WASC4_MOUSE
ID WASC4_MOUSE Reviewed; 1173 AA.
AC Q3UMB9; Q3TTQ9; Q6ZPZ7; Q8CAK8; Q8CGK0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=WASH complex subunit 4 {ECO:0000312|MGI:MGI:2441787};
DE AltName: Full=WASH complex subunit SWIP {ECO:0000305};
GN Name=Washc4 {ECO:0000312|MGI:MGI:2441787};
GN Synonyms=Kiaa1033 {ECO:0000312|MGI:MGI:2441787};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1145 AND 818-1173.
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, Mammary gland, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1145.
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-1173.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP FUNCTION OF THE WASH COMPLEX.
RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT "The Arp2/3 activator WASH controls the fission of endosomes through a
RT large multiprotein complex.";
RL Dev. Cell 17:712-723(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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:0000305|PubMed:19922875}.
CC -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or WASH3P),
CC WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5. The WASH core
CC complex associates via WASHC2 with the F-actin-capping protein dimer
CC (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or
CC substoichiometric manner which was initially described as WASH complex
CC (By similarity). {ECO:0000250|UniProtKB:Q2M389}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q2M389}.
CC -!- SIMILARITY: Belongs to the SWIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20314.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH20314.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAE36266.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC153508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK038582; BAC30055.1; -; mRNA.
DR EMBL; AK145000; BAE26179.1; -; mRNA.
DR EMBL; AK161247; BAE36266.1; ALT_INIT; mRNA.
DR EMBL; AK166233; BAE38648.1; -; mRNA.
DR EMBL; BC020314; AAH20314.1; ALT_SEQ; mRNA.
DR EMBL; AK129269; BAC98079.1; -; mRNA.
DR CCDS; CCDS36015.1; -.
DR RefSeq; NP_001028547.2; NM_001033375.2.
DR AlphaFoldDB; Q3UMB9; -.
DR BioGRID; 235172; 4.
DR ComplexPortal; CPX-1177; WASH complex, variant WASHC1/WASHC2.
DR STRING; 10090.ENSMUSP00000039322; -.
DR iPTMnet; Q3UMB9; -.
DR PhosphoSitePlus; Q3UMB9; -.
DR SwissPalm; Q3UMB9; -.
DR EPD; Q3UMB9; -.
DR MaxQB; Q3UMB9; -.
DR PaxDb; Q3UMB9; -.
DR PeptideAtlas; Q3UMB9; -.
DR PRIDE; Q3UMB9; -.
DR ProteomicsDB; 297842; -.
DR Antibodypedia; 56699; 41 antibodies from 15 providers.
DR Ensembl; ENSMUST00000038388; ENSMUSP00000039322; ENSMUSG00000034560.
DR GeneID; 319277; -.
DR KEGG; mmu:319277; -.
DR UCSC; uc007gkj.1; mouse.
DR CTD; 23325; -.
DR MGI; MGI:2441787; Washc4.
DR VEuPathDB; HostDB:ENSMUSG00000034560; -.
DR eggNOG; KOG3578; Eukaryota.
DR GeneTree; ENSGT00390000002524; -.
DR HOGENOM; CLU_002451_0_0_1; -.
DR InParanoid; Q3UMB9; -.
DR OMA; QFLFDEH; -.
DR OrthoDB; 186054at2759; -.
DR PhylomeDB; Q3UMB9; -.
DR TreeFam; TF324604; -.
DR BioGRID-ORCS; 319277; 11 hits in 71 CRISPR screens.
DR PRO; PR:Q3UMB9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3UMB9; protein.
DR Bgee; ENSMUSG00000034560; Expressed in uterus and 63 other tissues.
DR ExpressionAtlas; Q3UMB9; baseline and differential.
DR Genevisible; Q3UMB9; MM.
DR GO; GO:0031083; C:BLOC-1 complex; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0071203; C:WASH complex; IDA:MGI.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IC:ComplexPortal.
DR InterPro; IPR028191; WASH-4_N.
DR InterPro; IPR028283; WASH-7_C.
DR InterPro; IPR028282; WASH-7_central.
DR InterPro; IPR027307; WASH7.
DR PANTHER; PTHR31409; PTHR31409; 1.
DR Pfam; PF14746; WASH-7_C; 1.
DR Pfam; PF14744; WASH-7_mid; 1.
DR Pfam; PF14745; WASH-7_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Endosome; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q2M389"
FT CHAIN 2..1173
FT /note="WASH complex subunit 4"
FT /id="PRO_0000282576"
FT REGION 705..1173
FT /note="Sufficient for interaction with WASHC5"
FT /evidence="ECO:0000250|UniProtKB:Q2M389"
FT REGION 1141..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..56
FT /evidence="ECO:0000255"
FT COMPBIAS 1141..1158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q2M389"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M389"
FT MOD_RES 1154
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2M389"
SQ SEQUENCE 1173 AA; 136370 MW; B4473C932FAE26AF CRC64;
MAVDTLSPDW DFDRVDDGSQ KIHAEVQLKN YGRFLEEYTS QLRRIEDALD DLIGDVWDFN
LDPIALKLLP YEQSSLLELI KTENKVLNKV ITVYAALCCE IKKLKYEAET KFYNGLLFYG
EGATDSSMVE GDCQIQMGRF VSFLQELSCF VTRCYEVVMN VIHQLAALYI SNKIGPKIIE
TTGVHFQTMY EHLGELLTVL LTLDEIVDNH VTLKDHWTMY KRLLKSVHHN PSKFGIQEEK
LKPFEKFLLK LEGQLLDGMI FQACIEQQFD SLNGGISVSK NSTFAEEFAH SIRSIFANVE
AKLGEPSEID QRDKYVGICG LFVLHFQIFR TVDKKFYKSL LDICKKVPAI TLTANIIWFP
DNFLIHKMPA AAKLLDRKSL QAIKIHRDTF LQQKAQSLNK DVQSYYVFVS SWMMKMESML
SKEQRMDTFA EDLTNRCNVF IQGFLYAYSI STIIKTTMNL YMSMQKPMTK TSVKALCRLI
ELLKAIEHMF YRRSMVVADS VSHITQHLQH QALSSISVAK KRVISDKKYS EQRLDVLSAL
VLAENTLNGP STKQRRLIVS LALSVGTQMK TFKDEELFPL QVVMKKLDLI SELRERVQAQ
CDCCFLYWHR AVFPIYLDDV YENAVDAARL HYMFSALRDC VPAMMHSRHL ESHELLLDCY
DKEIMDILNE HLLDKLCKEI EKDLRLSVHT HLKLDDRNPF KVGRKDLALF FSLNPIRFFN
RFIDIRAYVT HYLDKTFYNL TTVALHDWAT YSEMRNLATQ RYGLVMTEAH LPSQTLEQGL
DVLEIMRNIH IFVSRYLYNL NNQIFIERTS NNKHLNTINI RHIANSIRTH GTGIMNTTVN
FTYQFLKKKF YIFSQFMYDE HIKSRLIKDI RFFREIKDQN DHKYPFDRAE KFNRGIRKLG
ITPEGQSYLD QFRQLISQIG NAMGYIRMIR SGGLHCSSNA IRFVPDLEDI VSFEELVKEE
GLAEETLRAA RHLDSVLSDH TRNSAEGTEY FKMLVDVFAP EFRRPKNIHL RNFYIIVPPL
TLNFVEHSIS CKEKLNKKNK LGAAFTDDGF AMGVAYTLKL LDQYQEFDSL HWFQSVREKY
IKEIRAVAKQ QNVQSTSQDE KLLQTMNLTQ KRLEVYLQEF ELLYFSLSSA RIFFRADKTA
AEENQEKKEK EEETKTSNGD GPESTVSADP VVK
