AT7L3_MOUSE
ID AT7L3_MOUSE Reviewed; 347 AA.
AC A2AWT3; A2AWT2; A2AWT4; Q8C1T7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ataxin-7-like protein 3 {ECO:0000255|HAMAP-Rule:MF_03047};
DE AltName: Full=SAGA-associated factor 11 homolog {ECO:0000255|HAMAP-Rule:MF_03047};
GN Name=Atxn7l3;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-308 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the transcription regulatory histone acetylation
CC (HAT) complex SAGA, a multiprotein complex that activates transcription
CC by remodeling chromatin and mediating histone acetylation and
CC deubiquitination. Within the SAGA complex, participates in a subcomplex
CC that specifically deubiquitinates both histones H2A and H2B. The SAGA
CC complex is recruited to specific gene promoters by activators such as
CC MYC, where it is required for transcription. Required for nuclear
CC receptor-mediated transactivation. Within the complex, it is required
CC to recruit USP22 and ENY2 into the SAGA complex. Regulates H2B
CC monoubiquitination (H2Bub1) levels. Affects subcellular distribution of
CC ENY2, USP22 and ATXN7L3B. {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT
CC complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H,
CC TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3,
CC and USP22 form an additional subcomplex of SAGA called the DUB module
CC (deubiquitination module). Interacts directly with ENY2 and USP22.
CC {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AWT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AWT3-2; Sequence=VSP_036728;
CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of
CC the SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- DOMAIN: The C-terminal SGF11-type zinc-finger domain together with the
CC C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the
CC SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000255|HAMAP-
CC Rule:MF_03047}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM25078.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL954730; CAM25078.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL954730; CAM25079.1; -; Genomic_DNA.
DR EMBL; AL954730; CAM25080.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34107.1; -; Genomic_DNA.
DR EMBL; AK090368; BAC41186.1; -; mRNA.
DR CCDS; CCDS48941.1; -. [A2AWT3-1]
DR CCDS; CCDS48942.1; -. [A2AWT3-2]
DR RefSeq; NP_001092306.1; NM_001098836.1. [A2AWT3-2]
DR RefSeq; NP_001092307.1; NM_001098837.1. [A2AWT3-1]
DR AlphaFoldDB; A2AWT3; -.
DR BMRB; A2AWT3; -.
DR SMR; A2AWT3; -.
DR BioGRID; 229867; 1.
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 IntAct; A2AWT3; 2.
DR MINT; A2AWT3; -.
DR STRING; 10090.ENSMUSP00000072967; -.
DR iPTMnet; A2AWT3; -.
DR PhosphoSitePlus; A2AWT3; -.
DR EPD; A2AWT3; -.
DR MaxQB; A2AWT3; -.
DR PaxDb; A2AWT3; -.
DR PeptideAtlas; A2AWT3; -.
DR PRIDE; A2AWT3; -.
DR ProteomicsDB; 265129; -. [A2AWT3-1]
DR ProteomicsDB; 265130; -. [A2AWT3-2]
DR Antibodypedia; 54391; 87 antibodies from 24 providers.
DR Ensembl; ENSMUST00000073234; ENSMUSP00000072967; ENSMUSG00000059995. [A2AWT3-1]
DR Ensembl; ENSMUST00000107132; ENSMUSP00000102750; ENSMUSG00000059995. [A2AWT3-2]
DR Ensembl; ENSMUST00000107134; ENSMUSP00000102752; ENSMUSG00000059995. [A2AWT3-1]
DR GeneID; 217218; -.
DR KEGG; mmu:217218; -.
DR UCSC; uc007lrg.1; mouse. [A2AWT3-2]
DR UCSC; uc007lrh.1; mouse. [A2AWT3-1]
DR CTD; 56970; -.
DR MGI; MGI:3036270; Atxn7l3.
DR VEuPathDB; HostDB:ENSMUSG00000059995; -.
DR eggNOG; KOG2612; Eukaryota.
DR GeneTree; ENSGT00940000158253; -.
DR HOGENOM; CLU_066241_0_0_1; -.
DR InParanoid; A2AWT3; -.
DR OMA; PSNYENM; -.
DR OrthoDB; 1244885at2759; -.
DR PhylomeDB; A2AWT3; -.
DR TreeFam; TF324580; -.
DR BioGRID-ORCS; 217218; 18 hits in 73 CRISPR screens.
DR ChiTaRS; Atxn7l3; mouse.
DR PRO; PR:A2AWT3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2AWT3; protein.
DR Bgee; ENSMUSG00000059995; Expressed in primary motor cortex and 250 other tissues.
DR ExpressionAtlas; A2AWT3; baseline and differential.
DR Genevisible; A2AWT3; MM.
DR GO; GO:0071819; C:DUBm complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000124; C:SAGA complex; ISS:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IC:ComplexPortal.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; ISO:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0010390; P:histone monoubiquitination; ISS:UniProtKB.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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 HAMAP; MF_03047; Sgf11; 1.
DR InterPro; IPR013246; SAGA_su_Sgf11.
DR InterPro; IPR013243; SCA7_dom.
DR Pfam; PF08313; SCA7; 1.
DR Pfam; PF08209; Sgf11; 1.
DR PROSITE; PS51505; SCA7; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromatin regulator; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..347
FT /note="Ataxin-7-like protein 3"
FT /id="PRO_0000367516"
FT DOMAIN 196..263
FT /note="SCA7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT ZN_FING 84..105
FT /note="SGF11-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT REGION 116..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CW9"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CW9"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CW9"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CW9"
FT VAR_SEQ 159
FT /note="K -> KLWYLPFQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036728"
SQ SEQUENCE 347 AA; 38594 MW; EB5A4DC807B674D0 CRC64;
MKMEEMSLSG LDNSKLEAIA QEIYADLVED SCLGFCFEVH RAVKCGYFFL DDTDPDSMKD
FEIVDQPGLD IFGQVFNQWK SKECVCPNCS RSIAASRFAP HLEKCLGMGR NSSRIANRRI
ANSNNMNKSE SDQEDNDDIN DNDWSYGSEK KAKKRKSDKN PNSPRRSKSL KHKNGELSNS
DPFKYSNSTG ISYETLGPEE LRSLLTTQCG VISEHTKKMC TRSLRCPQHT DEQRRTVRIY
FLGPSAVLPE VESSLDNDGF DMTDSQALIS RLQWDGSSDL SPSDSGSSKT SENQGWGLGT
NSSESRKTKK KKSHLSLVGT ASGLGSNKKK KPKPPAPPTP SIYDDIN
