AT7L3_DANRE
ID AT7L3_DANRE Reviewed; 367 AA.
AC A1L209; Q1RM53; Q8JFU1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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; ORFNames=si:dz180g5.4, zgc:136438, zgc:158566;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 histone H2B. The SAGA complex is
CC recruited to specific gene promoters by activators, where it is
CC required for transcription. {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT
CC complexes. Within the SAGA complex, participates in a subcomplex of
CC SAGA called the DUB module (deubiquitination module) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03047}.
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 forms part of the
CC 'catalytic lobe' of the SAGA deubiquitination module.
CC {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=CAD43430.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL604064; CAD43430.2; ALT_SEQ; Genomic_DNA.
DR EMBL; BC115132; AAI15133.1; -; mRNA.
DR EMBL; BC129298; AAI29299.1; -; mRNA.
DR RefSeq; NP_001005396.1; NM_001005396.1.
DR RefSeq; NP_001035431.2; NM_001040341.2.
DR AlphaFoldDB; A1L209; -.
DR SMR; A1L209; -.
DR STRING; 7955.ENSDARP00000094893; -.
DR PaxDb; A1L209; -.
DR GeneID; 368510; -.
DR KEGG; dre:368510; -.
DR CTD; 368510; -.
DR ZFIN; ZDB-GENE-030616-253; atxn7l3a.
DR eggNOG; ENOG502QTTX; Eukaryota.
DR InParanoid; A1L209; -.
DR OrthoDB; 1244885at2759; -.
DR PhylomeDB; A1L209; -.
DR PRO; PR:A1L209; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0071819; C:DUBm complex; IBA:GO_Central.
DR GO; GO:0000124; C:SAGA complex; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Activator; Chromatin regulator; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..367
FT /note="Ataxin-7-like protein 3"
FT /id="PRO_0000367517"
FT DOMAIN 199..266
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 280..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 85
FT /note="V -> I (in Ref. 2; AAI15133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40720 MW; C6D3FD63682C723B CRC64;
MKMEDMSLSG LDNTKLEALA HDVYSDLVED ACLGLCFEVH RAVKQGYFFL DETDQESMKD
FEIVDQPGVD IFGQVYNQWK NKECVCPNCS RSIAASRFAP HLEKCLGMGR NSSRIANRRI
ASSNNTSKSE SDQEDNDDIN DNDWSYGSEK KAKKRKSEKN PNSPRRSKSL KHKNGELSGS
VNPDMYKYNY SSGISYETLG PEELRSILTT QCGVVSEHTK KMCTRSQRCP QHTDEQRRAV
RVFLLGPSAS TLPDADTMLE NEAYEPPDGQ LIMSRLHWDA SSDISPSDSA SSKASTNNSE
SKRPKKKKPS TLSLTPAGER DKAQERDRIA GSGSSGSSSQ NALGLSSRKK RPKLAVPPAP
SIYDDLN
