ATX1_RAT
ID ATX1_RAT Reviewed; 789 AA.
AC Q63540;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ataxin-1;
DE AltName: Full=Spinocerebellar ataxia type 1 protein homolog;
GN Name=Atxn1; Synonyms=Sca1;
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].
RC TISSUE=Brain;
RX PubMed=8852664; DOI=10.1093/hmg/5.3.381;
RA Gossen M., Schmitt I., Obst K., Wahle P., Epplen J.T., Riess O.;
RT "cDNA cloning and expression of rsca1, the rat counterpart of the human
RT spinocerebellar ataxia type 1 gene.";
RL Hum. Mol. Genet. 5:381-389(1996).
CC -!- FUNCTION: Chromatin-binding factor that repress Notch signaling in the
CC absence of Notch intracellular domain by acting as a CBF1 corepressor.
CC Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-
CC mediated repression. Binds RNA in vitro. May be involved in RNA
CC metabolism. In concert with CIC and ATXN1L, involved brain development.
CC {ECO:0000250|UniProtKB:P54253, ECO:0000250|UniProtKB:P54254}.
CC -!- SUBUNIT: Homooligomer. Interacts with CIC. Interacts with ANP32A,
CC PQBP1, UBQLN4, ATXN1L and USP7. Directly interacts with RBPJ; this
CC interaction is disrupted in the presence of Notch intracellular domain.
CC Competes with ATXN1L for RBPJ-binding. Found in a complex with CIC and
CC ATXN1L. {ECO:0000250|UniProtKB:P54253, ECO:0000250|UniProtKB:P54254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54253}. Nucleus
CC {ECO:0000250|UniProtKB:P54253}. Note=Colocalizes with USP7 in the
CC nucleus. {ECO:0000250|UniProtKB:P54253}.
CC -!- DOMAIN: The AXH domain is required for interaction with CIC.
CC {ECO:0000250|UniProtKB:P54254}.
CC -!- PTM: Ubiquitinated by UBE3A, leading to its degradation by the
CC proteasome. {ECO:0000250|UniProtKB:P54254}.
CC -!- PTM: Phosphorylation at Ser-749 increases the pathogenicity of proteins
CC with an expanded polyglutamine tract. {ECO:0000250|UniProtKB:P54253}.
CC -!- PTM: Sumoylation is dependent on nuclear localization and
CC phosphorylation at Ser-749. It is reduced in the presence of an
CC expanded polyglutamine tract. {ECO:0000250|UniProtKB:P54253}.
CC -!- POLYMORPHISM: The rat poly-Gln region is very limited in comparison to
CC human ATXN1 and is not polymorphic.
CC -!- SIMILARITY: Belongs to the ATXN1 family. {ECO:0000305}.
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DR EMBL; X91619; CAA62822.1; -; mRNA.
DR RefSeq; NP_036858.1; NM_012726.2.
DR AlphaFoldDB; Q63540; -.
DR BMRB; Q63540; -.
DR SMR; Q63540; -.
DR STRING; 10116.ENSRNOP00000023140; -.
DR iPTMnet; Q63540; -.
DR PhosphoSitePlus; Q63540; -.
DR PaxDb; Q63540; -.
DR PRIDE; Q63540; -.
DR ABCD; Q63540; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000023140; ENSRNOP00000023140; ENSRNOG00000016998.
DR GeneID; 25049; -.
DR KEGG; rno:25049; -.
DR CTD; 6310; -.
DR RGD; 3624; Atxn1.
DR eggNOG; KOG4053; Eukaryota.
DR GeneTree; ENSGT00390000005939; -.
DR HOGENOM; CLU_019983_0_0_1; -.
DR InParanoid; Q63540; -.
DR OMA; ENHRADN; -.
DR OrthoDB; 249631at2759; -.
DR PhylomeDB; Q63540; -.
DR TreeFam; TF350643; -.
DR PRO; PR:Q63540; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000016998; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; Q63540; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0051168; P:nuclear export; ISS:UniProtKB.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0035176; P:social behavior; ISS:UniProtKB.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR InterPro; IPR020997; Ataxin-1_N.
DR InterPro; IPR043404; ATAXIN1-like.
DR InterPro; IPR003652; Ataxin_AXH_dom.
DR InterPro; IPR036096; Ataxin_AXH_dom_sf.
DR InterPro; IPR040172; ATXN1.
DR PANTHER; PTHR13392; PTHR13392; 1.
DR PANTHER; PTHR13392:SF5; PTHR13392:SF5; 1.
DR Pfam; PF12547; ATXN-1_C; 1.
DR Pfam; PF08517; AXH; 1.
DR SMART; SM00536; AXH; 1.
DR SUPFAM; SSF102031; SSF102031; 1.
DR PROSITE; PS51148; AXH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..789
FT /note="Ataxin-1"
FT /id="PRO_0000064753"
FT DOMAIN 536..667
FT /note="AXH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00496"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..578
FT /note="Self-association"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT REGION 512..789
FT /note="Interaction with USP7"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT REGION 514..740
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT REGION 736..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 768..771
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P54254"
FT COMPBIAS 212..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54254"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54254"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54254"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT CROSSLNK 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P54253"
FT CROSSLNK 719
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P54253"
SQ SEQUENCE 789 AA; 83501 MW; AFA042249BAC99FE CRC64;
MKSNQERSNE CLPPKKREIP ATSRPSEEKA TALPSDNHCV EGVAWLPSTP GSRGHGGGRH
GPAGTSGEHG LQGMGLHKAL SAGLDYSPPS APRSVPTANT LPTVYPPPQS GTPVSPVQYA
HLSHTFQFIG SSQYSGPYAG FIPSQLISPP GNPVTSAVAS AAGATTPSQR SQLEAYSTLL
ANMGSLSQAP GHKVEPPPQQ HLGRAAGLVN PGSPPPTQQN QYIHISSSPQ SSGRATSPPI
PVHLHPHQTM IPHTLTLGPS SQVVVQYSDA GGHFVPREST KKAESSRLQQ AMQAKEVLNG
EMEKSRRYGA SSSVELSLGK TSSKSVPHPY ESRHVVVHPS PADYSSRDTS GVRGSVMVLP
NSSTPSADLE TQQATHREAS PSTLNDKSGL HLGKPGHRSY ALSPHTVIQT THSASEPLPV
GLPATAFYAG AQPPVIGYLS SQQQAITYAG GLPQHLVIPG TQPLLIPVGS PDMDTPGAAS
AIVTSSPQFA AVPHTFVTTA LPKSENFNPE ALVTQAAYPA MVQAQIHLPV VQSVASPAAA
SPTLPPYFMK GSIIQLANGE LKKVEDLKTE DFIQSAEISN DLKIDSSTVE RIEDSHSPGV
AVIQFAVGEH RAQVSVEVLV EYPFFVFGQG WSSCCPERTS QLFDLPCSKL SVGDVCISLT
LKNLKNGSVK KGQPVDPASA LLKHAKTDSL AGSRHRYAEQ ENGINQGSAQ VLSENGELKF
PEKIGLPAAP FLTKIEPSKP TATRKRRWSA PETRKLEKSE DEPPLTLPKP SLIPQEVKIC
IEGRSNVGK
