P47117

PR
Gene name
ARP3 (ACT4, YJR065C, J1760)
Protein name
Actin-related protein 3
Names
Actin-like protein ARP3, Actin-like protein 3
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YJR065C
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

8-111 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P47117

Entry ID Method Resolution Chain Position Source
AF-P47117-F1 Predicted AlphaFoldDB

1 variants for P47117

Variant ID(s) Position Change Description Diseaes Association Provenance
s10-558307 282 K>R No SGRP

No associated diseases with P47117

1 regional properties for P47117

Type Name Position InterPro Accession
conserved_site Actin/actin-like conserved site 149 - 161 IPR020902

Functions

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

4 GO annotations of cellular component

Name Definition
actin cortical patch An endocytic patch that consists of an actin-containing structure found at the plasma membrane in cells; formed of networks of branched actin filaments that lie just beneath the plasma membrane and assemble, move, and disassemble rapidly. An example of this is the actin cortical patch found in Saccharomyces cerevisiae.
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
Arp2/3 protein complex A stable protein complex that contains two actin-related proteins, Arp2 and Arp3, and five novel proteins (ARPC1-5), and functions in the nucleation of branched actin filaments.
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 binding Binding to monomeric or multimeric forms of actin, including actin filaments.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

3 GO annotations of biological process

Name Definition
actin cortical patch organization A process that is carried out at the cellular level and results in the assembly, arrangement of constituent parts, or disassembly of an actin cortical patch, a discrete actin-containing structure found at the plasma membrane in cells, at sites of endocytosis.
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.
Arp2/3 complex-mediated actin nucleation The actin nucleation process in which actin monomers combine to form a new branch on the side of an existing actin filament; mediated by the Arp2/3 protein complex and its interaction with other proteins.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q12509 ARP6 Actin-like protein ARP6 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q12406 ARP7 Actin-related protein 7 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MSYLNNPAVV MDNGTGLTKL GFAGNDSPSW VFPTAIATAA PSNTKKSSGV GAPSAVSNEA
70 80 90 100 110 120
SYFGNSTSAT NFNGATGGLL SNNLSGKRGT EDLDFYIGNE ALVASQGPSY SLSYPIRHGQ
130 140 150 160 170 180
VENWDHMERF WENSIFKYLR TEPEDHFFLL TEPPLNPPEN REQVAEIFFE SFNCAGLYIA
190 200 210 220 230 240
VQAVLALAAS WTSSKVTDRS LTGTVIDSGD GVTHVIPVAE GYVIGSAIKN IPIAGRDITL
250 260 270 280 290 300
FIQSLLRERG EADTSLRTAE KIKQEYCYVC PDIVKEFNKF DKDPSKFAQF VVENQEKTRR
310 320 330 340 350 360
KVVDIGYERF LAPEIFFNPE IASSDFLTPL PTVVDQTIQA CPIDVRKGLY NNIVLSGGST
370 380 390 400 410 420
MFKDFGRRLQ RDLKSIVNNR IAQSELLSGT KSTGVDVSVI SHRKQRNAVW FGGSLLAQTA
430 440
EFKGYCHTKK DYEEYGPEIV RNFSLFNMV