WASC5_MOUSE
ID WASC5_MOUSE Reviewed; 1159 AA.
AC Q8C2E7; Q8BGY1; Q8K2J2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=WASH complex subunit 5 {ECO:0000312|MGI:MGI:2146110};
DE AltName: Full=WASH complex subunit strumpellin {ECO:0000305};
GN Name=Washc5 {ECO:0000312|MGI:MGI:2146110}; Synonyms=Kiaa0196;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Colon;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 633-1159.
RC STRAIN=NOD; TISSUE=Thymus;
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 681-1159.
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 [4]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP FUNCTION.
RX PubMed=24998208; DOI=10.1038/srep05596;
RA Wang F., Zhang L., Zhang G.L., Wang Z.B., Cui X.S., Kim N.H., Sun S.C.;
RT "WASH complex regulates Arp2/3 complex for actin-based polar body extrusion
RT in mouse oocytes.";
RL Sci. Rep. 4:5596-5596(2014).
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. May be involved in
CC axonal outgrowth. Involved in cellular localization of ADRB2. Involved
CC in cellular trafficking of BLOC-1 complex cargos such as ATP7A and
CC VAMP7 (By similarity). Involved in cytokinesis and following polar body
CC extrusion during oocyte meiotic maturation (PubMed:24998208).
CC {ECO:0000250|UniProtKB:Q12768, ECO:0000269|PubMed:24998208}.
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 Interacts with VCP, PI4K2A (By similarity).
CC {ECO:0000250|UniProtKB:Q12768}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q12768}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q12768}. Early endosome
CC {ECO:0000250|UniProtKB:Q12768}. Note=Colocalizes with SYP/synaptophysin
CC in the external molecular layer of the dentate gyrus and in motoneurons
CC of the ventral horn of spinal cord. {ECO:0000250|UniProtKB:Q12768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C2E7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C2E7-2; Sequence=VSP_010323, VSP_010324;
CC -!- SIMILARITY: Belongs to the strumpellin family. {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; BC031364; AAH31364.1; -; mRNA.
DR EMBL; BC034070; AAH34070.1; -; mRNA.
DR EMBL; BC040815; AAH40815.1; -; mRNA.
DR EMBL; BC067035; AAH67035.1; -; mRNA.
DR EMBL; AK088754; BAC40548.1; -; mRNA.
DR EMBL; AK129086; BAC97896.2; -; Transcribed_RNA.
DR CCDS; CCDS37083.1; -. [Q8C2E7-1]
DR RefSeq; NP_705776.2; NM_153548.2. [Q8C2E7-1]
DR AlphaFoldDB; Q8C2E7; -.
DR SMR; Q8C2E7; -.
DR BioGRID; 230156; 7.
DR ComplexPortal; CPX-1177; WASH complex, variant WASHC1/WASHC2.
DR IntAct; Q8C2E7; 1.
DR MINT; Q8C2E7; -.
DR STRING; 10090.ENSMUSP00000022976; -.
DR iPTMnet; Q8C2E7; -.
DR PhosphoSitePlus; Q8C2E7; -.
DR SwissPalm; Q8C2E7; -.
DR EPD; Q8C2E7; -.
DR MaxQB; Q8C2E7; -.
DR PaxDb; Q8C2E7; -.
DR PeptideAtlas; Q8C2E7; -.
DR PRIDE; Q8C2E7; -.
DR ProteomicsDB; 299742; -. [Q8C2E7-1]
DR ProteomicsDB; 299743; -. [Q8C2E7-2]
DR Antibodypedia; 56103; 50 antibodies from 15 providers.
DR Ensembl; ENSMUST00000022976; ENSMUSP00000022976; ENSMUSG00000022350. [Q8C2E7-1]
DR Ensembl; ENSMUST00000227725; ENSMUSP00000154441; ENSMUSG00000022350. [Q8C2E7-2]
DR GeneID; 223593; -.
DR KEGG; mmu:223593; -.
DR UCSC; uc007vxs.1; mouse. [Q8C2E7-2]
DR UCSC; uc007vxt.1; mouse. [Q8C2E7-1]
DR CTD; 9897; -.
DR MGI; MGI:2146110; Washc5.
DR VEuPathDB; HostDB:ENSMUSG00000022350; -.
DR eggNOG; KOG3666; Eukaryota.
DR GeneTree; ENSGT00390000011137; -.
DR HOGENOM; CLU_004021_1_0_1; -.
DR InParanoid; Q8C2E7; -.
DR OMA; FQSIHHY; -.
DR OrthoDB; 88928at2759; -.
DR PhylomeDB; Q8C2E7; -.
DR TreeFam; TF314480; -.
DR BioGRID-ORCS; 223593; 12 hits in 71 CRISPR screens.
DR ChiTaRS; E430025E21Rik; mouse.
DR PRO; PR:Q8C2E7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8C2E7; protein.
DR Bgee; ENSMUSG00000022350; Expressed in endothelial cell of lymphatic vessel and 247 other tissues.
DR Genevisible; Q8C2E7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0071203; C:WASH complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; IMP:MGI.
DR GO; GO:0140285; P:endosome fission; ISO:MGI.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; ISO:MGI.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0090306; P:meiotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:MGI.
DR GO; GO:0043933; P:protein-containing complex organization; IMP:MGI.
DR GO; GO:0051125; P:regulation of actin nucleation; IMP:MGI.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IC:ComplexPortal.
DR GO; GO:0097494; P:regulation of vesicle size; IMP:MGI.
DR InterPro; IPR019393; WASH_strumpellin.
DR PANTHER; PTHR15691; PTHR15691; 1.
DR Pfam; PF10266; Strumpellin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Endosome;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1159
FT /note="WASH complex subunit 5"
FT /id="PRO_0000050734"
FT VAR_SEQ 1..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010323"
FT VAR_SEQ 451..469
FT /note="TELADVFSGVKPLTRVEKN -> MAEPVWRCGCKASGQEEEL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010324"
FT CONFLICT 682
FT /note="I -> T (in Ref. 2; BAC40548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1159 AA; 134110 MW; F7E7B5A60340E1BF CRC64;
MLDFLAENNL CGQAILRIVS CGNAIIAEVL RLSEFIPAVF LLKDRADQQR YGDIIFDFSY
FKGPEFWESK LEAKPELQDL DEEFRENNIE IVTRFYLAFQ SVHKYIVDLN RYLDDLNEGV
YIQQTLETVL LSEDGKQLLC EALYLYGVML LVIDQKIEGE VRERMLVSYY RYSAARSSAD
SNMDDICKLL RSTGYSSQPG AKRPPNYPES YFQRVPINET FISMVIGRLR SDDIYNQVSA
YPLPEHRSTA LANQAAMLYV ILYFEPSILH THQAKMREIV DKYFPDNWVI SIYMGITVNL
ADAWEPYKAA KTALNNTLDL ANVKEQASRY ASVSDRVRAQ VQQFLKEGYL REEVLLDNIP
RLLNCLRDCN VAIRWLMLHT ADSACDPNNK RLRQIKDQIL ADSRYNPKIL FQLLLDTAQF
EFILKEMFKQ MLSEKQSKWE HYKKEGSERM TELADVFSGV KPLTRVEKNE NLQAWFREIS
KQILSLNYDD STAAGRKTVQ LIQALEEVQE FHQLESNLQV CQFLADTRKF LHQMIRTINI
KEEVLITVQI IGDLSFAWQL IDSFTSIMQE SIRVNPSMVT KLRATFLKLA SALDLPLLRI
NQANSPDLLS VSQYYSGELV SYVRKVLQII PESMFTSLLK IIKLQTHDIM EVPTRLDKDK
LRDYAQLGPR YEVAKLTHAI SIFTEGILMM KTTLVGIIKV DPKQLLEDGI RKELVKRVAF
ALHRGLIFNP RAKPSELMPK LKELGATMDG FHRSFEYIQD YVSIYGLKIW QEEVSRIINY
NVEQECNNFL RTKIQDWQSM YQSTHIPIPK FAPVDESITF IGRLCREILR ITDPKMTCYI
DQLNTWYDVK THQEVTSSRL FSEIQTTLGT FGLNGLDRLL CFMIVKELQN FLSMFQKIIL
KERTVQETLK MLMSAVNPLK SIVANSSKVY LSAITKTQKI WSAYLEAIMK VGQMQILRQQ
IANELNSSCR FDSRHLAAAL DNLNKALLAD IEAHYRDPSL PYPKEDNTLL YEITAYLEAA
GIHNPLNKIY ITTKRLPYFP IVNFLFLIAQ LPKLQYNKNL GMVCRKPADP VDWPPLVLGL
LTLLKQFHSR YTEQFLALIG QFIRSTMEQC TSQKMPEMPA DAVGALLFLE DYVRYTKLPR
RVAEAHVPNF IFDEFRTVL
