assembly The assembly of a cilium, a specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface. Each cilium is bounded by an extrusion of the cytoplasmic membrane, and contains a regular longitudinal array of microtubules, anchored basally in a centriole.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
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
O65570 VLN4 Villin-4 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MVVEHPEFLK AGKEPGLQIW RVEKFDLVPV PPNLYGDFFT GDAYVILKTV QLRNGNLQYD
70 80 90 100 110 120
LHYWLGNECS QDESGAAAIF TVQLDDYLNG RAVQHREVQG FESATFLGYF KSGLKYKKGG
130 140 150 160 170 180
VASGFKHVVP NEVVVQRLFQ VKGRRVVRAT EVPVSWESFN NGDCFILDLG NDIYQWCGSS
190 200 210 220 230 240
SNRFERLKAT QVSKGIRDNE RSGRARVHVS EEGAEPEAML EVLGPKPALP AGTEDTAKED
250 260 270 280 290 300
AANRKLAKLY KVSNGAGTMS VSLVADENPF AQGALRSEDC FILDHGKDGK IFVWKGRQAN
310 320 330 340 350 360
TEERKAALKT ASDFISKMDY PRQTQVSVLP EGGETPLFKQ FFKNWRDPDQ TDGPGLSYLS
370 380 390 400 410 420
SHIANVERVP FDAATLHTST AMAAQHGMDD DGRGQKQIWR IEGSDKVPVD PATYGQFYGG
430 440 450 460 470 480
DSYIILYNYR HGGRQGQIIY NWQGAQSTQD EVAASAILTA QLDEELGGTP VRSRVVQGKE
490 500 510 520 530 540
PAHLMSLFGG KPMIIYRGGT SREGGQTAPA STRLFQVRAS SSGATRAVEV MPKAGALNSN
550 560 570 580 590 600
DAFVLKTPSA AYLWVGAGAS EAEKTGALEL LRVLRAQPVQ VAEGSEPDSF WEALGGKAAY
610 620 630 640 650 660
RTSPRLKDKK MDAHPPRLFA CSNKIGRFVI EEVPGELMQE DLATDDVMLL DTWDQVFVWV
670 680 690 700 710 720
GKDSQEEEKT EALTSAKRYI ETDPANRDRR TPITVVKQGF EPPSFVGWFL GWDDNYWSVD
730
PLDRALAELA A