Q54IR8

PR
Gene name
washc5
Protein name
WASH complex subunit 5
Names
WASH complex subunit strumpellin homolog
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0288569
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

393-523 (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 Q54IR8

Entry ID Method Resolution Chain Position Source
AF-Q54IR8-F1 Predicted AlphaFoldDB

No variants for Q54IR8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54IR8

No associated diseases with Q54IR8

No regional properties for Q54IR8

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q54IR8

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
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
endosome A vacuole to which materials ingested by endocytosis are delivered.
phagolysosome membrane The lipid bilayer surrounding a phagolysosome.
WASH complex A protein complex that localizes at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization. In human, the WASH complex is composed of F-actin-capping protein subunits alpha and beta, WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53.

1 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.

9 GO annotations of biological process

Name Definition
actin filament polymerization Assembly of actin filaments by the addition of actin monomers to a filament.
endosome fission The process by which early and late endosomes undergo budding and fission reactions that separate regions destined for lysosomal degradation from carriers to be recycled to the plasma membrane.
endosome organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of endosomes.
exocytosis A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
lysosome organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lysosome. A lysosome is a cytoplasmic, membrane-bounded organelle that is found in most animal cells and that contains a variety of hydrolases.
phagocytosis A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles.
phagosome reneutralization Any process that increases the pH of the phagosome, measured by the concentration of the hydrogen ion, as part of the process of phagosome maturation.
protein-containing complex organization Any process in which macromolecules aggregate, disaggregate, or are modified, resulting in the formation, disassembly, or alteration of a protein complex.
regulation of actin nucleation Any process that modulates the frequency, rate or extent of actin nucleation, the initial step in the formation of an actin filament in which actin monomers combine to form a new filament.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVKEFLGEGS QAGQNLLRLV SRGNAIIAEL LRLSAHIPSV FKLEDRNEAR KYQDILLDFK
70 80 90 100 110 120
YLSNPDFYES KIEENADLVD LETEFRDNHI DILIRFYHLF ESIYKYIMDL EHYIVDVEKG
130 140 150 160 170 180
FYIHLTIEAI LINGDGKQLL SEAVYLYGVM LILMDNLIEG PVRERMLISY LRNKGPVDLP
190 200 210 220 230 240
LIDEVCKLCK STGYIPGSPK KPPNYPEEYF RRVELPENVI SMIVGRLRSD DLYNGTESFP
250 260 270 280 290 300
QPEHRSVALS TQACMIYVIL YFIPDILNNK NSIMREIVDK FFPDNWVISF FLGFTIDLSV
310 320 330 340 350 360
AWEPYKAAKT AMGNTIIQSN IQYQTQRFWK EVSELNKLVD DLLVDGLLVE EYIVDNVHKI
370 380 390 400 410 420
ITTLRRCNVT IRWVMLHSNA SQKKFKDLVL MGGSQEDVLY LLLNTAQLEF VFKNIFQQLL
430 440 450 460 470 480
ATKEEKWEEN KKLASDSMVE LSEYFSGEKA LTRVKKNENL QKWFGEISQK ISQLDSTDST
490 500 510 520 530 540
STGRKIQQLS LALEEVEQFQ QIDSSIQVKQ FLIETRQFLT KMIKIVNIKE EVLVNLSVCA
550 560 570 580 590 600
DMSYAWEIVN NYVDQMQKGI KSDPKCVLKL RATFLKLVSI LDLPLVRIAQ CSSPDLISVS
610 620 630 640 650 660
EYYSGELVGY VRKVLEIVPK QMFLILKQII NMQTNNIQEM PTKVEKERLR DFAQLDQRYD
670 680 690 700 710 720
LARATHSVSV FTEGILAMET TLVGIIEVDP KQLLEDGIRK ELVLQIALAM DKTLIFSGKP
730 740 750 760 770 780
YQAPSNKQQQ QEIELLQRLK ELSNILDGFR RSFQYIQDYV NIQGLKIWQE EFSRIVNFYV
790 800 810 820 830 840
EQECNSFLKK KVYDWQSQYQ SVAIPIPKFP SQSDQNSQQS VNMIGRLARE LLNQTNCKTT
850 860 870 880 890 900
LYLNQIGWFD PSSGKELVGI NTWSILHQSV GIFGLTGLDK LFSFMMVKDL QVFVSQTRSL
910 920 930 940 950 960
VEKSLKGFLN EFEDYLRPTT NIPDTMIRYQ QALDKTKLLY PIFIDVLTKI GQIQLIRRQI
970 980 990 1000 1010 1020
SNQLNFHCKI DSNMLFSSLD IMNKSLLNDI ESHFQRPDSN PYPSDDNTLL FDLAQYLDTA
1030 1040 1050 1060 1070 1080
GINDPFTKIY ITTSPLEQFP CLLFLFVLSQ VSKFQFNSKL NVMSSKKQKN SYDWTPFIIG
1090 1100 1110 1120 1130 1140
CITILQQFHS LHTQKFLAFV GQYIKSHINI ALANPKENNK DDADYPEDVI GLLRFLEDFC
1150 1160
KYSHTSRKIV EGYVPPYIFD YYNN