ID   WASC5_HUMAN             Reviewed;        1159 AA.
AC   Q12768; A8K4R7; Q3KQX5; Q8TBQ2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=WASH complex subunit 5 {ECO:0000312|HGNC:HGNC:28984};
DE   AltName: Full=Strumpellin;
DE   AltName: Full=WASH complex subunit strumpellin {ECO:0000305};
GN   Name=WASHC5 {ECO:0000312|HGNC:HGNC:28984}; Synonyms=KIAA0196;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA   Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. V. The
RT   coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 3:17-24(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [6]
RP   FUNCTION OF THE WASH COMPLEX, AND IDENTIFICATION IN 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   [7]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH VCP, FUNCTION,
RP   AND CHARACTERIZATION OF VARIANT SPG8 ASP-471.
RX   PubMed=20833645; DOI=10.1093/brain/awq222;
RA   Clemen C.S., Tangavelou K., Strucksberg K.H., Just S., Gaertner L.,
RA   Regus-Leidig H., Stumpf M., Reimann J., Coras R., Morgan R.O.,
RA   Fernandez M.P., Hofmann A., Muller S., Schoser B., Hanisch F.G.,
RA   Rottbauer W., Blumcke I., von Horsten S., Eichinger L., Schroder R.;
RT   "Strumpellin is a novel valosin-containing protein binding partner linking
RT   hereditary spastic paraplegia to protein aggregation diseases.";
RL   Brain 133:2920-2941(2010).
RN   [8]
RP   IDENTIFICATION IN THE WASH CORE COMPLEX, AND FUNCTION OF THE WASH CORE
RP   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).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS SPG8
RP   ASP-471; PHE-619 AND PHE-626.
RX   PubMed=23085491; DOI=10.1016/j.bbadis.2012.10.011;
RA   Freeman C., Seaman M.N., Reid E.;
RT   "The hereditary spastic paraplegia protein strumpellin: characterisation in
RT   neurons and of the effect of disease mutations on WASH complex assembly and
RT   function.";
RL   Biochim. Biophys. Acta 1832:160-173(2013).
RN   [11]
RP   INVOLVEMENT IN RTSC1.
RX   PubMed=24065355; DOI=10.1136/jmedgenet-2013-101715;
RA   Elliott A.M., Simard L.R., Coghlan G., Chudley A.E., Chodirker B.N.,
RA   Greenberg C.R., Burch T., Ly V., Hatch G.M., Zelinski T.;
RT   "A novel mutation in KIAA0196: identification of a gene involved in
RT   Ritscher-Schinzel/3C syndrome in a First Nations cohort.";
RL   J. Med. Genet. 50:819-822(2013).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PI4K2A.
RX   PubMed=23676666; DOI=10.1091/mbc.e13-02-0088;
RA   Ryder P.V., Vistein R., Gokhale A., Seaman M.N., Puthenveedu M.A.,
RA   Faundez V.;
RT   "The WASH complex, an endosomal Arp2/3 activator, interacts with the
RT   Hermansky-Pudlak syndrome complex BLOC-1 and its cargo
RT   phosphatidylinositol-4-kinase type IIalpha.";
RL   Mol. Biol. Cell 24:2269-2284(2013).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [15]
RP   VARIANTS SPG8 ASP-471; PHE-619 AND PHE-626, AND CHARACTERIZATION OF
RP   VARIANTS SPG8 PHE-619 AND PHE-626.
RX   PubMed=17160902; DOI=10.1086/510782;
RA   Valdmanis P.N., Meijer I.A., Reynolds A., Lei A., MacLeod P.,
RA   Schlesinger D., Zatz M., Reid E., Dion P.A., Drapeau P., Rouleau G.A.;
RT   "Mutations in the KIAA0196 gene at the SPG8 locus cause hereditary spastic
RT   paraplegia.";
RL   Am. J. Hum. Genet. 80:152-161(2007).
RN   [16]
RP   VARIANT SPG8 THR-226.
RX   PubMed=23881105; DOI=10.1007/s00415-013-7044-6;
RA   Bettencourt C., Morris H.R., Singleton A.B., Hardy J., Houlden H.;
RT   "Exome sequencing expands the mutational spectrum of SPG8 in a family with
RT   spasticity responsive to L-DOPA treatment.";
RL   J. Neurol. 260:2414-2416(2013).
RN   [17]
RP   VARIANT SPG8 ALA-696.
RX   PubMed=23455931; DOI=10.1007/s00415-013-6870-x;
RA   de Bot S.T., Vermeer S., Buijsman W., Heister A., Voorendt M., Verrips A.,
RA   Scheffer H., Kremer H.P., van de Warrenburg B.P., Kamsteeg E.J.;
RT   "Pure adult-onset Spastic Paraplegia caused by a novel mutation in the
RT   KIAA0196 (SPG8) gene.";
RL   J. Neurol. 260:1765-1769(2013).
RN   [18]
RP   VARIANT SPG8 ALA-620.
RX   PubMed=25454649; DOI=10.1016/j.jns.2014.10.018;
RA   Jahic A., Kreuz F., Zacher P., Fiedler J., Bier A., Reif S., Rieger M.,
RA   Krueger S., Beetz C., Plaschke J.;
RT   "A novel strumpellin mutation and potential pitfalls in the molecular
RT   diagnosis of hereditary spastic paraplegia type SPG8.";
RL   J. Neurol. Sci. 347:372-374(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 (PubMed:19922875,
CC       PubMed:20498093). May be involved in axonal outgrowth. Involved in
CC       cellular localization of ADRB2 (PubMed:23085491). Involved in cellular
CC       trafficking of BLOC-1 complex cargos such as ATP7A and VAMP7
CC       (PubMed:23676666). {ECO:0000269|PubMed:19922875,
CC       ECO:0000269|PubMed:20833645, ECO:0000269|PubMed:23085491,
CC       ECO:0000269|PubMed:23676666}.
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. {ECO:0000269|PubMed:19922875,
CC       ECO:0000269|PubMed:20498093, ECO:0000269|PubMed:20833645,
CC       ECO:0000269|PubMed:23676666}.
CC   -!- INTERACTION:
CC       Q12768; Q13596: SNX1; NbExp=2; IntAct=EBI-2563794, EBI-2822329;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20833645}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:20833645}. Early endosome
CC       {ECO:0000269|PubMed:23085491, ECO:0000269|PubMed:23676666}.
CC       Note=Colocalizes with SYP/synaptophysin in the external molecular layer
CC       of the dentate gyrus and in motoneurons of the ventral horn of spinal
CC       cord. {ECO:0000269|PubMed:20833645}.
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC       {ECO:0000269|PubMed:20833645}.
CC   -!- DISEASE: Spastic paraplegia 8, autosomal dominant (SPG8) [MIM:603563]:
CC       A form of spastic paraplegia, a neurodegenerative disorder
CC       characterized by a slow, gradual, progressive weakness and spasticity
CC       of the lower limbs. Rate of progression and the severity of symptoms
CC       are quite variable. Initial symptoms may include difficulty with
CC       balance, weakness and stiffness in the legs, muscle spasms, and
CC       dragging the toes when walking. In some forms of the disorder, bladder
CC       symptoms (such as incontinence) may appear, or the weakness and
CC       stiffness may spread to other parts of the body.
CC       {ECO:0000269|PubMed:17160902, ECO:0000269|PubMed:20833645,
CC       ECO:0000269|PubMed:23085491, ECO:0000269|PubMed:23455931,
CC       ECO:0000269|PubMed:23881105, ECO:0000269|PubMed:25454649}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Ritscher-Schinzel syndrome 1 (RTSC1) [MIM:220210]: A
CC       developmental malformation syndrome characterized by craniofacial
CC       abnormalities, congenital heart defects, and cerebellar brain
CC       malformations. Facial features include prominent occiput, prominent
CC       forehead, low-set ears, downslanting palpebral fissures, depressed
CC       nasal bridge, and micrognathia. Cardiac defects can include septal
CC       defects and aortic stenosis, among others, and brain imaging shows
CC       Dandy-Walker malformation, cerebellar vermis hypoplasia, posterior
CC       fossa cysts, and ventricular dilatation. Affected individuals have
CC       severe developmental delay. {ECO:0000269|PubMed:24065355}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the strumpellin family. {ECO:0000305}.
CC   -!- CAUTION: One study reported a nucleation-promoting factor (NPF)
CC       activity towards the Arp2/3 complex using partially purified samples of
CC       the WASH complex (PubMed:19922875). In another study, the in vitro
CC       reconstituted and purified recombinant WASH core complex, consisting of
CC       WASHC3, WASHC4, WASHC5, WASHC1 and the N-terminal residues 1-356 of
CC       WASHC2, did not show activity toward Arp2/3 complex (PubMed:20498093).
CC       {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA12109.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D83780; BAA12109.2; ALT_INIT; mRNA.
DR   EMBL; AK291032; BAF83721.1; -; mRNA.
DR   EMBL; CH471060; EAW92081.1; -; Genomic_DNA.
DR   EMBL; BC026951; AAH26951.1; -; mRNA.
DR   EMBL; BC106015; AAI06016.1; -; mRNA.
DR   CCDS; CCDS6355.1; -.
DR   RefSeq; NP_055661.3; NM_014846.3.
DR   RefSeq; XP_016869602.1; XM_017014113.1.
DR   AlphaFoldDB; Q12768; -.
DR   SMR; Q12768; -.
DR   BioGRID; 115226; 114.
DR   ComplexPortal; CPX-1163; WASH complex, variant WASHC1/WASHC2C.
DR   ComplexPortal; CPX-1168; WASH complex, variant WASH2P/WASHC2C.
DR   ComplexPortal; CPX-1169; WASH complex, variant WASH3P/WASHC2C.
DR   ComplexPortal; CPX-1170; WASH complex, variant WASH4P/WASHC2C.
DR   ComplexPortal; CPX-1171; WASH complex, variant WASH6P/WASHC2C.
DR   ComplexPortal; CPX-1172; WASH complex, variant WASHC1/WASHC2A.
DR   ComplexPortal; CPX-1173; WASH complex, variant WASH2P/WASHC2A.
DR   ComplexPortal; CPX-1174; WASH complex, variant WASH3P/WASHC2A.
DR   ComplexPortal; CPX-1175; WASH complex, variant WASH4P/WASHC2A.
DR   ComplexPortal; CPX-1176; WASH complex, variant WASH6P/WASHC2A.
DR   CORUM; Q12768; -.
DR   IntAct; Q12768; 37.
DR   MINT; Q12768; -.
DR   STRING; 9606.ENSP00000318016; -.
DR   GlyGen; Q12768; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q12768; -.
DR   MetOSite; Q12768; -.
DR   PhosphoSitePlus; Q12768; -.
DR   SwissPalm; Q12768; -.
DR   BioMuta; WASHC5; -.
DR   DMDM; 2495719; -.
DR   EPD; Q12768; -.
DR   jPOST; Q12768; -.
DR   MassIVE; Q12768; -.
DR   MaxQB; Q12768; -.
DR   PaxDb; 9606-ENSP00000318016; -.
DR   PeptideAtlas; Q12768; -.
DR   ProteomicsDB; 58911; -.
DR   Pumba; Q12768; -.
DR   Antibodypedia; 56103; 62 antibodies from 17 providers.
DR   DNASU; 9897; -.
DR   Ensembl; ENST00000318410.12; ENSP00000318016.7; ENSG00000164961.16.
DR   GeneID; 9897; -.
DR   KEGG; hsa:9897; -.
DR   MANE-Select; ENST00000318410.12; ENSP00000318016.7; NM_014846.4; NP_055661.3.
DR   UCSC; uc003yrt.4; human.
DR   AGR; HGNC:28984; -.
DR   CTD; 9897; -.
DR   DisGeNET; 9897; -.
DR   GeneCards; WASHC5; -.
DR   GeneReviews; WASHC5; -.
DR   HGNC; HGNC:28984; WASHC5.
DR   HPA; ENSG00000164961; Low tissue specificity.
DR   MalaCards; WASHC5; -.
DR   MIM; 220210; phenotype.
DR   MIM; 603563; phenotype.
DR   MIM; 610657; gene.
DR   neXtProt; NX_Q12768; -.
DR   OpenTargets; ENSG00000164961; -.
DR   Orphanet; 7; 3C syndrome.
DR   Orphanet; 100989; Autosomal dominant spastic paraplegia type 8.
DR   PharmGKB; PA142671624; -.
DR   VEuPathDB; HostDB:ENSG00000164961; -.
DR   eggNOG; KOG3666; Eukaryota.
DR   GeneTree; ENSGT00390000011137; -.
DR   HOGENOM; CLU_004021_1_0_1; -.
DR   InParanoid; Q12768; -.
DR   OMA; FFPDNWV; -.
DR   OrthoDB; 295709at2759; -.
DR   PhylomeDB; Q12768; -.
DR   TreeFam; TF314480; -.
DR   PathwayCommons; Q12768; -.
DR   SignaLink; Q12768; -.
DR   SIGNOR; Q12768; -.
DR   BioGRID-ORCS; 9897; 66 hits in 1157 CRISPR screens.
DR   ChiTaRS; WASHC5; human.
DR   GeneWiki; KIAA0196; -.
DR   GenomeRNAi; 9897; -.
DR   Pharos; Q12768; Tbio.
DR   PRO; PR:Q12768; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q12768; Protein.
DR   Bgee; ENSG00000164961; Expressed in corpus callosum and 194 other cell types or tissues.
DR   ExpressionAtlas; Q12768; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; NAS:ComplexPortal.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR   GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR   GO; GO:0016197; P:endosomal transport; NAS:ComplexPortal.
DR   GO; GO:0140285; P:endosome fission; IBA:GO_Central.
DR   GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR   GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR   GO; GO:0090306; P:meiotic spindle assembly; IEA:Ensembl.
DR   GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
DR   GO; GO:0040038; P:polar body extrusion after meiotic divisions; IEA:Ensembl.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0031503; P:protein-containing complex localization; IEA:Ensembl.
DR   GO; GO:0051125; P:regulation of actin nucleation; IBA:GO_Central.
DR   GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; NAS:ComplexPortal.
DR   GO; GO:0097494; P:regulation of vesicle size; IEA:Ensembl.
DR   InterPro; IPR019393; WASH_strumpellin.
DR   PANTHER; PTHR15691; WASH COMPLEX SUBUNIT 5; 1.
DR   PANTHER; PTHR15691:SF6; WASH COMPLEX SUBUNIT 5; 1.
DR   Pfam; PF10266; Strumpellin; 1.
DR   Genevisible; Q12768; HS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Disease variant; Endoplasmic reticulum; Endosome;
KW   Hereditary spastic paraplegia; Intellectual disability; Neurodegeneration;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1159
FT                   /note="WASH complex subunit 5"
FT                   /id="PRO_0000050733"
FT   MOD_RES         917
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         226
FT                   /note="I -> T (in SPG8; dopamine responsive spasticity;
FT                   dbSNP:rs755285830)"
FT                   /evidence="ECO:0000269|PubMed:23881105"
FT                   /id="VAR_069984"
FT   VARIANT         471
FT                   /note="N -> D (in SPG8; does not alter subcellular
FT                   distribution; no effect on its binding to VCP; no effect on
FT                   assembly in the WASH complex; dbSNP:rs80338865)"
FT                   /evidence="ECO:0000269|PubMed:17160902,
FT                   ECO:0000269|PubMed:23085491"
FT                   /id="VAR_031955"
FT   VARIANT         619
FT                   /note="L -> F (in SPG8; fails to rescue the curly phenotype
FT                   in a zebrafish model; no effect on assembly in the WASH
FT                   complex; dbSNP:rs80338866)"
FT                   /evidence="ECO:0000269|PubMed:17160902,
FT                   ECO:0000269|PubMed:23085491"
FT                   /id="VAR_031956"
FT   VARIANT         620
FT                   /note="V -> A (in SPG8)"
FT                   /evidence="ECO:0000269|PubMed:25454649"
FT                   /id="VAR_072417"
FT   VARIANT         626
FT                   /note="V -> F (in SPG8; fails to rescue the curly phenotype
FT                   in a zebrafish model; no effect on assembly in the WASH
FT                   complex; dbSNP:rs80338867)"
FT                   /evidence="ECO:0000269|PubMed:17160902,
FT                   ECO:0000269|PubMed:23085491"
FT                   /id="VAR_031957"
FT   VARIANT         696
FT                   /note="G -> A (in SPG8; dbSNP:rs397515564)"
FT                   /evidence="ECO:0000269|PubMed:23455931"
FT                   /id="VAR_069985"
FT   CONFLICT        229
FT                   /note="L -> R (in Ref. 4; AAH26951)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1159 AA;  134286 MW;  D6156D359981FC5F CRC64;
     MLDFLAENNL CGQAILRIVS CGNAIIAELL RLSEFIPAVF RLKDRADQQK YGDIIFDFSY
     FKGPELWESK LDAKPELQDL DEEFRENNIE IVTRFYLAFQ SVHKYIVDLN RYLDDLNEGV
     YIQQTLETVL LNEDGKQLLC EALYLYGVML LVIDQKIEGE VRERMLVSYY RYSAARSSAD
     SNMDDICKLL RSTGYSSQPG AKRPSNYPES YFQRVPINES FISMVIGRLR SDDIYNQVSA
     YPLPEHRSTA LANQAAMLYV ILYFEPSILH THQAKMREIV DKYFPDNWVI SIYMGITVNL
     VDAWEPYKAA KTALNNTLDL SNVREQASRY ATVSERVHAQ VQQFLKEGYL REEMVLDNIP
     KLLNCLRDCN VAIRWLMLHT ADSACDPNNK RLRQIKDQIL TDSRYNPRIL FQLLLDTAQF
     EFILKEMFKQ MLSEKQTKWE HYKKEGSERM TELADVFSGV KPLTRVEKNE NLQAWFREIS
     KQILSLNYDD STAAGRKTVQ LIQALEEVQE FHQLESNLQV CQFLADTRKF LHQMIRTINI
     KEEVLITMQI VGDLSFAWQL IDSFTSIMQE SIRVNPSMVT KLRATFLKLA SALDLPLLRI
     NQANSPDLLS VSQYYSGELV SYVRKVLQII PESMFTSLLK IIKLQTHDII EVPTRLDKDK
     LRDYAQLGPR YEVAKLTHAI SIFTEGILMM KTTLVGIIKV DPKQLLEDGI RKELVKRVAF
     ALHRGLIFNP RAKPSELMPK LKELGATMDG FHRSFEYIQD YVNIYGLKIW QEEVSRIINY
     NVEQECNNFL RTKIQDWQSM YQSTHIPIPK FTPVDESVTF IGRLCREILR ITDPKMTCHI
     DQLNTWYDMK THQEVTSSRL FSEIQTTLGT FGLNGLDRLL CFMIVKELQN FLSMFQKIIL
     RDRTVQDTLK TLMNAVSPLK SIVANSNKIY FSAIAKTQKI WTAYLEAIMK VGQMQILRQQ
     IANELNYSCR FDSKHLAAAL ENLNKALLAD IEAHYQDPSL PYPKEDNTLL YEITAYLEAA
     GIHNPLNKIY ITTKRLPYFP IVNFLFLIAQ LPKLQYNKNL GMVCRKPTDP VDWPPLVLGL
     LTLLKQFHSR YTEQFLALIG QFICSTVEQC TSQKIPEIPA DVVGALLFLE DYVRYTKLPR
     RVAEAHVPNF IFDEFRTVL
//