WASC3_HUMAN
ID WASC3_HUMAN Reviewed; 194 AA.
AC Q9Y3C0; B2RC74; Q53FF0; Q6IAI4; Q96QK0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=WASH complex subunit 3 {ECO:0000312|HGNC:HGNC:24256};
DE AltName: Full=Coiled-coil domain-containing protein 53;
GN Name=WASHC3 {ECO:0000312|HGNC:HGNC:24256};
GN ORFNames=AD-016, CCDC53, CGI-116, x0009;
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=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [8]
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 [9]
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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
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).
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:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093}.
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 {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093}.
CC -!- INTERACTION:
CC Q9Y3C0; Q9NYB9: ABI2; NbExp=4; IntAct=EBI-712969, EBI-743598;
CC Q9Y3C0; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-712969, EBI-11096309;
CC Q9Y3C0; Q13515: BFSP2; NbExp=3; IntAct=EBI-712969, EBI-10229433;
CC Q9Y3C0; Q6QNY1: BLOC1S2; NbExp=4; IntAct=EBI-712969, EBI-465872;
CC Q9Y3C0; Q9UL45: BLOC1S6; NbExp=8; IntAct=EBI-712969, EBI-465781;
CC Q9Y3C0; A1L168: C20orf202; NbExp=3; IntAct=EBI-712969, EBI-18396958;
CC Q9Y3C0; Q8NCU1: CCDC197; NbExp=7; IntAct=EBI-712969, EBI-750686;
CC Q9Y3C0; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-712969, EBI-10175300;
CC Q9Y3C0; Q9BS16: CENPK; NbExp=3; IntAct=EBI-712969, EBI-6871750;
CC Q9Y3C0; Q53EZ4: CEP55; NbExp=7; IntAct=EBI-712969, EBI-747776;
CC Q9Y3C0; Q9Y2V7: COG6; NbExp=4; IntAct=EBI-712969, EBI-3866319;
CC Q9Y3C0; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-712969, EBI-465804;
CC Q9Y3C0; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-712969, EBI-11427343;
CC Q9Y3C0; Q08379: GOLGA2; NbExp=6; IntAct=EBI-712969, EBI-618309;
CC Q9Y3C0; Q96CS2: HAUS1; NbExp=10; IntAct=EBI-712969, EBI-2514791;
CC Q9Y3C0; O75506: HSBP1; NbExp=13; IntAct=EBI-712969, EBI-748664;
CC Q9Y3C0; Q8IY31: IFT20; NbExp=4; IntAct=EBI-712969, EBI-744203;
CC Q9Y3C0; Q70UQ0-4: IKBIP; NbExp=4; IntAct=EBI-712969, EBI-12190633;
CC Q9Y3C0; Q2T9L4: INSYN1; NbExp=3; IntAct=EBI-712969, EBI-4311436;
CC Q9Y3C0; O60341: KDM1A; NbExp=3; IntAct=EBI-712969, EBI-710124;
CC Q9Y3C0; Q9Y448: KNSTRN; NbExp=6; IntAct=EBI-712969, EBI-373334;
CC Q9Y3C0; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-712969, EBI-3044087;
CC Q9Y3C0; Q3SY84: KRT71; NbExp=3; IntAct=EBI-712969, EBI-2952676;
CC Q9Y3C0; O95678: KRT75; NbExp=3; IntAct=EBI-712969, EBI-2949715;
CC Q9Y3C0; Q969G2: LHX4; NbExp=3; IntAct=EBI-712969, EBI-2865388;
CC Q9Y3C0; Q03252: LMNB2; NbExp=3; IntAct=EBI-712969, EBI-2830427;
CC Q9Y3C0; Q96EZ8: MCRS1; NbExp=13; IntAct=EBI-712969, EBI-348259;
CC Q9Y3C0; Q9H8S9: MOB1A; NbExp=3; IntAct=EBI-712969, EBI-748229;
CC Q9Y3C0; Q7L9L4: MOB1B; NbExp=3; IntAct=EBI-712969, EBI-2558745;
CC Q9Y3C0; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-712969, EBI-744402;
CC Q9Y3C0; O14777: NDC80; NbExp=10; IntAct=EBI-712969, EBI-715849;
CC Q9Y3C0; P37198: NUP62; NbExp=8; IntAct=EBI-712969, EBI-347978;
CC Q9Y3C0; Q96CV9: OPTN; NbExp=17; IntAct=EBI-712969, EBI-748974;
CC Q9Y3C0; P26367: PAX6; NbExp=3; IntAct=EBI-712969, EBI-747278;
CC Q9Y3C0; Q96AQ6: PBXIP1; NbExp=4; IntAct=EBI-712969, EBI-740845;
CC Q9Y3C0; Q15154: PCM1; NbExp=5; IntAct=EBI-712969, EBI-741421;
CC Q9Y3C0; Q15154-3: PCM1; NbExp=3; IntAct=EBI-712969, EBI-11742977;
CC Q9Y3C0; Q96FA3: PELI1; NbExp=3; IntAct=EBI-712969, EBI-448369;
CC Q9Y3C0; Q8TCD6: PHOSPHO2; NbExp=5; IntAct=EBI-712969, EBI-2861380;
CC Q9Y3C0; Q15276: RABEP1; NbExp=3; IntAct=EBI-712969, EBI-447043;
CC Q9Y3C0; O76064: RNF8; NbExp=3; IntAct=EBI-712969, EBI-373337;
CC Q9Y3C0; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-712969, EBI-12823227;
CC Q9Y3C0; O00560: SDCBP; NbExp=6; IntAct=EBI-712969, EBI-727004;
CC Q9Y3C0; O95295: SNAPIN; NbExp=3; IntAct=EBI-712969, EBI-296723;
CC Q9Y3C0; A0A286YEY3: SRGAP2B; NbExp=3; IntAct=EBI-712969, EBI-17766455;
CC Q9Y3C0; Q8N0S2: SYCE1; NbExp=4; IntAct=EBI-712969, EBI-6872807;
CC Q9Y3C0; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-712969, EBI-12833746;
CC Q9Y3C0; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-712969, EBI-1105213;
CC Q9Y3C0; P40222: TXLNA; NbExp=8; IntAct=EBI-712969, EBI-359793;
CC Q9Y3C0; Q8N3L3: TXLNB; NbExp=4; IntAct=EBI-712969, EBI-6116822;
CC Q9Y3C0; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-712969, EBI-2799833;
CC Q9Y3C0; A8K2R3; NbExp=3; IntAct=EBI-712969, EBI-9977437;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CCDC53 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}.
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DR EMBL; AF155655; AAF67012.1; -; mRNA.
DR EMBL; AF151874; AAD34111.1; -; mRNA.
DR EMBL; CR457171; CAG33452.1; -; mRNA.
DR EMBL; AK223339; BAD97059.1; -; mRNA.
DR EMBL; AK314970; BAG37471.1; -; mRNA.
DR EMBL; CH471054; EAW97687.1; -; Genomic_DNA.
DR EMBL; BC010889; AAH10889.1; -; mRNA.
DR CCDS; CCDS44959.1; -.
DR RefSeq; NP_057137.1; NM_016053.3.
DR AlphaFoldDB; Q9Y3C0; -.
DR SMR; Q9Y3C0; -.
DR BioGRID; 119225; 131.
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; Q9Y3C0; -.
DR IntAct; Q9Y3C0; 100.
DR MINT; Q9Y3C0; -.
DR STRING; 9606.ENSP00000240079; -.
DR TCDB; 9.A.3.1.2; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
DR iPTMnet; Q9Y3C0; -.
DR PhosphoSitePlus; Q9Y3C0; -.
DR BioMuta; WASHC3; -.
DR DMDM; 6831732; -.
DR EPD; Q9Y3C0; -.
DR jPOST; Q9Y3C0; -.
DR MassIVE; Q9Y3C0; -.
DR MaxQB; Q9Y3C0; -.
DR PaxDb; Q9Y3C0; -.
DR PeptideAtlas; Q9Y3C0; -.
DR PRIDE; Q9Y3C0; -.
DR ProteomicsDB; 86009; -.
DR Antibodypedia; 49055; 52 antibodies from 15 providers.
DR DNASU; 51019; -.
DR Ensembl; ENST00000240079.11; ENSP00000240079.6; ENSG00000120860.11.
DR GeneID; 51019; -.
DR KEGG; hsa:51019; -.
DR MANE-Select; ENST00000240079.11; ENSP00000240079.6; NM_016053.4; NP_057137.1.
DR UCSC; uc010svw.3; human.
DR CTD; 51019; -.
DR DisGeNET; 51019; -.
DR GeneCards; WASHC3; -.
DR HGNC; HGNC:24256; WASHC3.
DR HPA; ENSG00000120860; Low tissue specificity.
DR neXtProt; NX_Q9Y3C0; -.
DR OpenTargets; ENSG00000120860; -.
DR PharmGKB; PA142672169; -.
DR VEuPathDB; HostDB:ENSG00000120860; -.
DR eggNOG; KOG4496; Eukaryota.
DR GeneTree; ENSGT00390000014084; -.
DR InParanoid; Q9Y3C0; -.
DR OMA; GCETKFV; -.
DR OrthoDB; 1425330at2759; -.
DR PhylomeDB; Q9Y3C0; -.
DR TreeFam; TF318955; -.
DR PathwayCommons; Q9Y3C0; -.
DR SignaLink; Q9Y3C0; -.
DR SIGNOR; Q9Y3C0; -.
DR BioGRID-ORCS; 51019; 67 hits in 1045 CRISPR screens.
DR ChiTaRS; CCDC53; human.
DR GeneWiki; CCDC53; -.
DR GenomeRNAi; 51019; -.
DR Pharos; Q9Y3C0; Tdark.
DR PRO; PR:Q9Y3C0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y3C0; protein.
DR Bgee; ENSG00000120860; Expressed in left testis and 201 other tissues.
DR ExpressionAtlas; Q9Y3C0; baseline and differential.
DR Genevisible; Q9Y3C0; HS.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
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; IC:ComplexPortal.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
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; IPR019309; WASHC3.
DR PANTHER; PTHR13015; PTHR13015; 1.
DR Pfam; PF10152; CCDC53; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Endosome; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..194
FT /note="WASH complex subunit 3"
FT /id="PRO_0000076201"
FT REGION 93..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 46..74
FT /evidence="ECO:0000255"
FT COMPBIAS 160..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 81
FT /note="D -> G (in Ref. 5; BAD97059)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="N -> S (in Ref. 7; AAH10889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 21173 MW; B0CCF1AE76CDA6D2 CRC64;
MDEDGLPLMG SGIDLTKVPA IQQKRTVAFL NQFVVHTVQF LNRFSTVCEE KLADLSLRIQ
QIETTLNILD AKLSSIPGLD DVTVEVSPLN VTSVTNGAHP EATSEQPQQN STQDSGLQES
EVSAENILTV AKDPRYARYL KMVQVGVPVM AIRNKMISEG LDPDLLERPD APVPDGESEK
TVEESSDSES SFSD
