ID A0A091D2P6_FUKDA Unreviewed; 1806 AA.
AC A0A091D2P6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ORFNames=H920_13347 {ECO:0000313|EMBL:KFO25262.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO25262.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO25262.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO25262.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362035}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362035}. Nucleus {ECO:0000256|HAMAP-
CC 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 -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000256|ARBA:ARBA00010993, ECO:0000256|RuleBase:RU362035}.
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DR EMBL; KN123381; KFO25262.1; -; Genomic_DNA.
DR STRING; 885580.ENSFDAP00000000781; -.
DR eggNOG; KOG1172; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000124; C:SAGA complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
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 CDD; cd21998; HMG-box_UBF1_rpt1-like; 1.
DR CDD; cd22002; HMG-box_UBF1_rpt5; 1.
DR CDD; cd22003; HMG-box_UBF1_rpt6-like; 1.
DR Gene3D; 6.10.140.1270; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 3.
DR HAMAP; MF_03047; Sgf11; 1.
DR InterPro; IPR018241; Anion_exchange_CS.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR029215; HMG_box_5.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR013246; SAGA_su_Sgf11.
DR InterPro; IPR013243; SCA7_dom.
DR NCBIfam; TIGR00834; ae; 1.
DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR PANTHER; PTHR11453:SF12; BAND 3 ANION TRANSPORT PROTEIN; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 2.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF14887; HMG_box_5; 1.
DR Pfam; PF08313; SCA7; 1.
DR Pfam; PF08209; Sgf11; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SMART; SM00398; HMG; 3.
DR SUPFAM; SSF47095; HMG-box; 3.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
DR PROSITE; PS50118; HMG_BOX_2; 3.
DR PROSITE; PS51505; SCA7; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|HAMAP-Rule:MF_03047};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03047};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU362035};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362035};
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:UP000028990};
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362035};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362035};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362035};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03047};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_03047}.
FT TRANSMEM 547..570
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 582..613
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 633..658
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 665..686
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 706..727
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 743..763
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 801..819
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 840..863
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 900..919
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 926..945
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 1075..1143
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1250..1320
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1339..1405
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1655..1722
FT /note="SCA7"
FT /evidence="ECO:0000259|PROSITE:PS51505"
FT DNA_BIND 1075..1143
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT DNA_BIND 1250..1320
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT DNA_BIND 1339..1405
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT ZN_FING 1543..1564
FT /note="SGF11-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03047"
FT REGION 126..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1435
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1806 AA; 203460 MW; 0127244FABC6BAE0 CRC64;
MELSKPQPDC CCAMRPLFRL MQPYPGASVC HCDDWQELSL GQTDSSGFCG HSQVLKTLLC
QHVARATGML LETLGHPTRP PSPPHLDSGA CWWQPGWDAQ LGRGSYQAGQ EQLPRALECA
KAPCTPGPSA WDGSHGTTGG QEDFGAGLAA PAEQPGEEVL DIPEHARHRE DRAQDREMPG
NLDHEEGLEE ALDLEDYEDL GIPKPQEEEL QALPSAEPTA SDYVPAKPQP GTQEVYVQLQ
ELSMDGKNAE LQWAEVAHWM RVEENVGPRG SWGRPHVSYL TFWSLLQLQR AFAKGTVLLD
LQERSLAGVV DELLDRLIFE DRIRPEDRTP LHRALLLRCS HAQDQEALEG VTPAVLTRSG
DPHTPLLSSQ PSLETKFFCE KGEGDPEVRL ASAVLEQIPE ASESALLRVG RADFLEQPVL
AFVRLQEAAE LESVELPRPV RFLAVLLGPE QLHTDYTQLG RALATLMSER VFRMDAYLAQ
SRGELVRSLD SFLDCSLVLP PTDAPSERAL LGLLPRTGQL FGGLVRDVRR RYPYYLSDIR
DALSPQVLAA VIFIYFAALS PAITFGGLLG EKTGNQMGVS ELLISTAVQG IVFALLGAQP
LLVLGFSGPL LVFEDAFFLF CESHGLEYIV GRAWIGFWLI LLVLLVVAFE GSFLVRFISR
YTQEIFSFLI SLIFIYETFS KLIKIFQDHP LQKTYDPKVT KPRGPLPNTA LFSLVLMAGT
FILAMMLRKL KNSSYFPGKL RRVIGDFGVP ISILIMVLVD SFIKDTYTQK LSVPDGLKVS
NASARGWVIH PLGLYRLFPT WMMFASALPA LLVFILIFLE SQITTLIVSK PERKMTKGSG
FHLDLLLVVG MGGVAALFGM PWLSATTVRS VTHANALTVM GKASTPGAAA QIQEVKEQRI
SGLLVSVLVG LSILMEPVLS RIPLAVLFGI FLYMGVTSLS GIQLFDRILL LLKPAKYHPD
LPFVKRADVS FQKQHVCCTA QRHRWSQEDM LTLLECMKNN LPSNDSSKFK TTESHMDWEK
VAFKDFSGDM CKLKWVEISN EVRKFRTLTE LILDAQEHVK NPYKGKKLKK HPDFPKKPLT
PYFRFFMEKR AKYAKLHPEM SNLDLTKILS KKYKELPEKK KMKYIQDFQR EKQEFERNLA
RFREDHPDLI QNAKKSDIPE KPKTPQQLWY THEKKVYLKV RPDEIMRDYI QKHPELNISE
EGITKSTLTK AERQLKDKFD GRPTKPPPRS QARAGQGPPG TEREDRGKLP ESPKRAEEIW
QQSVIGDYLA RFKVGTNDRV KALKAMEMTW NNMEKKEKLM WIKKAAEDQK RYERELSEMR
APPAAANSSK KMKFQGEPKK PPMNGYQKFS QELLSNGELN HLPLKERMVE IGSRWQRISQ
SQKEHYKKLA EEQQKQYKVH LDLWVKESEE EDDEDDEDDE EDDDEDDGEN GDSSEDGGDS
SDRPLCYEQS ERRLHKSLQM KMEEMSLSGL DNSKLEAIAQ EIYADLVEDS CLGFCFEVHR
AVKCGYFFLD DTDPDSMKDF EIVDQPGLDI FGQVFNQWKS KECVCPNCSR SIAASRFAPH
LEKCLGMGRN SSRIANRRIA SSNSVNKSES DQEDNDDVND NDWSYGSEKR AKKRKSDKNP
NSPRRSKSLK HKNGELSNSD PFKYSNSMGI SYETLGPEEL RSLLTTQCGV ISEHTKKMCT
RSLRCPQHTD EQRRTVRIYF LGPSAVLPEV ESSLDTDSFD IADNQALLSR LQWDGSSDLS
PSDSGSSKTS DNQGWGLGTN SSESRKTKKK KSHLSLVGAA SALGSSKKKR PKPPAPPTPS
IYDDIN
//
