ID A0A3Q2EBE7_CYPVA Unreviewed; 359 AA.
AC A0A3Q2EBE7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000029004.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000029004.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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_015227557.1; XM_015372071.1.
DR AlphaFoldDB; A0A3Q2EBE7; -.
DR STRING; 28743.ENSCVAP00000029004; -.
DR Ensembl; ENSCVAT00000021578.1; ENSCVAP00000029004.1; ENSCVAG00000016451.1.
DR GeneID; 107083096; -.
DR KEGG; cvg:107083096; -.
DR CTD; 368510; -.
DR GeneTree; ENSGT00940000158253; -.
DR OMA; PSNYENM; -.
DR OrthoDB; 5404108at2759; -.
DR Proteomes; UP000265020; Unplaced.
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 GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule.
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:SF4; 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:UP000265020};
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 200..267
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 123..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..359
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 315..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 39891 MW; D614469330D20C5C CRC64;
MKMEEKPLSG PDNTRLEALV QDIYSELVED ACLGLCFEVH RAVKQGYFFL DETDQDSIKE
FEIVDQPGVD IFGQVFNQWK NKECECPNCK RLIAASRFAP HLEKCLGMGR NSSRIANRRL
ASNNNISKSE SDQEDNDDLN DNDWSYGAEK KSKKRRSDKN QNSPRRSKSL KHKNGELGTS
ISSDPYKPYN YNTGVSYESL GPNEVRLLLT TQCGVISEHT KKMCTRSHRC PQHTDDQRRA
IRLYLLGPSA LTLPDADVGG DCFDVPTDGQ ALLSRMQWED SPDISPSDSA SSKASTNHSD
SRRPKKKKKS ALSMNSGGGG VNLTGVGSSS FQSNISLSTK KKKPKTAAPL VPSIYDQLN
//
