SP3_CHICK
ID SP3_CHICK Reviewed; 771 AA.
AC Q90WR8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Transcription factor Sp3;
GN Name=SP3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH V-JUN.
RX PubMed=12821939; DOI=10.1038/sj.onc.1206713;
RA Chamboredon S., Briggs J., Vial E., Hurault J., Galvagni F., Oliviero S.,
RA Bos T., Castellazzi M.;
RT "v-Jun downregulates the SPARC target gene by binding to the proximal
RT promoter indirectly through Sp1/3.";
RL Oncogene 22:4047-4061(2003).
CC -!- FUNCTION: Transcriptional factor that can act as an activator or
CC repressor depending on post-translational modifications. Binds to GT
CC and GC boxes promoter elements. Competes with SP1 for the GC-box
CC promoters. Weak activator of transcription (By similarity). Required
CC for activation of SPARC transcription. {ECO:0000250,
CC ECO:0000269|PubMed:12821939}.
CC -!- SUBUNIT: Interacts with HDAC1 and HDAC2; the interaction deacetylates
CC SP3 and regulates its transcriptional activity (By similarity).
CC Interacts with v-Jun. {ECO:0000250, ECO:0000269|PubMed:12821939}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body
CC {ECO:0000250}. Note=Localizes to the nuclear periphery and in nuclear
CC dots when sumoylated. Some localization in PML nuclear bodies (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:Q02447}.
CC -!- PTM: Acetylated by histone acetyltransferase p300, deacetylated by
CC HDACs. Acetylation/deacetylation states regulate transcriptional
CC activity. Acetylation appears to activate transcription. Alternate
CC sumoylation and acetylation at Lys-541 also control transcriptional
CC activity.
CC -!- PTM: Sumoylation represses transcriptional activity. Lys-541 is the
CC major site. Sumoylation at this site promotes nuclear localization to
CC the nuclear periphery, nuclear dots and PML nuclear bodies. Alternate
CC sumoylation and acetylation at Lys-541 also control transcriptional
CC activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AJ317961; CAC84905.1; -; mRNA.
DR RefSeq; NP_989934.1; NM_204603.1.
DR AlphaFoldDB; Q90WR8; -.
DR SMR; Q90WR8; -.
DR STRING; 9031.ENSGALP00000015174; -.
DR PaxDb; Q90WR8; -.
DR Ensembl; ENSGALT00000068500; ENSGALP00000046340; ENSGALG00000031796.
DR GeneID; 395302; -.
DR KEGG; gga:395302; -.
DR CTD; 6670; -.
DR VEuPathDB; HostDB:geneid_395302; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155099; -.
DR HOGENOM; CLU_019688_2_1_1; -.
DR InParanoid; Q90WR8; -.
DR OMA; TCTQVES; -.
DR OrthoDB; 1085860at2759; -.
DR PhylomeDB; Q90WR8; -.
DR PRO; PR:Q90WR8; -.
DR Proteomes; UP000000539; Chromosome 7.
DR Bgee; ENSGALG00000031796; Expressed in spleen and 13 other tissues.
DR ExpressionAtlas; Q90WR8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0030219; P:megakaryocyte differentiation; IEA:Ensembl.
DR GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR InterPro; IPR030452; SP3.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF3; PTHR23235:SF3; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..771
FT /note="Transcription factor Sp3"
FT /id="PRO_0000047143"
FT ZN_FING 611..635
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 641..665
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 671..693
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..228
FT /note="Transactivation domain (Gln-rich)"
FT /evidence="ECO:0000250"
FT REGION 341..489
FT /note="Transactivation domain (Gln-rich)"
FT /evidence="ECO:0000250"
FT REGION 524..610
FT /note="Repressor domain"
FT /evidence="ECO:0000250"
FT MOTIF 451..459
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q02447"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 541
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 771 AA; 80950 MW; 36E795D490AE79B4 CRC64;
MTAPEQPVKQ EEMAALDVDS SGHGEYLQHG NGNASASAAA AAPQDAQPSP LALLAATCSK
IGPPSPEEDE AAAAAASHSA GATGDLASVQ LAGTPNRWEV LSAAPATIKD EAGNIVQIPG
AATVTSSGQY VLPIQSLQNQ QIFSVAPGSD SSNGTVSNVQ YQVIPQIQTA DGQQVQLGFA
ASSDNSSINQ ETGQIQIIPG SNQTIIASGS PSANIQNILS QSGQVQVQGV AIGGSSFPGQ
AQVVANVPLG LPGNITFVPI NSVDLDSLGL GSGSQTMTAG INADGHLINT GQAMDSSDNS
ERTGEQVSPE ITETATDNDL FVPTSSSSQL PVTIDSSSIL EQNANNLTTT SGQVHSSDLQ
GNYIQTSVSD DTQAQNIQVS TAQPIVQHIQ LQESQQPTSQ AQIVQGIAQQ TIHGVQASQS
ISPQALQNLQ LQLNPGTFLI QAQTVTPSGQ ITWQTFQVQG VQNLQNLQIQ NAPGQQITLT
PVQTLTLGQV AAGGALTSTP VSLSTAQLPN LQTVTVNSID SAGIQLHQGE NAGSPADIRI
KEEEPDPEEW QLSGDSTLNT NDLTHLRVQV VDEEGDQPHQ EGKRLRRVAC TCPNCKEGGG
RGSNLGKKKQ HICHIPGCGK VYGKTSHLRA HLRWHSGERP FVCNWMFCGK RFTRSDELQR
HRRTHTGEKK FVCPECSKRF MRSDHLAKHI KTHQNKKGIH SSSTVLASVE ATSDDTLITA
GGTTLILANI QQGSVSGIGT VNTSGTSNQD ILTNTEIPLQ LVTVSGNETM E
