ID   ATX10_RAT               Reviewed;         475 AA.
AC   Q9ER24;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Ataxin-10;
DE   AltName: Full=Neuronal beta-catenin-like protein;
DE   AltName: Full=Spinocerebellar ataxia type 10 protein homolog;
GN   Name=Atxn10; Synonyms=Sca10;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=15201271; DOI=10.1074/jbc.m405865200;
RA   Maerz P., Probst A., Lang S., Schwager M., Rose-John S., Otten U.,
RA   Ozbek S.;
RT   "Ataxin-10, the spinocerebellar ataxia type 10 neurodegenerative disorder
RT   protein, is essential for survival of cerebellar neurons.";
RL   J. Biol. Chem. 279:35542-35550(2004).
RN   [2]
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   [3]
RP   INTERACTION WITH OGT, AND FUNCTION.
RX   PubMed=16714295; DOI=10.1074/jbc.m601563200;
RA   Maerz P., Stetefeld J., Bendfeldt K., Nitsch C., Reinstein J.,
RA   Shoeman R.L., Dimitriades-Schmutz B., Schwager M., Leiser D., Ozcan S.,
RA   Otten U., Ozbek S.;
RT   "Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in
RT   the brain.";
RL   J. Biol. Chem. 281:20263-20270(2006).
RN   [4]
RP   FUNCTION.
RX   PubMed=16498633; DOI=10.1002/jnr.20807;
RA   Waragai M., Nagamitsu S., Xu W., Li Y.J., Lin X., Ashizawa T.;
RT   "Ataxin 10 induces neuritogenesis via interaction with G-protein beta2
RT   subunit.";
RL   J. Neurosci. Res. 83:1170-1178(2006).
CC   -!- FUNCTION: Necessary for the survival of cerebellar neurons. Induces
CC       neuritogenesis by activating the Ras-MAP kinase pathway. May play a
CC       role in the maintenance of a critical intracellular glycosylation level
CC       and homeostasis. {ECO:0000269|PubMed:15201271,
CC       ECO:0000269|PubMed:16498633, ECO:0000269|PubMed:16714295}.
CC   -!- SUBUNIT: Interacts with GNB2 (By similarity). Homooligomer. Interacts
CC       with OGT in the brain. Interacts with IQCB1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15201271}.
CC       Cytoplasm, perinuclear region {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous distribution. Markedly increased
CC       expression in testis, adrenals, and brain.
CC       {ECO:0000269|PubMed:15201271}.
CC   -!- SIMILARITY: Belongs to the ataxin-10 family. {ECO:0000305}.
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DR   EMBL; AJ301634; CAC16214.1; -; mRNA.
DR   EMBL; BC062087; AAH62087.1; -; mRNA.
DR   RefSeq; NP_579847.1; NM_133313.2.
DR   AlphaFoldDB; Q9ER24; -.
DR   SMR; Q9ER24; -.
DR   BioGRID; 250992; 2.
DR   IntAct; Q9ER24; 4.
DR   STRING; 10116.ENSRNOP00000021071; -.
DR   iPTMnet; Q9ER24; -.
DR   PhosphoSitePlus; Q9ER24; -.
DR   jPOST; Q9ER24; -.
DR   PaxDb; Q9ER24; -.
DR   PRIDE; Q9ER24; -.
DR   GeneID; 170821; -.
DR   KEGG; rno:170821; -.
DR   CTD; 25814; -.
DR   RGD; 621813; Atxn10.
DR   VEuPathDB; HostDB:ENSRNOG00000014637; -.
DR   eggNOG; KOG2676; Eukaryota.
DR   HOGENOM; CLU_046084_1_0_1; -.
DR   InParanoid; Q9ER24; -.
DR   OMA; DICAWES; -.
DR   OrthoDB; 1416864at2759; -.
DR   PhylomeDB; Q9ER24; -.
DR   TreeFam; TF323870; -.
DR   PRO; PR:Q9ER24; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000014637; Expressed in cerebellum and 20 other tissues.
DR   Genevisible; Q9ER24; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR   GO; GO:0007399; P:nervous system development; ISO:RGD.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR019156; Ataxin-10_domain.
DR   Pfam; PF09759; Atx10homo_assoc; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methylation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..475
FT                   /note="Ataxin-10"
FT                   /id="PRO_0000064750"
FT   MOD_RES         10
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P28658"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBB4"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBB4"
SQ   SEQUENCE   475 AA;  53727 MW;  530F6E3E498CBB38 CRC64;
     MAAPRMPPSR LSGIMVPAPI QDLEALRALT ALFKEQRNRE TAPRTIFQRV LDILKKSTQA
     VELACRDPSQ VEHLASSLQL ITECFRCLRN ACIECSVNQN SIRNLDTIGV AVDLVLLFRE
     LRVEQDSLLT AFRCGLQFLG NVASRNEDSQ SIVWVHAFPE LFMSCLNHPD KKIVAYCSMI
     LFTSLNSERM KDLEENLNIA INVIEAHQKH PESEWPFLII TDHFLKSPEL VEAMYGKLSN
     QERVTLLDIM IAKIVGDEQL TKDDISIFLR HAELIANSFV DQCRNVLKLT SEPQTEDKEA
     LVTIRLLDVL CEMTSNTELL GYLQVFPGLM ERVIDVLRVI HSVGKDSTNI FSPSDSLKAE
     GDIEHMTEGF KSHLIRLIGN LCYKNKENQD KVNELDGIPL ILDSSNIDDN NPFMMQWVVY
     AVRNLTEDNS QNQDFIAKME EQGLADASLL KKMGFEVEKS GDKLILKSNN DIPPP