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O35126 (ATN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Atrophin-1
Alternative name(s):
Dentatorubral-pallidoluysian atrophy protein homolog
Gene names
Name:Atn1
Synonyms:Drpla
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1175 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of the poly-Q repeats By similarity. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation. Ref.5 Ref.7

Subunit structure

Interacts with BAIAP2, WWP1, WWP2, WWP3 and RERE. Interacts (via its N-terminus) with MTG8; the interaction enhances transcriptional repression of MTG8 By similarity. Interacts with NR2E1; the interaction represses the transcriptional activity of NR2E1. Interacts with FAT1 (via a C-terminal domain). Ref.5 Ref.7

Subcellular location

Nucleus. Cytoplasmperinuclear region. Cell junction By similarity. Nucleus By similarity. Note: Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells. Colocalizes with MTG8 in discrete nuclear dots By similarity.

Tissue specificity

Widely expressed. Most abundant in the brain. Ref.1

Developmental stage

Expressed as early as 5 days and thereafter shows little variation throughout 17 days. Ref.1

Induction

In vascular smooth muscle, induced by angiotensin II, FGF; PGF and IL1B. Ref.7

Post-translational modification

Phosphorylated in vitro by MAPK8/JNK1 on Ser-724 By similarity.

Polymorphism

The poly-Gln region of Atn1 is polymorphic (3 to 8 repeats).

Miscellaneous

The mouse model of DRPLA with 129 CAG repeats (Q129) exhibited severe neurological defects similar to those of juvenile-onset DRPLA patients including age-dependent and region-specific presynaptic dysfunction in the globus pallidus and cerebellum. Progressive shrinkage of distal dendrites of Purkinje cells and decreased currents through alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid and gamma-aminobutyrate type A receptors in CA1 neurons was observed. There is progressive brain atrophy.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11751175Atrophin-1
PRO_0000356253

Regions

Region503 – 55351Involved in binding BAIAP2 By similarity
Region864 – 87916Required for interaction with FAT1 By similarity
Motif16 – 3217Nuclear localization signal By similarity
Motif1018 – 10269Nuclear export signal By similarity
Compositional bias166 – 1727Poly-Pro
Compositional bias304 – 3074Poly-Pro
Compositional bias378 – 3836Poly-Ser
Compositional bias387 – 39610Poly-Ser
Compositional bias441 – 4466Poly-Pro
Compositional bias477 – 4804Poly-His
Compositional bias481 – 4877Poly-Gln
Compositional bias495 – 4984Poly-Pro
Compositional bias555 – 56410Poly-Ser
Compositional bias694 – 6974Poly-Pro
Compositional bias792 – 80514Ala/Arg-rich
Compositional bias806 – 81712Arg/Glu-rich (mixed charge)
Compositional bias915 – 92410Arg/Glu-rich (mixed charge)
Compositional bias1035 – 106228His-rich

Sites

Site109 – 1102Cleavage Potential

Amino acid modifications

Modified residue341Phosphoserine By similarity
Modified residue771Phosphoserine By similarity
Modified residue791Phosphoserine By similarity
Modified residue1011Phosphoserine By similarity
Modified residue1031Phosphoserine By similarity
Modified residue1071Phosphoserine By similarity
Modified residue6261N6-acetyllysine By similarity
Modified residue6381Phosphothreonine By similarity
Modified residue6461Phosphoserine By similarity
Modified residue7241Phosphoserine; by MAPK8 By similarity
Modified residue7311Phosphoserine By similarity
Modified residue7331Phosphoserine By similarity

Experimental info

Sequence conflict4521A → G in BAA13450. Ref.1
Sequence conflict4951P → A in BAA13450. Ref.1
Sequence conflict5321P → A in BAA13450. Ref.1
Sequence conflict6911S → L in BAA13450. Ref.1
Sequence conflict7341P → A in BAA13450. Ref.1
Sequence conflict7661D → T in BAA13450. Ref.1
Sequence conflict9261D → N in BAA13450. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35126 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 8BEFFAB75DDC0F36

FASTA1,175123,724
        10         20         30         40         50         60 
MKTRQNKDSM SMRSGRKKEA PGPREELRSR GRASPGGVST SSSDGKAEKS RQTAKKARIE 

        70         80         90        100        110        120 
EPSAPKASKQ GRSEEISESE SEETSAPKKT KTEQELPRPQ SPSDLDSLDG RSINDDGSSD 

       130        140        150        160        170        180 
PRDIDQDNRS TSPSIYSPGS VENDSDSSSG LSQGPARPYH PPPLFPPSPP PPDSTPRQPE 

       190        200        210        220        230        240 
SGFEPHPSVP PTGYHAPMEP PTSRLFQGPP PGAPPTHPQL YPGNASGGVL SGPPMGPKGG 

       250        260        270        280        290        300 
AAASSVGAPS GGKQHPPPTT PIPISSSGAS GAPPAKPPSA PVGGGSLPSA PPPASFPHVT 

       310        320        330        340        350        360 
PNLPPPPALR PLNNASASPP GMGAQPIPGH LPSPHAMGQG MSGLPPGPEK GPTLAPSPHP 

       370        380        390        400        410        420 
LPPASSSAPG PPMRYPYSSS SSSAAASSSS SSSSASQYPA SQALPSYPHS FPPPTSMSVS 

       430        440        450        460        470        480 
NQPPKYTQPS LPSQAVWSQG PPPPPPYGRL LANNNTHPGP FPPTGGQSTA HPAAPTHHHH 

       490        500        510        520        530        540 
QQQPQQQHHH GNSGPPPPGA YPHPLESSNS HHAHPYNMSP SLGSLRPYPP GPAHLPPPHG 

       550        560        570        580        590        600 
QVSYNQAGPN GPPVSSSNSS GSSSQASYSC SHPSSSQGPQ GASYPFPPVP PVTTSSATLS 

       610        620        630        640        650        660 
TVIATVASSP AGYKTASPPG PPQYSKRAPS PGSYKTATPP GYKPGSPPSF RTGTPPGYRG 

       670        680        690        700        710        720 
TSPPAGPGTF KPGSPTVGPG PLPPAGPSSL SSLPPPPAAP TTGPPLTATQ IKQEPAEEYE 

       730        740        750        760        770        780 
PPESPVPPAR SPSPPPKVVD VPSHASQSAR FNKHLDRGFN SCARSDLYFV PLEGSKLAKK 

       790        800        810        820        830        840 
RADLVEKVRR EAEQRAREEK EREREREREK EREREKEREL ERSVKLAQEG RAPVECPSLG 

       850        860        870        880        890        900 
PVPHRPPFEP GSAVATVPPY LGPDTPALRT LSEYARPHVM SPGNRNHPFY VPLGAVDPGL 

       910        920        930        940        950        960 
LGYNVPALYS SDPAARERER EARERDLRDR LKPGFEVKPS ELEPLHGVPG PGLDPFPRHG 

       970        980        990       1000       1010       1020 
GLALQPGPPG LHPFPFHPSL GPLERERLAL AAGPALRPDM SYAERLAAER QHAERVAALG 

      1030       1040       1050       1060       1070       1080 
NDPLARLQML NVTPHHHQHS HIHSHLHLHQ QDAIHAASAS VHPLIDPLAS GSHLTRIPYP 

      1090       1100       1110       1120       1130       1140 
AGTLPNPLLP HPLHENEVLR HQLFAAPYRD LPASLSAPMS AAHQLQAMHA QSAELQRLAL 

      1150       1160       1170 
EQQQWLHAHH PLHSVPLPAQ EDYYSHLKKE SDKPL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of murine homologue dentatorubral-pallidoluysian atrophy (DRPLA) cDNA: strong conservation of a polymorphic CAG repeat in the murine gene."
Oyake M., Onodera O., Shiroishi T., Takano H., Takahashi Y., Komonami R., Moriwaki K., Ikeuchi T., Igarashi S., Tanaka H., Tsuji S.
Genomics 40:205-207(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, POLYMORPHISM OF POLY-GLN REGION.
[2]"Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6."
Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.
Genome Res. 8:29-40(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[5]"Nuclear receptor TLX prevents retinal dystrophy and recruits the corepressor atrophin1."
Zhang C.L., Zou Y., Yu R.T., Gage F.H., Evans R.M.
Genes Dev. 20:1308-1320(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2E1, FUNCTION.
[6]"Severe neurological phenotypes of Q129 DRPLA transgenic mice serendipitously created by en masse expansion of CAG repeats in Q76 DRPLA mice."
Sato T., Miura M., Yamada M., Yoshida T., Wood J.D., Yazawa I., Masuda M., Suzuki T., Shin R.M., Yau H.J., Liu F.C., Shimohata T., Onodera O., Ross C.A., Katsuki M., Takahashi H., Kano M., Aosaki T., Tsuji S.
Hum. Mol. Genet. 18:723-736(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERISTICS OF THE MOUSE MODEL OF DRPLA.
[7]"Atrophin proteins interact with the Fat1 cadherin and regulate migration and orientation in vascular smooth muscle cells."
Hou R., Sibinga N.E.
J. Biol. Chem. 284:6955-6965(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FAT1, INDUCTION, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D87744 mRNA. Translation: BAA13450.1.
AC002397 Genomic DNA. Translation: AAC36003.1.
CH466523 Genomic DNA. Translation: EDK99754.1.
CH466523 Genomic DNA. Translation: EDK99755.1.
BC050920 mRNA. Translation: AAH50920.2.
BC053051 mRNA. Translation: AAH53051.1.
CCDSCCDS20526.1.
RefSeqNP_031907.2. NM_007881.4.
UniGeneMm.333380.

3D structure databases

ProteinModelPortalO35126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199314. 2 interactions.

PTM databases

PhosphoSiteO35126.

Proteomic databases

PaxDbO35126.
PRIDEO35126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000088357; ENSMUSP00000085695; ENSMUSG00000004263.
ENSMUST00000129411; ENSMUSP00000115407; ENSMUSG00000004263.
GeneID13498.
KEGGmmu:13498.
UCSCuc009drq.1. mouse.

Organism-specific databases

CTD1822.
MGIMGI:104725. Atn1.

Phylogenomic databases

eggNOGNOG331121.
GeneTreeENSGT00580000081398.
HOGENOMHOG000231091.
HOVERGENHBG075369.
InParanoidO35126.
KOK05626.
OMAGPEKGPT.
OrthoDBEOG7D59MN.
PhylomeDBO35126.
TreeFamTF328554.

Gene expression databases

ArrayExpressO35126.
BgeeO35126.
GenevestigatorO35126.

Family and domain databases

InterProIPR017993. Atrophin-1.
IPR002951. Atrophin-like.
[Graphical view]
PfamPF03154. Atrophin-1. 2 hits.
[Graphical view]
PRINTSPR01222. ATROPHIN.
ProtoNetSearch...

Other

ChiTaRSATN1. mouse.
NextBio284033.
PROO35126.
SOURCESearch...

Entry information

Entry nameATN1_MOUSE
AccessionPrimary (citable) accession number: O35126
Secondary accession number(s): P70200, Q80YQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot