ATX7_MOUSE
ID ATX7_MOUSE Reviewed; 867 AA.
AC Q8R4I1; E9QPX9; Q8BL17;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ataxin-7;
DE AltName: Full=Spinocerebellar ataxia type 7 protein homolog;
GN Name=Atxn7; Synonyms=Sca7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=12039035; DOI=10.1016/s0378-1119(02)00399-2;
RA Stroem A.-L., Jonasson J., Hart P., Braennstroem T., Forsgren L.,
RA Holmberg M.;
RT "Cloning and expression analysis of the murine homolog of the
RT spinocerebellar ataxia type 7 (SCA7) gene.";
RL Gene 285:91-99(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP INTERACTION WITH CRX.
RX PubMed=11580893; DOI=10.1016/s0896-6273(01)00422-6;
RA La Spada A.R., Fu Y.-H., Sopher B.L., Libby R.T., Wang X., Li L.Y.,
RA Einum D.D., Huang J., Possin D.E., Smith A.C., Martinez R.A., Koszdin K.L.,
RA Treuting P.M., Ware C.B., Hurley J.B., Ptacek L.J., Chen S.;
RT "Polyglutamine-expanded ataxin-7 antagonizes CRX function and induces cone-
RT rod dystrophy in a mouse model of SCA7.";
RL Neuron 31:913-927(2001).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Involved in neurodegeneration. Acts as component of the STAGA
CC transcription coactivator-HAT complex. Mediates the interaction of
CC STAGA complex with the CRX and is involved in CRX-dependent gene
CC activation (By similarity). Necessary for microtubule cytoskeleton
CC stabilization (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the STAGA transcription coactivator-HAT complex,
CC at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L,
CC TAD1L, TAF10, TAF12, TRRAP, TAF9 and ATXN7. The STAGA core complex is
CC associated with a subcomplex required for histone deubiquitination
CC composed of ATXN7L3, ENY2 and USP22. Interacts with SORBS1, PSMC1 and
CC CRX. Interacts with TRRAP, GCN5L2 and TAF10 (By similarity). Interacts
CC with alpha tubulin (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8R4I1; Q80YV3: Trrap; NbExp=3; IntAct=EBI-7990748, EBI-2942477;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus, nucleolus
CC {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=In addition to a diffuse distribution throughout
CC the nucleus, it is associated with the nuclear matrix and the
CC nucleolus. It is able to shuttle between the nucleus and cytoplasm (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues, with the highest
CC expression in heart, brain, liver and kidney.
CC -!- PTM: Proteolytically cleaved. {ECO:0000250}.
CC -!- PTM: Sumoylation has no effect on subcellular location or interaction
CC with components of the STAGA complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ataxin-7 family. {ECO:0000305}.
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DR EMBL; AF455111; AAL84238.1; -; mRNA.
DR EMBL; AK046679; BAC32834.1; -; mRNA.
DR EMBL; AC116479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS26823.1; -.
DR RefSeq; NP_631973.3; NM_139227.4.
DR AlphaFoldDB; Q8R4I1; -.
DR BMRB; Q8R4I1; -.
DR SMR; Q8R4I1; -.
DR BioGRID; 232871; 2.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR DIP; DIP-29176N; -.
DR IntAct; Q8R4I1; 4.
DR MINT; Q8R4I1; -.
DR STRING; 10090.ENSMUSP00000022257; -.
DR iPTMnet; Q8R4I1; -.
DR PhosphoSitePlus; Q8R4I1; -.
DR MaxQB; Q8R4I1; -.
DR PaxDb; Q8R4I1; -.
DR PRIDE; Q8R4I1; -.
DR ProteomicsDB; 277229; -.
DR Antibodypedia; 7629; 168 antibodies from 32 providers.
DR DNASU; 246103; -.
DR Ensembl; ENSMUST00000022257; ENSMUSP00000022257; ENSMUSG00000021738.
DR Ensembl; ENSMUST00000223880; ENSMUSP00000152934; ENSMUSG00000021738.
DR GeneID; 246103; -.
DR KEGG; mmu:246103; -.
DR UCSC; uc007sgi.2; mouse.
DR CTD; 6314; -.
DR MGI; MGI:2179277; Atxn7.
DR VEuPathDB; HostDB:ENSMUSG00000021738; -.
DR eggNOG; KOG4140; Eukaryota.
DR GeneTree; ENSGT00940000157279; -.
DR HOGENOM; CLU_014451_1_0_1; -.
DR InParanoid; Q8R4I1; -.
DR OMA; PFVHHQP; -.
DR PhylomeDB; Q8R4I1; -.
DR TreeFam; TF331337; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 246103; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Atxn7; mouse.
DR PRO; PR:Q8R4I1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8R4I1; protein.
DR Bgee; ENSMUSG00000021738; Expressed in ganglion of central nervous system and 235 other tissues.
DR ExpressionAtlas; Q8R4I1; baseline and differential.
DR Genevisible; Q8R4I1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000124; C:SAGA complex; IC:ComplexPortal.
DR GO; GO:0033276; C:transcription factor TFTC complex; IC:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0016578; P:histone deubiquitination; ISO:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR InterPro; IPR030706; ATXN7.
DR InterPro; IPR013243; SCA7_dom.
DR PANTHER; PTHR15117:SF2; PTHR15117:SF2; 1.
DR Pfam; PF08313; SCA7; 1.
DR PROSITE; PS51505; SCA7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Isopeptide bond; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..867
FT /note="Ataxin-7"
FT /id="PRO_0000064760"
FT DOMAIN 320..387
FT /note="SCA7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00838"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15265"
FT CONFLICT 110
FT /note="R -> H (in Ref. 1; AAL84238)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..178
FT /note="LPS -> FPP (in Ref. 1; AAL84238)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="V -> A (in Ref. 1; AAL84238)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="S -> L (in Ref. 1; AAL84238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 867 AA; 92697 MW; D12908CFD3257A4A CRC64;
MSERAADDVR GEPRRAAGGA AAARQQQQQP QPLQPQRQHP PLRRPRAEDG GTGDTTTSAA
AMATVGERRP LPSPEAMLGQ SWNLWVEASK LPGKDGTELD ESFKEFGKNR EVMGLCREDM
PIFGLCPAHD DFYLVVCNDC NQVVKPQAFQ SHYERRHSSS SKPALAVPHT SVFSLLPSLS
KSKGSGAGGS SRPPSGGVLC ASSSSKLLRL PKEKLPLRGN MKPMHPVQQI KVPHGRVMTP
SVKVEKMHPK MDGTLLKSTV GPACPATMSS AVKPGLNCPS IPKPTLPSPG QILNGKGLPA
MPTLEKKSED SSNNRKFLNK RLSEREFDPD IHCGVIDLDT KKPCTRSLTC KTHSLTQRRA
VQGRRKRFDV LLAEHKNKAR EKELIRHDSQ QVPHPLRDPH PTPPRTPQEP QLPAESKPFL
ASKPKPQTPS LPRPPGCPAQ QGGSTPIDPP PGQESPHPPL PATEPASRLS SEEGEGDDRE
ESVEKLDCHY SGRHPQPASF CTFGSRQIGR GYYVFDSRWN RLRCALNLMV EKHLNAQLWK
KIPPVPCTTS PVSARVPHRT NSVPTSQGGI SYLAATTVSA PPVLLSSTCI SPNSKSVPAH
GTTLNAQPAG SGAMDPVCSV QSRQVSASSS PPSTPSGLSS VPSSPLSRKP QKWKPSKSIR
PKESSALSTN CHNASSSTSG GSGKKRKNSS PLLVPSSSSS SSSSSSSSHS VNSFRKNCVA
HSGTPYLSTA PSSHSIGLNC VTNKTHSVSL RHEQAGRGPA GVSSAEPIKR MSVMVNSSDS
TLSLGPFIHQ ASELPVNPHS HTPLDKLIGK KRKCSPGSST VGNSGSKPTK VAKLPAMNNV
HMKHTGNISG AQGLTNNSLL HQPKARP
