ID ATX3_HUMAN Reviewed; 361 AA. AC P54252; A7LFZ5; D6RDL9; E9PB63; O15284; O15285; O15286; Q8N189; Q96TC3; AC Q96TC4; Q9H3N0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2017, sequence version 5. DT 27-MAR-2024, entry version 229. DE RecName: Full=Ataxin-3; DE EC=3.4.19.12 {ECO:0000269|PubMed:17696782, ECO:0000269|PubMed:33157014}; DE AltName: Full=Machado-Joseph disease protein 1; DE AltName: Full=Spinocerebellar ataxia type 3 protein; GN Name=ATXN3 {ECO:0000303|PubMed:33157014, ECO:0000312|HGNC:HGNC:7106}; GN Synonyms=ATX3, MJD, MJD1, SCA3; 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 [MRNA] (ISOFORM 1), VARIANTS MET-212 AND GLY-306 DELINS RP GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-ARG, VARIANT RP 349-TYR--LEU-364 DEL (ISOFORM 1), AND INVOLVEMENT IN SCA3. RC TISSUE=Brain; RX PubMed=7874163; DOI=10.1038/ng1194-221; RA Kawaguchi Y., Okamoto T., Taniwaki M., Aizawa M., Inoue M., Katayama S., RA Kawakami H., Nakamura S., Nishimura M., Akiguchi I., Kimura J., RA Narumiya S., Kakizuka A.; RT "CAG expansions in a novel gene for Machado-Joseph disease at chromosome RT 14q32.1."; RL Nat. Genet. 8:221-228(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS MET-212 AND GLY-306 RP DELINS GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-ARG, AND VARIANT RP 349-TYR--LEU-364 DEL (ISOFORM 1). RX PubMed=9274833; DOI=10.1016/s0168-0102(97)00056-4; RA Goto J., Watanabe M., Ichikawa Y., Yee S.-B., Ihara N., Endo K., RA Igarashi S., Takiyama Y., Gaspar C., Maciel P., Tsuji S., Rouleau G.A., RA Kanazawa I.; RT "Machado-Joseph disease gene products carrying different carboxyl RT termini."; RL Neurosci. Res. 28:373-377(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANT RP 349-TYR--LEU-364 DEL (ISOFORM 1). RX PubMed=11450850; DOI=10.1007/s100380170060; RA Ichikawa Y., Goto J., Hattori M., Toyoda A., Ishii K., Jeong S.-Y., RA Hashida H., Masuda N., Ogata K., Kasai F., Hirai M., Maciel P., RA Rouleau G.A., Sakaki Y., Kanazawa I.; RT "The genomic structure and expression of MJD, the Machado-Joseph disease RT gene."; RL J. Hum. Genet. 46:413-422(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-212. RG NIEHS SNPs program; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). 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] (ISOFORM 2), AND VARIANT GLY-306 RP DELINS GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-ARG. RC TISSUE=Mammary gland; 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 SUBCELLULAR LOCATION. RX PubMed=9580663; DOI=10.1093/hmg/7.6.991; RA Tait D., Riccio M., Sittler A., Scherzinger E., Santi S., Ognibene A., RA Maraldi N.M., Lehrach H., Wanker E.E.; RT "Ataxin-3 is transported into the nucleus and associates with the nuclear RT matrix."; RL Hum. Mol. Genet. 7:991-997(1998). RN [9] RP FUNCTION. RX PubMed=12297501; DOI=10.1074/jbc.m205259200; RA Li F., Macfarlan T., Pittman R.N., Chakravarti D.; RT "Ataxin-3 is a histone-binding protein with two independent transcriptional RT corepressor activities."; RL J. Biol. Chem. 277:45004-45012(2002). RN [10] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=17696782; DOI=10.1515/bc.2007.107; RA Tzvetkov N., Breuer P.; RT "Josephin domain-containing proteins from a variety of species are active RT de-ubiquitination enzymes."; RL Biol. Chem. 388:973-978(2007). RN [11] 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 [12] RP FUNCTION, AND MUTAGENESIS OF CYS-14. RX PubMed=23625928; DOI=10.1074/jbc.m113.463406; RA Seki T., Gong L., Williams A.J., Sakai N., Todi S.V., Paulson H.L.; RT "JosD1, a membrane-targeted deubiquitinating enzyme, is activated by RT ubiquitination and regulates membrane dynamics, cell motility, and RT endocytosis."; RL J. Biol. Chem. 288:17145-17155(2013). RN [13] RP UBIQUITINATION AT MET-1 AND LYS-200. RX PubMed=23696636; DOI=10.1074/jbc.c113.477596; RA Scaglione K.M., Basrur V., Ashraf N.S., Konen J.R., Elenitoba-Johnson K.S., RA Todi S.V., Paulson H.L.; RT "The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus RT of substrates."; RL J. Biol. Chem. 288:18784-18788(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, 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 [15] RP INTERACTION WITH BECN1, FUNCTION, AND DOMAIN. RX PubMed=28445460; DOI=10.1038/nature22078; RA Ashkenazi A., Bento C.F., Ricketts T., Vicinanza M., Siddiqi F., Pavel M., RA Squitieri F., Hardenberg M.C., Imarisio S., Menzies F.M., Rubinsztein D.C.; RT "Polyglutamine tracts regulate beclin 1-dependent autophagy."; RL Nature 545:108-111(2017). RN [16] RP SUBCELLULAR LOCATION, INTERACTION WITH CASP7; PRKN; UBR2; VCP; RAD23A AND RP RAD23B, INTERACTION WITH TUBULIN, AND CHARACTERIZATION OF VARIANT RP 349-TYR--LEU-364 DEL (ISOFORM 1). RX PubMed=30455355; DOI=10.1074/jbc.ra118.005801; RA Weishaeupl D., Schneider J., Peixoto Pinheiro B., Ruess C., Dold S.M., RA von Zweydorf F., Gloeckner C.J., Schmidt J., Riess O., Schmidt T.; RT "Physiological and pathophysiological characteristics of ataxin-3 RT isoforms."; RL J. Biol. Chem. 294:644-661(2019). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVE SITE, AND RP MUTAGENESIS OF CYS-14. RX PubMed=33157014; DOI=10.1016/j.molcel.2020.10.004; RA Yao Y., Hong S., Ikeda T., Mori H., MacDougald O.A., Nada S., Okada M., RA Inoki K.; RT "Amino acids enhance polyubiquitination of Rheb and its binding to mTORC1 RT by blocking lysosomal ATXN3 deubiquitinase activity."; RL Mol. Cell 80:437-451(2020). RN [18] RP 3D-STRUCTURE MODELING. RX PubMed=12486728; DOI=10.1002/prot.10280; RA Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T.; RT "Structural modeling of ataxin-3 reveals distant homology to adaptins."; RL Proteins 50:355-370(2003). RN [19] RP STRUCTURE BY NMR OF 1-182, AND INTERACTION WITH RAD23A AND RAD23B. RX PubMed=16020535; DOI=10.1073/pnas.0501732102; RA Nicastro G., Menon R.P., Masino L., Knowles P.P., McDonald N.Q., RA Pastore A.; RT "The solution structure of the Josephin domain of ataxin-3: structural RT determinants for molecular recognition."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10493-10498(2005). RN [20] RP STRUCTURE BY NMR OF 1-185, FUNCTION, AND MUTAGENESIS OF CYS-14; SER-236; RP SER-256 AND SER-335. RX PubMed=16118278; DOI=10.1073/pnas.0506344102; RA Mao Y., Senic-Matuglia F., Di Fiore P.P., Polo S., Hodsdon M.E., RA De Camilli P.; RT "Deubiquitinating function of ataxin-3: insights from the solution RT structure of the Josephin domain."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12700-12705(2005). CC -!- FUNCTION: Deubiquitinating enzyme involved in protein homeostasis CC maintenance, transcription, cytoskeleton regulation, myogenesis and CC degradation of misfolded chaperone substrates (PubMed:12297501, CC PubMed:17696782, PubMed:23625928, PubMed:28445460, PubMed:33157014, CC PubMed:16118278). Binds long polyubiquitin chains and trims them, while CC it has weak or no activity against chains of 4 or less ubiquitins CC (PubMed:17696782). Involved in degradation of misfolded chaperone CC substrates via its interaction with STUB1/CHIP: recruited to CC monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin CC chain attached to STUB1/CHIP substrates and preventing further chain CC extension (By similarity). Interacts with key regulators of CC transcription and represses transcription: acts as a histone-binding CC protein that regulates transcription (PubMed:12297501). Acts as a CC negative regulator of mTORC1 signaling in response to amino acid CC deprivation by mediating deubiquitination of RHEB, thereby promoting CC RHEB inactivation by the TSC-TBC complex (PubMed:33157014). Regulates CC autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the CC stabilization of BECN1 (PubMed:28445460). CC {ECO:0000250|UniProtKB:Q9CVD2, ECO:0000269|PubMed:12297501, CC ECO:0000269|PubMed:16118278, ECO:0000269|PubMed:17696782, CC ECO:0000269|PubMed:23625928, ECO:0000269|PubMed:28445460, CC ECO:0000269|PubMed:33157014}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:17696782, CC ECO:0000269|PubMed:33157014}; CC -!- SUBUNIT: Interacts with STUB1/CHIP (when monoubiquitinated) (By CC similarity). Interacts with DNA repair proteins RAD23A and RAD23B CC (PubMed:16020535, PubMed:30455355). Interacts with BECN1 (via its poly- CC Gln domain) (PubMed:28445460). Interacts with PRKN, UBR2, VCP and CC tubulin. Short isoform 1 interacts with CASP7 (PubMed:30455355). CC {ECO:0000250|UniProtKB:Q9CVD2, ECO:0000269|PubMed:16020535, CC ECO:0000269|PubMed:28445460, ECO:0000269|PubMed:30455355}. CC -!- INTERACTION: CC P54252; Q9H7C9: AAMDC; NbExp=3; IntAct=EBI-946046, EBI-10308705; CC P54252; Q6PCB6: ABHD17C; NbExp=3; IntAct=EBI-946046, EBI-22011868; CC P54252; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-946046, EBI-10173507; CC P54252; O43488: AKR7A2; NbExp=3; IntAct=EBI-946046, EBI-748855; CC P54252; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-946046, EBI-2875816; CC P54252; Q14CB8: ARHGAP19; NbExp=4; IntAct=EBI-946046, EBI-954525; CC P54252; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-946046, EBI-14199987; CC P54252; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-946046, EBI-9089489; CC P54252; P06276: BCHE; NbExp=3; IntAct=EBI-946046, EBI-7936069; CC P54252; Q96G97-4: BSCL2; NbExp=3; IntAct=EBI-946046, EBI-10178113; CC P54252; Q6UWD8: C16orf54; NbExp=3; IntAct=EBI-946046, EBI-18041102; CC P54252; P29466-3: CASP1; NbExp=9; IntAct=EBI-946046, EBI-12248206; CC P54252; P42574: CASP3; NbExp=9; IntAct=EBI-946046, EBI-524064; CC P54252; Q96LX7-5: CCDC17; NbExp=3; IntAct=EBI-946046, EBI-12165781; CC P54252; P40227: CCT6A; NbExp=3; IntAct=EBI-946046, EBI-356687; CC P54252; Q5VV42: CDKAL1; NbExp=3; IntAct=EBI-946046, EBI-10194801; CC P54252; Q16740: CLPP; NbExp=3; IntAct=EBI-946046, EBI-1056029; CC P54252; Q02930-3: CREB5; NbExp=3; IntAct=EBI-946046, EBI-10192698; CC P54252; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-946046, EBI-2872414; CC P54252; Q9H816: DCLRE1B; NbExp=3; IntAct=EBI-946046, EBI-3508943; CC P54252; Q9P1A6-3: DLGAP2; NbExp=3; IntAct=EBI-946046, EBI-12019838; CC P54252; P50570-2: DNM2; NbExp=3; IntAct=EBI-946046, EBI-10968534; CC P54252; Q3B7T1: EDRF1; NbExp=3; IntAct=EBI-946046, EBI-2870947; CC P54252; Q01844: EWSR1; NbExp=4; IntAct=EBI-946046, EBI-739737; CC P54252; Q01844-3: EWSR1; NbExp=9; IntAct=EBI-946046, EBI-25973273; CC P54252; Q01844-4: EWSR1; NbExp=3; IntAct=EBI-946046, EBI-25896785; CC P54252; O15287: FANCG; NbExp=3; IntAct=EBI-946046, EBI-81610; CC P54252; P23142-4: FBLN1; NbExp=3; IntAct=EBI-946046, EBI-11956479; CC P54252; Q9UHY8: FEZ2; NbExp=6; IntAct=EBI-946046, EBI-396453; CC P54252; Q3SYB3: FOXD4L6; NbExp=3; IntAct=EBI-946046, EBI-6425864; CC P54252; P06241-3: FYN; NbExp=3; IntAct=EBI-946046, EBI-10691738; CC P54252; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-946046, EBI-11110431; CC P54252; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-946046, EBI-739467; CC P54252; O75409: H2AP; NbExp=3; IntAct=EBI-946046, EBI-6447217; CC P54252; P68431: H3C12; NbExp=3; IntAct=EBI-946046, EBI-79722; CC P54252; Q969S8: HDAC10; NbExp=3; IntAct=EBI-946046, EBI-301762; CC P54252; O75330-3: HMMR; NbExp=3; IntAct=EBI-946046, EBI-12098658; CC P54252; P22692: IGFBP4; NbExp=3; IntAct=EBI-946046, EBI-2831948; CC P54252; Q16891: IMMT; NbExp=4; IntAct=EBI-946046, EBI-473801; CC P54252; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-946046, EBI-714379; CC P54252; Q9BYZ2: LDHAL6B; NbExp=3; IntAct=EBI-946046, EBI-1108377; CC P54252; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-946046, EBI-10258746; CC P54252; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-946046, EBI-12056869; CC P54252; O94851: MICAL2; NbExp=3; IntAct=EBI-946046, EBI-2804835; CC P54252; A4FUJ8: MKL1; NbExp=3; IntAct=EBI-946046, EBI-21250407; CC P54252; Q13064: MKRN3; NbExp=3; IntAct=EBI-946046, EBI-2340269; CC P54252; Q9Y483-4: MTF2; NbExp=3; IntAct=EBI-946046, EBI-10698053; CC P54252; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-946046, EBI-6952711; CC P54252; Q15466: NR0B2; NbExp=3; IntAct=EBI-946046, EBI-3910729; CC P54252; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-946046, EBI-1059321; CC P54252; Q96DC9: OTUB2; NbExp=9; IntAct=EBI-946046, EBI-746259; CC P54252; Q96DC9-2: OTUB2; NbExp=9; IntAct=EBI-946046, EBI-25973449; CC P54252; Q9BWI9: OTUB2; NbExp=6; IntAct=EBI-946046, EBI-10300896; CC P54252; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-946046, EBI-2513978; CC P54252; Q9NVD7: PARVA; NbExp=9; IntAct=EBI-946046, EBI-747655; CC P54252; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-946046, EBI-11022007; CC P54252; O15530-4: PDPK1; NbExp=3; IntAct=EBI-946046, EBI-9087775; CC P54252; Q9BSU1: PHAF1; NbExp=4; IntAct=EBI-946046, EBI-946080; CC P54252; O75925: PIAS1; NbExp=9; IntAct=EBI-946046, EBI-629434; CC P54252; P42336: PIK3CA; NbExp=3; IntAct=EBI-946046, EBI-2116585; CC P54252; Q03405-2: PLAUR; NbExp=3; IntAct=EBI-946046, EBI-11028203; CC P54252; Q8NBT0: POC1A; NbExp=3; IntAct=EBI-946046, EBI-2557132; CC P54252; P17612: PRKACA; NbExp=3; IntAct=EBI-946046, EBI-476586; CC P54252; P51665: PSMD7; NbExp=9; IntAct=EBI-946046, EBI-357659; CC P54252; P54725: RAD23A; NbExp=9; IntAct=EBI-946046, EBI-746453; CC P54252; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-946046, EBI-438710; CC P54252; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-946046, EBI-740343; CC P54252; Q6ZNA4-2: RNF111; NbExp=6; IntAct=EBI-946046, EBI-21535400; CC P54252; Q96EP0: RNF31; NbExp=3; IntAct=EBI-946046, EBI-948111; CC P54252; Q8N5Z7: RPL6; NbExp=6; IntAct=EBI-946046, EBI-25973375; CC P54252; Q8TBK5: RPL6; NbExp=9; IntAct=EBI-946046, EBI-1642329; CC P54252; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-946046, EBI-10248967; CC P54252; P16581: SELE; NbExp=3; IntAct=EBI-946046, EBI-8007671; CC P54252; P50454: SERPINH1; NbExp=3; IntAct=EBI-946046, EBI-350723; CC P54252; Q8IVP1: SH3GL3; NbExp=3; IntAct=EBI-946046, EBI-6503765; CC P54252; Q9NQ40: SLC52A3; NbExp=3; IntAct=EBI-946046, EBI-25845274; CC P54252; O95416: SOX14; NbExp=3; IntAct=EBI-946046, EBI-9087806; CC P54252; Q99932-2: SPAG8; NbExp=6; IntAct=EBI-946046, EBI-11959123; CC P54252; Q8IUW3: SPATA2L; NbExp=3; IntAct=EBI-946046, EBI-2510414; CC P54252; Q8N865: SPMIP4; NbExp=3; IntAct=EBI-946046, EBI-10174456; CC P54252; Q9NRP7: STK36; NbExp=3; IntAct=EBI-946046, EBI-863797; CC P54252; Q8TDW5-2: SYTL5; NbExp=3; IntAct=EBI-946046, EBI-12243980; CC P54252; Q9Y458: TBX22; NbExp=3; IntAct=EBI-946046, EBI-6427217; CC P54252; O95551: TDP2; NbExp=3; IntAct=EBI-946046, EBI-2819865; CC P54252; Q9Y4R8: TELO2; NbExp=3; IntAct=EBI-946046, EBI-1043674; CC P54252; Q15554-4: TERF2; NbExp=3; IntAct=EBI-946046, EBI-25840535; CC P54252; Q8IYF3-3: TEX11; NbExp=6; IntAct=EBI-946046, EBI-11523345; CC P54252; Q8NA77: TEX19; NbExp=3; IntAct=EBI-946046, EBI-13323487; CC P54252; P37173: TGFBR2; NbExp=3; IntAct=EBI-946046, EBI-296151; CC P54252; Q9BXR5: TLR10; NbExp=3; IntAct=EBI-946046, EBI-16825459; CC P54252; Q9H8H3: TMT1A; NbExp=3; IntAct=EBI-946046, EBI-1390168; CC P54252; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-946046, EBI-741480; CC P54252; P13051-2: UNG; NbExp=3; IntAct=EBI-946046, EBI-25834258; CC P54252; Q92995: USP13; NbExp=3; IntAct=EBI-946046, EBI-714351; CC P54252; P55072: VCP; NbExp=4; IntAct=EBI-946046, EBI-355164; CC P54252; Q8NEZ2: VPS37A; NbExp=3; IntAct=EBI-946046, EBI-2850578; CC P54252; Q15007-2: WTAP; NbExp=3; IntAct=EBI-946046, EBI-25840023; CC P54252; Q9H0M0: WWP1; NbExp=3; IntAct=EBI-946046, EBI-742157; CC P54252; Q9H4I2-2: ZHX3; NbExp=3; IntAct=EBI-946046, EBI-10693326; CC P54252; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-946046, EBI-2682299; CC P54252; Q8N895: ZNF366; NbExp=3; IntAct=EBI-946046, EBI-2813661; CC P54252-1; P54252-1: ATXN3; NbExp=6; IntAct=EBI-946068, EBI-946068; CC P54252-1; Q14457: BECN1; NbExp=10; IntAct=EBI-946068, EBI-949378; CC P54252-1; P54257: HAP1; NbExp=6; IntAct=EBI-946068, EBI-712814; CC P54252-1; P0CG48: UBC; NbExp=2; IntAct=EBI-946068, EBI-3390054; CC P54252-1; P55072: VCP; NbExp=16; IntAct=EBI-946068, EBI-355164; CC P54252-2; O60260: PRKN; NbExp=5; IntAct=EBI-9684323, EBI-716346; CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:9580663}. CC Nucleus {ECO:0000269|PubMed:30455355}. Lysosome membrane CC {ECO:0000269|PubMed:33157014}; Peripheral membrane protein CC {ECO:0000269|PubMed:33157014}. Note=Predominantly nuclear, but not CC exclusively, inner nuclear matrix (PubMed:9580663). Recruited to CC lysosomal membrane in response to amino acid deprivation by the CC RagA/RRAGA-RagB/RRAGB complex (PubMed:33157014). CC {ECO:0000269|PubMed:33157014, ECO:0000269|PubMed:9580663}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=2; CC IsoId=P54252-2; Sequence=Displayed; CC Name=1; Synonyms=MJD1a; CC IsoId=P54252-1; Sequence=VSP_002784; CC Name=3; CC IsoId=P54252-3; Sequence=VSP_002783; CC Name=4; CC IsoId=P54252-4; Sequence=VSP_047086; CC Name=5; CC IsoId=P54252-5; Sequence=VSP_047085; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DOMAIN: The UIM domains bind ubiquitin and interact with various E3 CC ubiquitin-protein ligase, such as STUB1/CHIP. They are essential to CC limit the length of ubiquitin chains (By similarity). CC {ECO:0000250|UniProtKB:Q9CVD2}. CC -!- DOMAIN: The poly-Gln domain is involved in the interaction with BECN1 CC and subsequent starvation-induced autophagy (PubMed:28445460). CC {ECO:0000269|PubMed:28445460}. CC -!- PTM: Monoubiquitinated N-terminally by UBE2W, possibly leading to CC activate the deubiquitinating enzyme activity (PubMed:23696636). CC {ECO:0000269|PubMed:23696636}. CC -!- POLYMORPHISM: The poly-Gln region of ATXN3 is highly polymorphic (14 to CC 41 repeats) in the normal population and is expanded to about 55-82 CC repeats in spinocerebellar ataxia 3 (SCA3) patients (PubMed:7874163, CC PubMed:9274833). {ECO:0000269|PubMed:7874163, CC ECO:0000269|PubMed:9274833}. CC -!- DISEASE: Spinocerebellar ataxia 3 (SCA3) [MIM:109150]: Spinocerebellar CC ataxia is a clinically and genetically heterogeneous group of CC cerebellar disorders. Patients show progressive incoordination of gait CC and often poor coordination of hands, speech and eye movements, due to CC cerebellum degeneration with variable involvement of the brainstem and CC spinal cord. SCA3 belongs to the autosomal dominant cerebellar ataxias CC type I (ADCA I) which are characterized by cerebellar ataxia in CC combination with additional clinical features like optic atrophy, CC ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy CC and dementia. The molecular defect in SCA3 is the a CAG repeat CC expansion in ATX3 coding region. Longer expansions result in earlier CC onset and more severe clinical manifestations of the disease. CC {ECO:0000269|PubMed:7874163}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/atxn3/"; 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; S75313; AAB33571.1; -; mRNA. DR EMBL; U64820; AAB63352.1; -; mRNA. DR EMBL; U64821; AAB63353.1; -; mRNA. DR EMBL; U64822; AAB63354.1; -; mRNA. DR EMBL; AB050194; BAB18798.1; -; mRNA. DR EMBL; AB038653; BAB55645.1; -; Genomic_DNA. DR EMBL; AB038653; BAB55646.1; -; Genomic_DNA. DR EMBL; EU009923; ABS29269.1; -; Genomic_DNA. DR EMBL; AL049872; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121773; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471061; EAW81472.1; -; Genomic_DNA. DR EMBL; BC033711; AAH33711.1; -; mRNA. DR CCDS; CCDS32143.1; -. [P54252-3] DR CCDS; CCDS45154.1; -. [P54252-4] DR CCDS; CCDS53908.1; -. [P54252-5] DR CCDS; CCDS9900.1; -. [P54252-2] DR PIR; S50830; S50830. DR RefSeq; NP_001121168.1; NM_001127696.1. [P54252-4] DR RefSeq; NP_001158252.1; NM_001164780.1. [P54252-5] DR RefSeq; NP_004984.2; NM_004993.5. [P54252-2] DR RefSeq; NP_109376.1; NM_030660.4. [P54252-3] DR PDB; 1YZB; NMR; -; A=1-182. DR PDB; 2AGA; NMR; -; A=1-185. DR PDB; 2DOS; NMR; -; A=1-171. DR PDB; 2JRI; NMR; -; A=1-182. DR PDB; 2KLZ; NMR; -; A=222-263. DR PDB; 4WTH; X-ray; 2.25 A; A/B=278-324. DR PDB; 4YS9; X-ray; 2.00 A; B=278-324. DR PDBsum; 1YZB; -. DR PDBsum; 2AGA; -. DR PDBsum; 2DOS; -. DR PDBsum; 2JRI; -. DR PDBsum; 2KLZ; -. DR PDBsum; 4WTH; -. DR PDBsum; 4YS9; -. DR AlphaFoldDB; P54252; -. DR BMRB; P54252; -. DR SASBDB; P54252; -. DR SMR; P54252; -. DR BioGRID; 110433; 452. DR ELM; P54252; -. DR IntAct; P54252; 133. DR MINT; P54252; -. DR STRING; 9606.ENSP00000496695; -. DR BindingDB; P54252; -. DR ChEMBL; CHEMBL4523240; -. DR MEROPS; C86.001; -. DR iPTMnet; P54252; -. DR MetOSite; P54252; -. DR PhosphoSitePlus; P54252; -. DR BioMuta; ATXN3; -. DR DMDM; 290457685; -. DR EPD; P54252; -. DR jPOST; P54252; -. DR MassIVE; P54252; -. DR MaxQB; P54252; -. DR PaxDb; 9606-ENSP00000478320; -. DR PeptideAtlas; P54252; -. DR ProteomicsDB; 14137; -. DR ProteomicsDB; 19154; -. DR ProteomicsDB; 56655; -. [P54252-1] DR ProteomicsDB; 56656; -. [P54252-2] DR ProteomicsDB; 56657; -. [P54252-3] DR Pumba; P54252; -. DR Antibodypedia; 13668; 373 antibodies from 32 providers. DR DNASU; 4287; -. DR Ensembl; ENST00000340660.10; ENSP00000339110.6; ENSG00000066427.25. [P54252-3] DR Ensembl; ENST00000502250.5; ENSP00000425322.1; ENSG00000066427.25. [P54252-5] DR Ensembl; ENST00000503767.5; ENSP00000426697.1; ENSG00000066427.25. [P54252-4] DR Ensembl; ENST00000532032.5; ENSP00000437157.1; ENSG00000066427.25. [P54252-1] DR Ensembl; ENST00000644486.2; ENSP00000496695.1; ENSG00000066427.25. [P54252-2] DR GeneID; 4287; -. DR KEGG; hsa:4287; -. DR MANE-Select; ENST00000644486.2; ENSP00000496695.1; NM_004993.6; NP_004984.2. DR UCSC; uc001yac.5; human. [P54252-2] DR AGR; HGNC:7106; -. DR CTD; 4287; -. DR DisGeNET; 4287; -. DR GeneCards; ATXN3; -. DR GeneReviews; ATXN3; -. DR HGNC; HGNC:7106; ATXN3. DR HPA; ENSG00000066427; Low tissue specificity. DR MalaCards; ATXN3; -. DR MIM; 109150; phenotype. DR MIM; 607047; gene. DR neXtProt; NX_P54252; -. DR OpenTargets; ENSG00000066427; -. DR Orphanet; 276238; Machado-Joseph disease type 1. DR Orphanet; 276241; Machado-Joseph disease type 2. DR Orphanet; 276244; Machado-Joseph disease type 3. DR PharmGKB; PA134971833; -. DR VEuPathDB; HostDB:ENSG00000066427; -. DR eggNOG; KOG2935; Eukaryota. DR GeneTree; ENSGT00390000001830; -. DR InParanoid; P54252; -. DR OMA; LGQAYIC; -. DR OrthoDB; 337428at2759; -. DR PhylomeDB; P54252; -. DR TreeFam; TF314228; -. DR PathwayCommons; P54252; -. DR Reactome; R-HSA-5689877; Josephin domain DUBs. DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes. DR SignaLink; P54252; -. DR SIGNOR; P54252; -. DR BioGRID-ORCS; 4287; 10 hits in 1195 CRISPR screens. DR ChiTaRS; ATXN3; human. DR EvolutionaryTrace; P54252; -. DR GeneWiki; Ataxin_3; -. DR GenomeRNAi; 4287; -. DR Pharos; P54252; Tbio. DR PRO; PR:P54252; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P54252; Protein. DR Bgee; ENSG00000066427; Expressed in calcaneal tendon and 187 other cell types or tissues. DR ExpressionAtlas; P54252; baseline and differential. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; ISS:ParkinsonsUK-UCL. DR GO; GO:0031966; C:mitochondrial membrane; ISS:ParkinsonsUK-UCL. DR GO; GO:0042405; C:nuclear inclusion body; ISS:ParkinsonsUK-UCL. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0051117; F:ATPase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:1990380; F:K48-linked deubiquitinase activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0061578; F:K63-linked deubiquitinase activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI. DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB. DR GO; GO:0034605; P:cellular response to heat; ISS:ParkinsonsUK-UCL. DR GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB. DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc. DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI. DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IDA:UniProtKB. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0006289; P:nucleotide-excision repair; TAS:ProtInc. DR GO; GO:1904294; P:positive regulation of ERAD pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:ParkinsonsUK-UCL. DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:ParkinsonsUK-UCL. DR GO; GO:1904327; P:protein localization to cytosolic proteasome complex; IMP:ParkinsonsUK-UCL. DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB. DR GO; GO:0010810; P:regulation of cell-substrate adhesion; IMP:MGI. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:ParkinsonsUK-UCL. DR DisProt; DP00576; -. DR Gene3D; 3.90.70.40; -; 1. DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1. DR InterPro; IPR033865; Ataxin-3. DR InterPro; IPR006155; Josephin. DR InterPro; IPR003903; UIM_dom. DR PANTHER; PTHR14159; ATAXIN-3-RELATED; 1. DR PANTHER; PTHR14159:SF0; ATAXIN-3-RELATED; 1. DR Pfam; PF02099; Josephin; 1. DR Pfam; PF16619; SUIM_assoc; 1. DR Pfam; PF02809; UIM; 3. DR PRINTS; PR01233; JOSEPHIN. DR SMART; SM01246; Josephin; 1. DR SMART; SM00726; UIM; 3. DR PROSITE; PS50957; JOSEPHIN; 1. DR PROSITE; PS50330; UIM; 3. DR Genevisible; P54252; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Hydrolase; Isopeptide bond; Lysosome; KW Membrane; Neurodegeneration; Nucleus; Phosphoprotein; Protease; KW Reference proteome; Repeat; Spinocerebellar ataxia; Thiol protease; KW Transcription; Transcription regulation; Triplet repeat expansion; KW Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..361 FT /note="Ataxin-3" FT /id="PRO_0000053831" FT DOMAIN 1..180 FT /note="Josephin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331" FT DOMAIN 224..243 FT /note="UIM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT DOMAIN 244..263 FT /note="UIM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT DOMAIN 331..349 FT /note="UIM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT REGION 258..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 258..277 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 292..319 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 14 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:23625928, FT ECO:0000305|PubMed:33157014" FT ACT_SITE 119 FT /note="Proton acceptor" FT /evidence="ECO:0000305|PubMed:16020535, FT ECO:0000305|PubMed:16118278" FT ACT_SITE 134 FT /evidence="ECO:0000305|PubMed:16020535, FT ECO:0000305|PubMed:16118278" FT MOD_RES 219 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CVD2" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 272 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CVD2" FT MOD_RES 328 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CVD2" FT CROSSLNK 1 FT /note="Peptide (Met-Gly) (interchain with G-Cter in FT ubiquitin)" FT /evidence="ECO:0000269|PubMed:23696636" FT CROSSLNK 200 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:23696636" FT VAR_SEQ 1..179 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_047085" FT VAR_SEQ 10..64 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_002783" FT VAR_SEQ 63..77 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_047086" FT VAR_SEQ 332..361 FT /note="DAMSEEDMLQAAVTMSLETVRNDLKTEGKK -> KACSPFIMFATFTLYLTY FT ELHVIFALHYSSFPL (in isoform 1)" FT /evidence="ECO:0000303|PubMed:7874163, FT ECO:0000303|PubMed:9274833" FT /id="VSP_002784" FT VARIANT 212 FT /note="V -> M (in dbSNP:rs1048755)" FT /evidence="ECO:0000269|PubMed:7874163, FT ECO:0000269|PubMed:9274833, ECO:0000269|Ref.4" FT /id="VAR_013688" FT VARIANT 306 FT /note="G -> QQQQQQQQQQQQR" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:7874163, ECO:0000269|PubMed:9274833" FT /id="VAR_013689" FT MUTAGEN 14 FT /note="C->A: Loss of deubiquitination activity." FT /evidence="ECO:0000269|PubMed:16118278, FT ECO:0000269|PubMed:23625928, ECO:0000269|PubMed:33157014" FT MUTAGEN 236 FT /note="S->A: Inhibits substrate trapping." FT /evidence="ECO:0000269|PubMed:16118278" FT MUTAGEN 256 FT /note="S->A: Inhibits substrate trapping." FT /evidence="ECO:0000269|PubMed:16118278" FT MUTAGEN 335 FT /note="S->A: No effect on ubiquitination." FT /evidence="ECO:0000269|PubMed:16118278" FT CONFLICT 252 FT /note="A -> T (in Ref. 2; AAB63352/AAB63353/AAB63354)" FT /evidence="ECO:0000305" FT HELIX 1..3 FT /evidence="ECO:0007829|PDB:2AGA" FT HELIX 14..22 FT /evidence="ECO:0007829|PDB:1YZB" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:2JRI" FT HELIX 30..49 FT /evidence="ECO:0007829|PDB:1YZB" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:2AGA" FT HELIX 56..62 FT /evidence="ECO:0007829|PDB:1YZB" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:1YZB" FT HELIX 78..85 FT /evidence="ECO:0007829|PDB:1YZB" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:1YZB" FT STRAND 90..96 FT /evidence="ECO:0007829|PDB:1YZB" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:1YZB" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:1YZB" FT STRAND 109..116 FT /evidence="ECO:0007829|PDB:1YZB" FT STRAND 119..126 FT /evidence="ECO:0007829|PDB:1YZB" FT STRAND 129..134 FT /evidence="ECO:0007829|PDB:1YZB" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:1YZB" FT HELIX 145..158 FT /evidence="ECO:0007829|PDB:1YZB" FT STRAND 161..167 FT /evidence="ECO:0007829|PDB:1YZB" FT HELIX 173..176 FT /evidence="ECO:0007829|PDB:1YZB" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:2JRI" FT HELIX 222..240 FT /evidence="ECO:0007829|PDB:2KLZ" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:2KLZ" FT HELIX 246..257 FT /evidence="ECO:0007829|PDB:2KLZ" FT HELIX 279..282 FT /evidence="ECO:0007829|PDB:4YS9" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:4YS9" FT VARIANT P54252-1:349..364 FT /note="Missing (in short isoform 1, due to a stop-gain FT single nucleotide variant, has reduced half-life due to FT increased proteasomal degradation, has reduced solubility FT and increased tendency to form aggregates, increased FT localization to the nucleus)" FT /evidence="ECO:0000269|PubMed:11450850, FT ECO:0000269|PubMed:30455355, ECO:0000269|PubMed:7874163, FT ECO:0000269|PubMed:9274833" FT /id="VAR_082841" SQ SEQUENCE 361 AA; 41250 MW; 90C3EF73BB26CAFD CRC64; MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERMRMAE GGVTSEDYRT FLQQPSGNMD DSGFFSIQVI SNALKVWGLE LILFNSPEYQ RLRIDPINER SFICNYKEHW FTVRKLGKQW FNLNSLLTGP ELISDTYLAL FLAQLQQEGY SIFVVKGDLP DCEADQLLQM IRVQQMHRPK LIGEELAQLK EQRVHKTDLE RVLEANDGSG MLDEDEEDLQ RALALSRQEI DMEDEEADLR RAIQLSMQGS SRNISQDMTQ TSGTNLTSEE LRKRREAYFE KQQQKQQQQQ QQQQQGDLSG QSSHPCERPA TSSGALGSDL GDAMSEEDML QAAVTMSLET VRNDLKTEGK K //