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WASH1_BOVIN
ID   WASH1_BOVIN             Reviewed;         471 AA.
AC   A7Z063;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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;
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=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2007) 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. Involved in
CC       endocytic trafficking of EGF. Involved in transferrin receptor
CC       recycling. Regulates the trafficking of endosomal alpha5beta1 integrin
CC       to the plasma membrane and involved in invasive cell migration. In T-
CC       cells involved in endosome-to-membrane recycling of receptors including
CC       T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T-
CC       cell proliferation and effector function. In dendritic cells involved
CC       in 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 negative regulation of autophagy independently from its
CC       role in endosomal sorting by inhibiting BECN1 ubiquitination to
CC       inactivate PIK3C3/Vps34 activity (By similarity).
CC       {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7,
CC       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); the
CC       assembly has been initially described as WASH complex
CC       (PubMed:20498093). Interacts (via WHD1 region) with WASHC2; the
CC       interaction is direct. Interacts with alpha-tubulin. Interacts with
CC       BECN1; WASHC1 and AMBRA1 can competitively interact with BECN1.
CC       Interacts with BLOC1S2; may associate with the BLOC-1 complex.
CC       Interacts with tubulin gamma chain (TUBG1 or TUBG2) (By similarity).
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:A8K0Z3}. Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:Q8VDD8}. Late endosome
CC       {ECO:0000250|UniProtKB:A8K0Z3}. Cytoplasmic vesicle, autophagosome
CC       {ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome
CC       membrane is mediated via its interaction with WASHC2.
CC       {ECO:0000250|UniProtKB:A8K0Z3}.
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; BC153261; AAI53262.1; -; mRNA.
DR   RefSeq; NP_001098876.1; NM_001105406.1.
DR   AlphaFoldDB; A7Z063; -.
DR   SMR; A7Z063; -.
DR   STRING; 9913.ENSBTAP00000015790; -.
DR   PaxDb; A7Z063; -.
DR   PeptideAtlas; A7Z063; -.
DR   PRIDE; A7Z063; -.
DR   Ensembl; ENSBTAT00000069933; ENSBTAP00000059564; ENSBTAG00000011902.
DR   GeneID; 533602; -.
DR   KEGG; bta:533602; -.
DR   CTD; 100287171; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011902; -.
DR   eggNOG; ENOG502QSX3; Eukaryota.
DR   GeneTree; ENSGT00390000016717; -.
DR   HOGENOM; CLU_029156_1_0_1; -.
DR   InParanoid; A7Z063; -.
DR   OMA; MYSAAKY; -.
DR   OrthoDB; 904881at2759; -.
DR   TreeFam; TF318222; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000011902; Expressed in retina and 105 other tissues.
DR   ExpressionAtlas; A7Z063; baseline and differential.
DR   GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
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:0005770; C:late endosome; 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; IDA: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   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endosome;
KW   Membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..471
FT                   /note="WASH complex subunit 1"
FT                   /id="PRO_0000390961"
FT   DOMAIN          365..387
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          297..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..471
FT                   /note="VCA"
FT                   /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT   COMPBIAS        301..336
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  50773 MW;  15F8DDCF10B5816A CRC64;
     MTPTGTQHSL AGQTYAVPLI QPDLRREEAI QQVADALQYL QKVSGDIFSR ISQRVELSRS
     QLQAIGERVS LAQAKIEKIK GSKKAIKVFS SAKYPAPERL QEYGSIFMGA QDPGLQRRPR
     HRIQSKHRPL DERALQEKLK FFPVCVNTKP EPEDEAEEGL GGLPSNISSV SSLLLFNTTE
     NLYKKYVFLD PLAGAVTKTH VMLGAETEEK LFDAPLSISR REQLERQVPE NYFYVPDLGQ
     VPDIDVPSYL PDLPGVADDL MYSADLGPGI APSAPGAIPE LPTFHTEVAQ PFKPDLEDGV
     LTARPPPPPP PPPPPAPAVL MSVPPPPPPP QAPPGQPAKG DDSGGASPSA PVQGAPKEVV
     DPSSGRATLL ESIRQAGGIG KAKLRSVKER KLEKKKQKEQ EQVRATSQGG DLMSDLFNKL
     AMRRKGISGK GPGSGASEGP GGAFARMSDS IPPLPPPQQP PGEEDEDDWE S
 
 
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