ATN1_RAT
ID ATN1_RAT Reviewed; 1183 AA.
AC P54258;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Atrophin-1;
DE AltName: Full=Dentatorubral-pallidoluysian atrophy protein homolog;
GN Name=Atn1; Synonyms=Drpla;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Cerebellum, and Corpus striatum;
RX PubMed=9173996; DOI=10.1006/nbdi.1995.0014;
RA Loev S.J., Margolis R.L., Young W.S., Li S.-H., Schilling G.,
RA Ashworth R.G., Ross C.A.;
RT "Cloning and expression of the rat atrophin-I (DRPLA disease gene)
RT homologue.";
RL Neurobiol. Dis. 2:129-138(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain, Cerebellum, Hippocampus, and Substantia nigra;
RX PubMed=8541849; DOI=10.1093/hmg/4.9.1619;
RA Schmitt I., Epplen J.T., Riess O.;
RT "Predominant neuronal expression of the gene responsible for dentatorubral-
RT pallidoluysian atrophy (DRPLA) in rat.";
RL Hum. Mol. Genet. 4:1619-1624(1995).
RN [3]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=19131340; DOI=10.1074/jbc.m809333200;
RA Hou R., Sibinga N.E.;
RT "Atrophin proteins interact with the Fat1 cadherin and regulate migration
RT and orientation in vascular smooth muscle cells.";
RL J. Biol. Chem. 284:6955-6965(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-79; SER-100 AND
RP SER-106, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional corepressor. Recruits NR2E1 to repress
CC transcription. Promotes vascular smooth cell (VSMC) migration and
CC orientation. Corepressor of MTG8 transcriptional repression. Has some
CC intrinsic repression activity (By similarity).
CC {ECO:0000250|UniProtKB:O35126}.
CC -!- SUBUNIT: Interacts with NR2E1; the interaction represses the
CC transcriptional activity of NR2E1. Interact (via its N-terminus) with
CC FAT1 (via a C-terminal domain). Interacts with BAIAP2, WWP1, WWP2, WWP3
CC and RERE. Interacts (via its N-terminus) with MTG8; the interaction
CC enhances transcriptional repression of MTG8. Interacts with PQBP1 (By
CC similarity). {ECO:0000250|UniProtKB:P54259}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19131340}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:19131340}. Cell junction
CC {ECO:0000269|PubMed:19131340}. Note=Shuttles between nucleus and
CC cytoplasm. Colocalizes with MTG8 in discrete nuclear dots (By
CC similarity). Colocalizes with FAT1 in the perinuclear area, at cell-
CC cell junctions and leading edges of cells.
CC {ECO:0000250|UniProtKB:O35126}.
CC -!- TISSUE SPECIFICITY: Predominant neuronal expression, Expressed in most
CC brain regions including striatum, hippocampus, cerebral cortex,
CC diencephalon, brain stem and cerebellum. Highest levels in cerebellum.
CC Also highly expressed in kidney and testis, low expression in skeletal
CC muscle and heart. {ECO:0000269|PubMed:9173996}.
CC -!- DEVELOPMENTAL STAGE: Similar expression at all development stages (14.5
CC dpc, 17.5 dpc, newborns and adults). {ECO:0000269|PubMed:8541849}.
CC -!- INDUCTION: Induced after vascular injury and by growth factors.
CC Decreased levels with INF-gamma. {ECO:0000269|PubMed:19131340}.
CC -!- PTM: Phosphorylated in vitro by MAPK8/JNK1 on Ser-732. {ECO:0000250}.
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DR EMBL; U31777; AAA80337.1; -; mRNA.
DR EMBL; X89453; CAA61623.1; -; Genomic_DNA.
DR AlphaFoldDB; P54258; -.
DR SMR; P54258; -.
DR IntAct; P54258; 1.
DR MINT; P54258; -.
DR STRING; 10116.ENSRNOP00000045475; -.
DR iPTMnet; P54258; -.
DR PhosphoSitePlus; P54258; -.
DR PaxDb; P54258; -.
DR PRIDE; P54258; -.
DR UCSC; RGD:61832; rat.
DR RGD; 61832; Atn1.
DR eggNOG; KOG2133; Eukaryota.
DR InParanoid; P54258; -.
DR PhylomeDB; P54258; -.
DR PRO; PR:P54258; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0008432; F:JUN kinase binding; IMP:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0090729; F:toxin activity; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0030011; P:maintenance of cell polarity; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0032094; P:response to food; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0009404; P:toxin metabolic process; ISO:RGD.
DR InterPro; IPR017993; Atrophin-1.
DR InterPro; IPR002951; Atrophin-like.
DR Pfam; PF03154; Atrophin-1; 2.
DR PRINTS; PR01222; ATROPHIN.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Cytoplasm; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1183
FT /note="Atrophin-1"
FT /id="PRO_0000064732"
FT REGION 1..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..560
FT /note="Involved in binding BAIAP2"
FT /evidence="ECO:0000250"
FT REGION 617..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..887
FT /note="Required for interaction with FAT1"
FT /evidence="ECO:0000250"
FT REGION 921..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 16..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 1026..1034
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..220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..711
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..747
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..836
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:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 634
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 646
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 662
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 732
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT MOD_RES 1108
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35126"
FT CROSSLNK 1176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P54259"
FT CONFLICT 455
FT /note="N -> S (in Ref. 2; CAA61623)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="F -> L (in Ref. 2; CAA61623)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="P -> R (in Ref. 2; CAA61623)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="T -> M (in Ref. 2; CAA61623)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="A -> V (in Ref. 2; CAA61623)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="Missing (in Ref. 2; CAA61623)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1183 AA; 124779 MW; 7FB9928DCADF9B1F CRC64;
MKTRQNKDSM SMRSGRKKEA PGPREELRSR GRASPGGVST SSSDGKAEKS RQTAKKARVE
ETSTPKANKQ GRSEEISESE SEETSAPKKT KTEELPRPQS PSDLDSLDGR SINDDGSSDP
RDIDQDNRST SPSIYSPGSV ENDSDSSSGL SQGPARPYHP PPLFPPSPPP PDSIPRQPES
GFEPHPSVPP TGYHAPMEPP TSRLFQGPPP GAPPPHPQLY PGSAGGGVLS GPPMGPKGGA
AASSVGPPSG GKQHPPPTTP IPISSSGASG APPAKPPNTP VGAGNLPSAP PPATFPHVTP
NLPPPPALRP LNNASASPPG MGAQPIPGHL PSPHAMGQGM SGLPPGPEKG PTLAPSPHPL
PPASSSAPGP PMRYPYSSCS SSSVAASSSS SAATSQYPAS QTLPSYPHSF PPPTSMSVSN
QPPKYTQPSL PSQAVWSQGP PPPPPPYGRL LPNNNTHPGP FPPTGGQSTA HPPAPAHHHH
QQQQQPQPQP QPQQHHHGNS GPPPPGAYPH PLESSNSHHA HPYNMSPSLG SLRPYPPGPA
HLPPSHGQVS YSQAGPNGPP VSSSSNSSGS SSQAAYSCSH PSSSQGPQGA SYPFPPVPPI
TTSSATLSTV IATVASSPAG YKTASPPGPP QYSKRAPSPG SYKTATPPGY KPGSPPSFRT
GTPPGYRGTS PPAGPGTFKP GSPTVGPGPL PPAGPSSLSS LPPPPAAPTT GPPLTATQIK
QEPAEEYETP ESPVPPARSP SPPPKVVDVP SHASQSARFN KHLDRGFNSC ARSDLYFVPL
EGSKLAKKRA DLVEKVRREA EQRAREEKER EREREREKER EREKERELER SVKLAQEGRA
PVECPSLGPV PHRPPFEPGS AVATVPPYLG PDTPALRTLS EYARPHVMSP GNRNHPFYVP
LGAVDPGLLG YNVPALYSSD PAAREREREA RERDLRDRLK PGFEVKPSEL EPLHGVPGPG
LDPFPRHGGL ALQPGPPGLH PFPFHPSLGP LERERLALAA GPALRPDMSY AERLAAERQH
AERVAALGND PLARLQMLNV TPHHHQHSHI HSHLHLHQQD AIHAASASVH PLIDPLASGS
HLTRIPYPAG TLPNPLLPHP LHENEVLRHQ LFAAPYRDLP ASLSAPMSAA HQLQAMHAQS
AELQRLALEQ QQWLHAHHPL HSVPLPAQED YYSHLKKESD KPL
