WASH1_CHICK
ID WASH1_CHICK Reviewed; 476 AA.
AC Q5ZKA6;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=WASH complex subunit 1 {ECO:0000250|UniProtKB:A8K0Z3};
DE AltName: Full=WAS protein family homolog 1;
GN Name=WASHC1 {ECO:0000250|UniProtKB:A8K0Z3}; Synonyms=WASH1;
GN ORFNames=RCJMB04_12b7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Acts as a nucleation-promoting factor at the surface of
CC endosomes, where it recruits and activates the Arp2/3 complex to induce
CC actin polymerization, playing a key role in the fission of tubules that
CC serve as transport intermediates during endosome sorting.
CC {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7}.
CC -!- SUBUNIT: Component of the WASH complex. {ECO:0000250|UniProtKB:A8K0Z3,
CC ECO:0000250|UniProtKB:C4AMC7}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:A8K0Z3}. Recycling endosome membrane
CC {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 -!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
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DR EMBL; AJ720178; CAG31837.1; -; mRNA.
DR RefSeq; NP_001006245.1; NM_001006245.1.
DR AlphaFoldDB; Q5ZKA6; -.
DR SMR; Q5ZKA6; -.
DR STRING; 9031.ENSGALP00000029912; -.
DR PaxDb; Q5ZKA6; -.
DR GeneID; 418145; -.
DR KEGG; gga:418145; -.
DR CTD; 100287171; -.
DR VEuPathDB; HostDB:geneid_418145; -.
DR eggNOG; ENOG502QSX3; Eukaryota.
DR InParanoid; Q5ZKA6; -.
DR OrthoDB; 904881at2759; -.
DR PhylomeDB; Q5ZKA6; -.
DR PRO; PR:Q5ZKA6; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
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; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..476
FT /note="WASH complex subunit 1"
FT /id="PRO_0000390965"
FT DOMAIN 366..388
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..54
FT /note="Required for WASH complex assembly"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 273..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..476
FT /note="VCA"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 427..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 51683 MW; 6AAD170FC8111383 CRC64;
MTTVAQKHFL EGQTYSVPLI QPDLRREEAV QQVADALQYL QKVSGDIFNR ISQRVETSRA
QLQAISERVT LAQAKIEKIK GSKKAIKVFS SAKYPAPERL QEYCSIFAGA EDPSKQKWPR
HKIQSKHRML DEKSLQEKLK YFPVCVNTKI HQEDDAEEGL GSLPRNISSL SSLLLFNTTE
NLYKKYVFLD PLAGAVTKTH VALETETEEK LFDAPLSITE RGQLDRQVAE NYFYVPDLGQ
VPEIDVPSYL PDLPGIAADL MYSADLGPGI APSAPSSAIP ELPTFSTESV EPSQADLQDP
GLLPPPPPPP PPPPPVMPTT VPPPPPLPQP TAPSEPARTA SEDSSKTVPA ASVQGAPKEV
VNPSTGRASL LESIRQAGGI GKANLRSVKE RKLEKKKQKE QEQVRATGQG GDLMSDLFNK
LVLRRKGISG KGPGASANPD APGSPAGAFA RMSDSIPPLP PPQQPPGEED EDDWES
