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WAS protein family homolog 2 (CXYorf1-like protein on chromosome 2) (Protein FAM39B)

 WASH2_HUMAN             Reviewed;         465 AA.
Q6VEQ5;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
19-JAN-2010, sequence version 2.
28-FEB-2018, entry version 92.
RecName: Full=WAS protein family homolog 2;
AltName: Full=CXYorf1-like protein on chromosome 2;
AltName: Full=Protein FAM39B;
Name=WASH2P; Synonyms=FAM39B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 202-465, AND GENE DUPLICATION.
PubMed=15233989; DOI=10.1016/j.ygeno.2004.03.001;
Wong A., Vallender E.J., Heretis K., Ilkin Y., Lahn B.T.,
Lese Martin C., Ledbetter D.H.;
"Diverse fates of paralogs following segmental duplication of
telomeric genes.";
Genomics 84:239-247(2004).
[3]
GENE DUPLICATION.
PubMed=10655549; DOI=10.1093/hmg/9.3.395;
Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F.,
Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A.,
Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A.,
Cocchia S., Mercadante G., Pannone E., Archidiacono N., Rocchi M.,
Schlessinger D., D'Urso M.;
"Differentially regulated and evolved genes in the fully sequenced
Xq/Yq pseudoautosomal region.";
Hum. Mol. Genet. 9:395-401(2000).
[4]
GENE DUPLICATION.
PubMed=18159949; DOI=10.1371/journal.pgen.0030237;
Linardopoulou E.V., Parghi S.S., Friedman C., Osborn G.E.,
Parkhurst S.M., Trask B.J.;
"Human subtelomeric WASH genes encode a new subclass of the WASP
family.";
PLoS Genet. 3:E237-E237(2007).
-!- FUNCTION: Acts as a nucleation-promoting factor at the surface of
endosomes, where it recruits and activates the Arp2/3 complex to
induce actin polymerization, playing a key role in the fission of
tubules that serve as transport intermediates during endosome
sorting. Involved in endocytic trafficking of EGF. Its assembly in
the WASH core complex seems to inhibit its NPF activity and via
WASHC2 is required for its membrane targeting. Involved in
transferrin receptor recycling. Regulates the trafficking of
endosomal alpha5beta1 integrin to the plasma membrane and involved
in invasive cell migration. In T-cells involved in endosome-to-
membrane recycling of receptors including T-cell receptor (TCR),
CD28 and ITGAL; proposed to be implicated in T-cell proliferation
and effector function. In dendritic cells involved in endosome-to-
membrane recycling of major histocompatibility complex (MHC) class
II probably involving retromer and subsequently allowing antigen
sampling, loading and presentation during T-cell activation.
Involved in Arp2/3 complex-dependent actin assembly driving
Salmonella typhimurium invasion independent of ruffling. Involved
in the exocytosis of MMP14 leading to matrix remodeling during
invasive migration and implicating late endosome-to-plasma
membrane tubular connections and cooperation with the exocyst
complex. Involved in negative regulation of autophagy
independently from its role in endosomal sorting by inhibiting
BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By
similarity). {ECO:0000250|UniProtKB:A8K0Z3,
ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8}.
-!- SUBUNIT: Component of the WASH core complex also described as WASH
regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or
WASH3P), WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5.
The WASH core complex associates with the F-actin-capping protein
dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a
transient or substoichiometric manner which was initially
described as WASH complex. Interacts (via WHD1 region) with
WASHC2C; the interaction is direct. Interacts with alpha-tubulin.
Interacts with BECN1; WASHC1 and AMBRA1 can competetively interact
with BECN1. Interacts with BLOC1S2; may associate with the BLOC-1
complex. Interacts with tubulin gamma chain (TUBG1 or TUBG2).
Interacts with EXOC1, EXOC4, EXOC8; in MMP14-positive endosomes in
breast tumor cells; indicative for an association with the exocyst
complex (By similarity). {ECO:0000250|UniProtKB:A8K0Z3,
ECO:0000250|UniProtKB:C4AMC7, ECO:0000250|UniProtKB:Q8VDD8}.
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000250|UniProtKB:A8K0Z3}. Recycling endosome membrane
{ECO:0000250|UniProtKB:Q8VDD8}. Late endosome
{ECO:0000250|UniProtKB:A8K0Z3}. Cytoplasmic vesicle, autophagosome
{ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole
{ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome
membrane is mediated via its interaction with WASHC2.
{ECO:0000250|UniProtKB:A8K0Z3}.
-!- DOMAIN: The VCA (verprolin, cofilin, acidic) domain promotes actin
polymerization by the Arp2/3 complex in vitro.
{ECO:0000250|UniProtKB:C4AMC7}.
-!- MISCELLANEOUS: WASH genes duplicated to multiple chromosomal ends
during primate evolution, with highest copy number reached in
humans, whose WASH repertoires probably vary extensively among
individuals (PubMed:18159949). It is therefore difficult to
determine which gene is functional or not. The telomeric region of
chromosome 9p is paralogous to the pericentromeric regions of
chromosome 9 as well as to 2q. Paralogous regions contain 7
transcriptional units. Duplicated WASH genes are also present in
the Xq/Yq pseudoautosomal region, as well as on chromosome 1 and
15. The chromosome 16 copy seems to be a pseudogene.
{ECO:0000305|PubMed:18159949}.
-!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AL078621; Type=Erroneous termination; Positions=25; Note=Translated as Arg.; Evidence={ECO:0000305};
Sequence=AL078621; Type=Erroneous termination; Positions=180; Note=Translated as Glu.; Evidence={ECO:0000305};
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EMBL; AL078621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY341936; AAQ76875.1; -; mRNA.
UniGene; Hs.446466; -.
UniGene; Hs.459573; -.
UniGene; Hs.709408; -.
IntAct; Q6VEQ5; 5.
MINT; Q6VEQ5; -.
STRING; 9606.ENSP00000352498; -.
DMDM; 284018148; -.
EPD; Q6VEQ5; -.
MaxQB; Q6VEQ5; -.
PaxDb; Q6VEQ5; -.
PeptideAtlas; Q6VEQ5; -.
PRIDE; Q6VEQ5; -.
GeneCards; WASH2P; -.
H-InvDB; HIX0000004; -.
H-InvDB; HIX0023492; -.
H-InvDB; HIX0094926; -.
H-InvDB; HIX0195874; -.
HGNC; HGNC:33145; WASH2P.
HPA; HPA002689; -.
neXtProt; NX_Q6VEQ5; -.
eggNOG; ENOG410IFZ4; Eukaryota.
eggNOG; ENOG410YN2V; LUCA.
HOGENOM; HOG000007381; -.
HOVERGEN; HBG066686; -.
InParanoid; Q6VEQ5; -.
PhylomeDB; Q6VEQ5; -.
PRO; PR:Q6VEQ5; -.
Proteomes; UP000005640; Unplaced.
GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
InterPro; IPR028290; WASH1.
InterPro; IPR021854; WASH1_WAHD.
InterPro; IPR003124; WH2_dom.
PANTHER; PTHR23331; PTHR23331; 1.
Pfam; PF11945; WASH_WAHD; 1.
PROSITE; PS51082; WH2; 1.
2: Evidence at transcript level;
Actin-binding; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Endosome; Isopeptide bond; Membrane; Protein transport;
Reference proteome; Transport; Ubl conjugation.
CHAIN 1 465 WAS protein family homolog 2.
/FTId=PRO_0000257971.
DOMAIN 361 383 WH2. {ECO:0000255|PROSITE-
ProRule:PRU00406}.
REGION 1 167 WHD1.
REGION 1 54 Required for WASH complex assembly.
{ECO:0000250|UniProtKB:C4AMC7}.
REGION 349 465 VCA. {ECO:0000250|UniProtKB:C4AMC7}.
COMPBIAS 268 330 Pro-rich.
COMPBIAS 340 347 Poly-Ser.
CROSSLNK 220 220 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:A8K0Z3}.
SEQUENCE 465 AA; 50312 MW; 54FD1BB405E391DF CRC64;
MTPVRMQHSL AGQTYAVPLI QPDLRREEAV QQMADALQYL QKVSGDIFSR ISQQVEQSRS
QVQAIGEKVS LAQAKIEKIK GSKKAIKVFS SAKYPAPERL QEYGSIFTGA QDPGLQRRPR
HRIQSKHRPL DERALQEKLK DFPVCVSTKP EPEDDAEEGL GGLPSNISSV SSLLLFNTTE
NLYKKYVFLD PLAGAVTKTH VMLGAETEEK LFDAPLSISK REQLEQQVPE NYFYVPDLGQ
VPEIDVPSYL PDLPGIANDL MYIADLGPGI APSAPGTIPE LPTFHTEVAE PLKVDLQDGV
LTPPPPPPPP PPAPEVLASA PPLPPSTAAP VGQGARQDDS SSSASPSVQG APREVVDPSG
GRATLLESIR QAGGIGKAKL RSMKERKLEK KKQKEQEQVR ATSQGGHLMS DLFNKLVMRR
KGISGKGPGA GEGPGGAFAR VSDSIPPLPP PQQPQAEEDE DDWES


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