ID A0A1S3GHI5_DIPOR Unreviewed; 373 AA.
AC A0A1S3GHI5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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:0000313|RefSeq:XP_012887472.1};
GN Synonyms=ATXN7L3 {ECO:0000256|HAMAP-Rule:MF_03047};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012887472.1};
RN [1] {ECO:0000313|RefSeq:XP_012887472.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012887472.1};
RG RefSeq;
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 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}.
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DR RefSeq; XP_012887472.1; XM_013032018.1.
DR AlphaFoldDB; A0A1S3GHI5; -.
DR GeneID; 105997559; -.
DR KEGG; dord:105997559; -.
DR CTD; 56970; -.
DR InParanoid; A0A1S3GHI5; -.
DR OrthoDB; 5404108at2759; -.
DR Proteomes; UP000081671; 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 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:UP000081671};
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 222..289
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..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 41529 MW; C65B7E4B7FCEA4C2 CRC64;
MKMEEMSLSG LDNSKLEAIA QEIYADLVED SCLGFCFEVH RAVKCGYFFL DDTDPESMKD
FEIVDQPGLD IFGQVFNQWK SKECVCPNCS RSIAASRFAP HLEKCLGMGR NSSRIANRRI
ANSNNMNKSE SDQEDNDDIN DNDWSYGSEK KAKKRKSDKL WYLPFQNPNS PRRSKSLKHK
NGFSVCTSAS NTLPLLFSSS GELSNSDPFK YSNSSGISYE TLGPEELRSL LTTQCGVISE
HTKKMCTRSL RCPQHTDEQR RTVRIYFLGP SAVLPEVESS LDNDSFDMTD SQALISRLQW
DGSSDLSPSD SGSSKTSENQ GWGLGTNSSE SRKTKKKKSH LSLVGTASNL GSNKKKKPKP
PAPPTPSIYD DIN
//
