ATN1_PANTR
ID ATN1_PANTR Reviewed; 1186 AA.
AC Q5IS70;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Atrophin-1;
DE AltName: Full=Dentatorubral-pallidoluysian atrophy protein homolog;
GN Name=ATN1; Synonyms=DRPLA;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
CC -!- FUNCTION: Transcriptional corepressor. Corepressor of MTG8
CC transcriptional repression. Recruits NR2E1 to repress transcription.
CC Has some intrinsic repression activity. Promotes vascular smooth cell
CC (VSMC) migration and orientation (By similarity).
CC {ECO:0000250|UniProtKB:O35126}.
CC -!- SUBUNIT: Interacts with NR2E1; the interaction represses the
CC transcriptional activity of NR2E1. Interacts with BAIAP2, WWP1, WWP2,
CC WWP3 and RERE. Interacts (via its N-terminus) with MTG8; the
CC interaction enhances transcriptional repression of MTG8. Interacts with
CC FAT1 (via a C-terminal domain). Interacts with PQBP1 (By similarity).
CC {ECO:0000250|UniProtKB:P54259}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54258}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P54258}. Cell
CC junction {ECO:0000250|UniProtKB:P54258}. Note=Shuttles between nucleus
CC and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-
CC cell junctions and leading edges of cells. Colocalizes with MTG8 in
CC discrete nuclear dots (By similarity). {ECO:0000250|UniProtKB:O35126,
CC ECO:0000250|UniProtKB:P54258}.
CC -!- PTM: Phosphorylated in vitro by MAPK8/JNK1 on Ser-735. {ECO:0000250}.
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DR EMBL; AY665258; AAV74296.1; -; mRNA.
DR RefSeq; NP_001029337.1; NM_001034165.1.
DR RefSeq; XP_016778060.1; XM_016922571.1.
DR AlphaFoldDB; Q5IS70; -.
DR SMR; Q5IS70; -.
DR STRING; 9598.ENSPTRP00000060554; -.
DR PaxDb; Q5IS70; -.
DR GeneID; 451803; -.
DR KEGG; ptr:451803; -.
DR CTD; 1822; -.
DR eggNOG; KOG2133; Eukaryota.
DR InParanoid; Q5IS70; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR InterPro; IPR017993; Atrophin-1.
DR InterPro; IPR002951; Atrophin-like.
DR Pfam; PF03154; Atrophin-1; 2.
DR PRINTS; PR01222; ATROPHIN.
PE 2: Evidence at transcript level;
KW Acetylation; Cell junction; Cytoplasm; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1186
FT /note="Atrophin-1"
FT /id="PRO_0000064731"
FT REGION 1..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..563
FT /note="Involved in binding BAIAP2"
FT /evidence="ECO:0000250"
FT REGION 618..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..890
FT /note="Required for interaction with FAT1"
FT /evidence="ECO:0000250"
FT MOTIF 16..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 1029..1037
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..601
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..750
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 637
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 649
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 665
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 735
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 1111
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35126"
FT CROSSLNK 1179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P54259"
SQ SEQUENCE 1186 AA; 124902 MW; 9EA09E863EAAA58A CRC64;
MKTRQNKDSM SMRSGRKKEA PGPREELRSR GRASPGGVST SSSDGKAEKS RQTAKKARVE
EASTPKVNKQ GRSEEISESE SEETNAPKKT KTEELPRPQS PSDLDSLDGR SLNDDGSSDP
RDIDQDNRST SPSIYSPGSV ENDSDSSSGL SQGPARPYHP PPLFPPSPQP PDSTPRQPEA
SFEPHPSVTP TGYHAPMEPP TSRMFQAPPG APPPHPQLYP GGTGGVLSGP PMGPKGGGAA
SSVGGPNGGK QHPPPTTPIS VSSSGASGAP PTKPPTTPVG GGNLPSAPPP ANFPHVTPNL
PPPPALRPLN NASASPPGLG AQPLPGHLPS PHAMGQGMGG LPPGPEKGPT LAPSPHSLPP
ASSSAPAPPM RFPYSSSSSS SAAASSSSSS SSSSASPFPA SQALPSYPHS FPPPTSLSVS
NQPPKYTQPS LPSQAVWSQG PPPPPPYGRL LANSNAHPGP FPPSTGAQST AHPPVSTHHH
HHQQQQQQQQ QQQQQQQQHH GNSGPPPPGA FPHPLEGGSS HHAHPYAMSP SLGSLRPYPP
GPAHLPPPHS QVSYSQAGPN GPPVSSSSNS SSSTSQGSYP CSHPSPSQGP QGAPYPFPPV
PTVTTSSATL STVIATVASS PAGYKTASPP GPPPYGKRAP SPGAYKTATP PGYKPGSPPS
FRTGTPPGYR GTSPPAGPGT FKPGSPTVGP GPLPPAGPSG LPSLPPPPAA PASGPPLSAT
QIKQEPAEEY ETPESPVPPA RSPSPPPKVV DVPSHASQSA RFNKHLDRGF NSCARSDLYF
VPLEGSKLAK KRADLVEKVR REAEQRAREE KERERERERE KEREREKERE LERSVKLAQE
GRAPVECPSL GPVPHRPPFE PGSAVATVPP YLGPDTPALR TLSEYARPHV MSPGNRNHPF
YVPLGAVDPG LLGYNVPALY SSDPAARERE REARERDLRD RLKPGFEVKP SELEPLHGVP
GPGLDPFPRH GGLALQPGPP GLHPFPFHPS LGPLERERLA LAAGPALRPD MSYAERLAAE
RQHAERVAAL GNDPLARLQM LNVTPHHHQH SHIHSHLHLH QQDAIHAASA SVHPLIDPLA
SGSHLTRIPY PAGTLPNPLL PHPLHENEVL RHQLFAAPYR DLPASLSAPM SAAHQLQAMH
AQSAELQRLA LEQQQWLHAH HPLHSVPLPA QEDYYSHLKK ESDKPL
