WASH1_RAT
ID WASH1_RAT Reviewed; 475 AA.
AC B2RYF7;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=WASH complex subunit 1 {ECO:0000312|RGD:1310196};
DE AltName: Full=WAS protein family homolog 1;
GN Name=Washc1 {ECO:0000312|RGD:1310196}; Synonyms=Wash1, Wash2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acts as a component of the WASH core complex that functions
CC as a nucleation-promoting factor (NPF) at the surface of endosomes,
CC where it recruits and activates the Arp2/3 complex to induce actin
CC polymerization, playing a key role in the fission of tubules that serve
CC as transport intermediates during endosome sorting. Regulates the
CC trafficking of endosomal alpha5beta1 integrin to the plasma membrane
CC and involved in invasive cell migration. In T-cells involved in
CC endosome-to-membrane recycling of receptors including T-cell receptor
CC (TCR), CD28 and ITGAL; proposed to be implicated in T-cell
CC proliferation and effector function. In dendritic cells involved in
CC endosome-to-membrane recycling of major histocompatibility complex
CC (MHC) class II probably involving retromer and subsequently allowing
CC antigen sampling, loading and presentation during T-cell activation.
CC Involved in cytokinesis and following polar body extrusion during
CC oocyte meiotic maturation. Involved in Arp2/3 complex-dependent actin
CC assembly driving Salmonella typhimurium invasion independent of
CC ruffling. Involved in the exocytosis of MMP14 leading to matrix
CC remodeling during invasive migration and implicating late endosome-to-
CC plasma membrane tubular connections and cooperation with the exocyst
CC complex. Involved in negative regulation of autophagy independently
CC from its role in endosomal sorting by inhibiting BECN1 ubiquitination
CC to inactivate PIK3C3/Vps34 activity. {ECO:0000250|UniProtKB:A8K0Z3,
CC ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8}.
CC -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC regulatory complex SHRC composed of WASHC1, WASHC2, WASHC3, WASHC4 and
CC WASHC5. The WASH core complex associates with the F-actin-capping
CC protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a
CC transient or substoichiometric manner which was initially described as
CC WASH complex. Interacts (via WHD1 region) with WASHC2; the interaction
CC is direct. Interacts with BECN1; WASHC1 and AMBRA1 can competitively
CC interact with BECN1. Interacts with BLOC1S2; may associate with the
CC BLOC-1 complex. Interacts with tubulin gamma chain (TUBG1 or TUBG2).
CC Interacts with TBC1D23 (By similarity). {ECO:0000250|UniProtKB:A8K0Z3,
CC ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q8VDD8}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome
CC membrane is mediated via its interaction with WASHC2. Localized to
CC Salmonella typhimurium entry sites (By similarity).
CC {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:Q8VDD8}.
CC -!- DOMAIN: The VCA (verprolin, cofilin, acidic) domain promotes actin
CC polymerization by the Arp2/3 complex in vitro.
CC {ECO:0000250|UniProtKB:C4AMC7}.
CC -!- PTM: Ubiquitinated at Lys-219 via 'Lys-63'-linked ubiquitin chains by
CC the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to promote
CC endosomal F-actin assembly. {ECO:0000250|UniProtKB:A8K0Z3}.
CC -!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
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DR EMBL; BC166761; AAI66761.1; -; mRNA.
DR RefSeq; NP_001120862.1; NM_001127390.1.
DR AlphaFoldDB; B2RYF7; -.
DR SMR; B2RYF7; -.
DR IntAct; B2RYF7; 6.
DR STRING; 10116.ENSRNOP00000016588; -.
DR PhosphoSitePlus; B2RYF7; -.
DR PeptideAtlas; B2RYF7; -.
DR PRIDE; B2RYF7; -.
DR GeneID; 367328; -.
DR KEGG; rno:367328; -.
DR UCSC; RGD:1310196; rat.
DR CTD; 100287171; -.
DR RGD; 1310196; Washc1.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; B2RYF7; -.
DR OrthoDB; 904881at2759; -.
DR PhylomeDB; B2RYF7; -.
DR PRO; PR:B2RYF7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:0031083; C:BLOC-1 complex; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0002468; P:dendritic cell antigen processing and presentation; ISO:RGD.
DR GO; GO:0032456; P:endocytic recycling; ISO:RGD.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISO:RGD.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; ISO:RGD.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:RGD.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0090306; P:meiotic spindle assembly; ISO:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; ISO:RGD.
DR GO; GO:0001556; P:oocyte maturation; ISO:RGD.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:1904109; P:positive regulation of cholesterol import; ISO:RGD.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:RGD.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0050776; P:regulation of immune response; ISO:RGD.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR InterPro; IPR028290; WASH1.
DR InterPro; IPR021854; WASH1_WAHD.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23331; PTHR23331; 1.
DR Pfam; PF11945; WASH_WAHD; 1.
DR PROSITE; PS51082; WH2; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Endosome; Isopeptide bond; Membrane; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..475
FT /note="WASH complex subunit 1"
FT /id="PRO_0000390964"
FT DOMAIN 369..391
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..167
FT /note="WHD1"
FT REGION 1..54
FT /note="Required for WASH complex assembly"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 296..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..475
FT /note="VCA"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT COMPBIAS 299..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:A8K0Z3"
SQ SEQUENCE 475 AA; 51327 MW; DCBD9991A1B689F9 CRC64;
MTAVKTQHSL AGQVYAVPLI QPDLRREEAI QQVADALQYL QNISGDIFSR ISQRVELSRR
QLQAIGERVS LAQAKIEKIK GSKKAIKVFS SAKYPAPEHL QEYNSVFTGA LDPGLQRRPR
YRIQSKHRPL DERALQEKLK YFPVCVSTKS EPEDEAEEGL GGLPSNISSI SSLLLFNTTE
NLYKKYVFLD PLAGAVTKTH TMLGTEEEKL FDAPLSISKR EQLEQPAPEN YFYVPGLGQV
PEIDVPSYLP DLPGVADDLM YSADLGPGIA PSAPGAIPEL PAFHTEVAEP FQPEREDGAL
LAPPPPPPPP PPPPPPAPTA VVSAPQPPMS PDVVTVTGKV AREEDSGSGE AHSASVQGAP
KEVVDPSSGR ATLLESIRQA GGIGKAKLRS VKERKLEKKK QKEQEQVRAT SQGGDLMSDL
FNKLVMRRKG ISGKGPGTGT SEGPGGAFSR MSDSIPPLPP PQQPAGDEDE DDWES
