ID   WASC3_BOVIN             Reviewed;         194 AA.
AC   Q05B58;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=WASH complex subunit 3 {ECO:0000250|UniProtKB:Q9Y3C0};
DE   AltName: Full=Coiled-coil domain-containing protein 53;
GN   Name=WASHC3 {ECO:0000250|UniProtKB:Q9Y3C0}; Synonyms=CCDC53;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION IN THE WASH COMPLEX.
RX   PubMed=20498093; DOI=10.1073/pnas.0913293107;
RA   Jia D., Gomez T.S., Metlagel Z., Umetani J., Otwinowski Z., Rosen M.K.,
RA   Billadeau D.D.;
RT   "WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein
RT   (WASP) family are controlled by analogous structurally related complexes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:10442-10447(2010).
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.
CC       {ECO:0000250|UniProtKB:Q9Y3C0}.
CC   -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC       regulatory complex (SHRC) composed of WASHC1, WASHC2, WASHC3, WASHC4
CC       and WASHC5 (PubMed:20498093). The WASH core complex associates via
CC       WASHC2 with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2
CC       or CAPZA3 and CAPZB) in a transient or substoichiometric manner which
CC       was initially described as WASH complex. {ECO:0000250|UniProtKB:Q9Y3C0,
CC       ECO:0000269|PubMed:20498093}.
CC   -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CCDC53 family. {ECO:0000305}.
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DR   EMBL; BC122780; AAI22781.1; -; mRNA.
DR   RefSeq; NP_001073782.1; NM_001080313.2.
DR   AlphaFoldDB; Q05B58; -.
DR   SMR; Q05B58; -.
DR   STRING; 9913.ENSBTAP00000000022; -.
DR   PaxDb; Q05B58; -.
DR   PRIDE; Q05B58; -.
DR   GeneID; 613720; -.
DR   KEGG; bta:613720; -.
DR   CTD; 51019; -.
DR   eggNOG; KOG4496; Eukaryota.
DR   InParanoid; Q05B58; -.
DR   OrthoDB; 1425330at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR   GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019309; WASHC3.
DR   PANTHER; PTHR13015; PTHR13015; 1.
DR   Pfam; PF10152; CCDC53; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Endosome; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..194
FT                   /note="WASH complex subunit 3"
FT                   /id="PRO_0000390954"
FT   REGION          98..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          46..74
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        160..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3C0"
SQ   SEQUENCE   194 AA;  21345 MW;  9643A1D92FC31A8F CRC64;
     MDEDGLPLMG SGIDLTKVPA IQQKRTVAFL NQFVVHTVQF LNRFSTVCEE KLADLSLRIQ
     QIETTLNILD AKLSSIPGLD DVTFEVSPVN VTRITNGTHS EATSEQSQQN SLQDSGPQES
     EVTPENILTV AKDPRYARYH KMVQVGVPVM AIRNKMISEG LDPDLLERPD APVPDGEGEK
     NTEESSDSES SFSD