ID H2LBH2_ORYLA Unreviewed; 360 AA.
AC H2LBH2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Ataxin-7-like protein 3 {ECO:0000256|HAMAP-Rule:MF_03047};
DE AltName: Full=SAGA-associated factor 11 homolog {ECO:0000256|HAMAP-Rule:MF_03047};
GN Name=ATXN7L3 {ECO:0000256|HAMAP-Rule:MF_03047};
GN Synonyms=atxn7l3 {ECO:0000313|Ensembl:ENSORLP00000003245.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000003245.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000003245.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000003245.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000003245.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000003245.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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:0000256|HAMAP-Rule:MF_03047}.
CC -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT
CC complexes. Within the SAGA complex, participates to a subcomplex of
CC SAGA called the DUB module (deubiquitination module).
CC {ECO:0000256|HAMAP-Rule:MF_03047}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|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:0000256|HAMAP-Rule:MF_03047}.
CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of
CC the SAGA deubiquitination module. {ECO:0000256|HAMAP-Rule:MF_03047}.
CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000256|HAMAP-
CC Rule:MF_03047}.
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DR RefSeq; XP_004071299.1; XM_004071251.2.
DR AlphaFoldDB; H2LBH2; -.
DR Ensembl; ENSORLT00000003246.2; ENSORLP00000003245.2; ENSORLG00000002605.2.
DR GeneID; 101170517; -.
DR KEGG; ola:101170517; -.
DR CTD; 368510; -.
DR eggNOG; ENOG502QTTX; Eukaryota.
DR GeneTree; ENSGT00940000167574; -.
DR HOGENOM; CLU_066241_0_0_1; -.
DR OrthoDB; 5404108at2759; -.
DR TreeFam; TF324580; -.
DR Proteomes; UP000001038; Chromosome 8.
DR Bgee; ENSORLG00000002605; Expressed in testis and 14 other cell types or tissues.
DR GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000124; C:SAGA complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 6.10.140.1270; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR HAMAP; MF_03047; Sgf11; 1.
DR InterPro; IPR013246; SAGA_su_Sgf11.
DR InterPro; IPR013243; SCA7_dom.
DR PANTHER; PTHR46367; ATAXIN-7-LIKE PROTEIN 3; 1.
DR PANTHER; PTHR46367:SF2; ATAXIN-7-LIKE PROTEIN 3; 1.
DR Pfam; PF08209; Sgf11; 1.
DR PROSITE; PS51505; SCA7; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|HAMAP-Rule:MF_03047};
KW Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03047};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03047};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03047};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_03047};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_03047};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03047};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_03047}.
FT DOMAIN 199..266
FT /note="SCA7"
FT /evidence="ECO:0000259|PROSITE:PS51505"
FT ZN_FING 84..105
FT /note="SGF11-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03047"
FT REGION 116..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..360
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..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 39759 MW; 78368405DCC7B5A5 CRC64;
MKMEDMPLSG PDNTKLEALV NDIYSELVED ACLGLCFEVH RAVKQGYFFL DETDQESMKE
FEIVDQPGVD IFGQVYNQWK NKECECPNCK RLIAASRFAP HLEKCLGMGR NSSRIANRRL
ASNNNTSKSE SDQEDNDDLN DNDWSYGAEK RAKKRKSDKS QNSPRRSKTL KHKNGELGSS
MSADPYKYNY NAGINYEMLG PDEVRSFLTT QCGVISEHTK KMCTRSQRCP QHTDEQRMAV
RVFLLGPSAP VLPEADSVAG PESFDIPDGQ ALMSRLQWED SPEISPSDSA SSKASTNHSD
SRRPKKKKRP PLGLNSGGGI GSLSGGGGSG GSQTNISLST KKKKPKLTAP SISSIYDDLN
//