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WASH complex subunit 5 (WASH complex subunit strumpellin)

 WASC5_MOUSE             Reviewed;        1159 AA.
Q8C2E7; Q8BGY1; Q8K2J2;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
20-JUN-2018, entry version 103.
RecName: Full=WASH complex subunit 5 {ECO:0000312|MGI:MGI:2146110};
AltName: Full=WASH complex subunit strumpellin {ECO:0000305};
Name=Washc5 {ECO:0000312|MGI:MGI:2146110}; Synonyms=Kiaa0196;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Brain, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 633-1159.
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 681-1159.
TISSUE=Brain;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[4]
SEQUENCE REVISION.
Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION.
PubMed=24998208; DOI=10.1038/srep05596;
Wang F., Zhang L., Zhang G.L., Wang Z.B., Cui X.S., Kim N.H.,
Sun S.C.;
"WASH complex regulates Arp2/3 complex for actin-based polar body
extrusion in mouse oocytes.";
Sci. Rep. 4:5596-5596(2014).
-!- FUNCTION: Acts at least in part as component of the WASH core
complex whose assembly at the surface of endosomes seems to
inhibit WASH nucleation-promoting factor (NPF) activity in
recruiting and activating the Arp2/3 complex to induce actin
polymerization, and which is involved in regulation of the fission
of tubules that serve as transport intermediates during endosome
sorting. May be involved in axonal outgrowth. Involved in cellular
localization of ADRB2. Involved in cellular trafficking of BLOC-1
complex cargos such as ATP7A and VAMP7 (By similarity). Involved
in cytokinesis and following polar body extrusion during oocyte
meiotic maturation (PubMed:24998208).
{ECO:0000250|UniProtKB:Q12768, ECO:0000269|PubMed:24998208}.
-!- 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 via WASHC2 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 with VCP, PI4K2A
(By similarity). {ECO:0000250|UniProtKB:Q12768}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q12768}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q12768}. Early endosome
{ECO:0000250|UniProtKB:Q12768}. Note=Colocalizes with
SYP/synaptophysin in the external molecular layer of the dentate
gyrus and in motoneurons of the ventral horn of spinal cord.
{ECO:0000250|UniProtKB:Q12768}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8C2E7-1; Sequence=Displayed;
Name=2;
IsoId=Q8C2E7-2; Sequence=VSP_010323, VSP_010324;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the strumpellin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC031364; AAH31364.1; -; mRNA.
EMBL; BC034070; AAH34070.1; -; mRNA.
EMBL; BC040815; AAH40815.1; -; mRNA.
EMBL; BC067035; AAH67035.1; -; mRNA.
EMBL; AK088754; BAC40548.1; -; mRNA.
EMBL; AK129086; BAC97896.2; -; Transcribed_RNA.
CCDS; CCDS37083.1; -. [Q8C2E7-1]
RefSeq; NP_705776.2; NM_153548.2. [Q8C2E7-1]
UniGene; Mm.218665; -.
BioGrid; 230156; 1.
ComplexPortal; CPX-1177; WASH complex, variant WASHC1/WASHC2.
STRING; 10090.ENSMUSP00000022976; -.
iPTMnet; Q8C2E7; -.
PhosphoSitePlus; Q8C2E7; -.
EPD; Q8C2E7; -.
PaxDb; Q8C2E7; -.
PeptideAtlas; Q8C2E7; -.
PRIDE; Q8C2E7; -.
Ensembl; ENSMUST00000022976; ENSMUSP00000022976; ENSMUSG00000022350. [Q8C2E7-1]
Ensembl; ENSMUST00000227725; ENSMUSP00000154441; ENSMUSG00000022350. [Q8C2E7-2]
GeneID; 223593; -.
KEGG; mmu:223593; -.
UCSC; uc007vxs.1; mouse. [Q8C2E7-2]
UCSC; uc007vxt.1; mouse. [Q8C2E7-1]
CTD; 9897; -.
MGI; MGI:2146110; Washc5.
eggNOG; KOG3666; Eukaryota.
eggNOG; ENOG410XNSS; LUCA.
GeneTree; ENSGT00390000011137; -.
HOGENOM; HOG000258245; -.
HOVERGEN; HBG102793; -.
InParanoid; Q8C2E7; -.
KO; K18464; -.
OMA; CRKPADP; -.
OrthoDB; EOG091G02GF; -.
PhylomeDB; Q8C2E7; -.
TreeFam; TF314480; -.
ChiTaRS; E430025E21Rik; mouse.
PRO; PR:Q8C2E7; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022350; -.
CleanEx; MM_E430025E21RIK; -.
Genevisible; Q8C2E7; MM.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
GO; GO:0016197; P:endosomal transport; IMP:MGI.
GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0090306; P:spindle assembly involved in meiosis; IMP:UniProtKB.
InterPro; IPR019393; WASH_strumpellin.
PANTHER; PTHR15691; PTHR15691; 1.
Pfam; PF10266; Strumpellin; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Endosome; Protein transport;
Reference proteome; Transport.
CHAIN 1 1159 WASH complex subunit 5.
/FTId=PRO_0000050734.
VAR_SEQ 1 450 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010323.
VAR_SEQ 451 469 TELADVFSGVKPLTRVEKN -> MAEPVWRCGCKASGQEEE
L (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010324.
CONFLICT 682 682 I -> T (in Ref. 2; BAC40548).
{ECO:0000305}.
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


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