ID A0A2K6QYE5_RHIRO Unreviewed; 400 AA.
AC A0A2K6QYE5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ECO:0000313|Ensembl:ENSRROP00000033807.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000033807.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000033807.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 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:0000256|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: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 together with the
CC C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the
CC SAGA deubiquitination module. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_010352262.1; XM_010353960.1.
DR AlphaFoldDB; A0A2K6QYE5; -.
DR STRING; 61622.ENSRROP00000033807; -.
DR Ensembl; ENSRROT00000058248.1; ENSRROP00000033807.1; ENSRROG00000040467.1.
DR GeneID; 104654711; -.
DR CTD; 56970; -.
DR GeneTree; ENSGT00940000158253; -.
DR OMA; PSNYENM; -.
DR OrthoDB; 5404108at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000124; C:SAGA complex; IEA:UniProtKB-UniRule.
DR GO; GO:0030374; F:nuclear receptor 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 GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
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:SF1; ATAXIN-7-LIKE PROTEIN 3; 1.
DR Pfam; PF08313; SCA7; 1.
DR Pfam; PF08209; Sgf11; 1.
DR PROSITE; PS51505; SCA7; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, 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:UP000233200};
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|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_03047}.
FT DOMAIN 249..316
FT /note="SCA7"
FT /evidence="ECO:0000259|PROSITE:PS51505"
FT ZN_FING 137..158
FT /note="SGF11-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03047"
FT REGION 169..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 44412 MW; E3A35F27E4303CDB CRC64;
MPGLSSGQRG GRAGGRLQRC LGLTTTPPPP CVQPCCRPLC YEQSERRLHK SLQMKMEEMS
LSGLDNSKLE AIAQEIYADL VEDSCLGFCF EVHRAVKCGY FFLDDTDPDS MKDFEIVDQP
GLDIFGQVFN QWKSKECVCP NCSRSIAASR FAPHLEKCLG MGRNSSRIAN RRIANSNNMN
KSESDQEDND DINDNDWSYG SEKKAKKRKS DKNPNSPRRS KSLKHKNGEL SNSDPFKYNN
STGISYETLG PEELRSLLTT QCGVISEHTK KMCTRSLRCP QHTDEQRRTV RIYFLGPSAV
LPEVESSLDN DSFDMTDSQA LISRLQWDGS SDLSPSDSGS SKTSENQGWG LGTNSSESRK
TKKKKSHLSL VGTASGLGSN KKKKPKPPAP PTPSIYDDIN
//
