IKZF3_BOVIN
ID IKZF3_BOVIN Reviewed; 509 AA.
AC A2VDW9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Zinc finger protein Aiolos;
DE AltName: Full=Ikaros family zinc finger protein 3;
GN Name=IKZF3; Synonyms=ZNFN1A3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that plays an important role in the
CC regulation of lymphocyte differentiation. Plays an essential role in
CC regulation of B-cell differentiation, proliferation and maturation to
CC an effector state. Involved in regulating BCL2 expression and
CC controlling apoptosis in T-cells in an IL2-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q9UKT9}.
CC -!- SUBUNIT: Homodimer. Heterodimer with other IKAROS family members.
CC Interacts with IKZF4 AND IKZF5. Interacts with IKZF1. Interacts with
CC HRAS. Interacts with FOXP3; this interaction may be required for
CC silencing target genes and regulating the suppressive activity of
CC FOXP3-positive regulatory T-cells (Treg). Interacts with BCL21L; this
CC interaction blocks the anti-apoptotic role of BCL21L. Associates with
CC histone deacetylase complexes containing HDAC1, MTA2 and SIN3A (By
CC similarity). {ECO:0000250|UniProtKB:Q9UKT9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKT9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UKT9}.
CC -!- DOMAIN: C2H2-type 5 and C2H2-type 6 mediate homodimerization and
CC heterodimerization. {ECO:0000250|UniProtKB:Q9UKT9}.
CC -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; BC133439; AAI33440.1; -; mRNA.
DR RefSeq; NP_001075082.1; NM_001081613.2.
DR AlphaFoldDB; A2VDW9; -.
DR SMR; A2VDW9; -.
DR STRING; 9913.ENSBTAP00000014617; -.
DR PaxDb; A2VDW9; -.
DR PRIDE; A2VDW9; -.
DR Ensembl; ENSBTAT00000014617; ENSBTAP00000014617; ENSBTAG00000011003.
DR GeneID; 540676; -.
DR KEGG; bta:540676; -.
DR CTD; 22806; -.
DR VEuPathDB; HostDB:ENSBTAG00000011003; -.
DR VGNC; VGNC:30104; IKZF3.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160462; -.
DR InParanoid; A2VDW9; -.
DR OMA; CCNVYEF; -.
DR OrthoDB; 385551at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000011003; Expressed in thymus and 68 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045577; P:regulation of B cell differentiation; ISS:UniProtKB.
DR GO; GO:0030888; P:regulation of B cell proliferation; ISS:UniProtKB.
DR GO; GO:0045619; P:regulation of lymphocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW B-cell activation; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..509
FT /note="Zinc finger protein Aiolos"
FT /id="PRO_0000297485"
FT ZN_FING 118..140
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 146..168
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 174..196
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 202..224
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 452..474
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 480..504
FT /note="C2H2-type 6; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..504
FT /note="Mediates homodimerization and heterodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q9UKT9"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O08900"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKT9"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08900"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKT9"
FT CROSSLNK 73
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKT9"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKT9"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKT9"
SQ SEQUENCE 509 AA; 58154 MW; 900477CC9E7CCF10 CRC64;
MEDIKPNVEL KSTQEQSVPT EGSELLNDYD LTKAHETENV DGTEGPANED EDIGDDSMKV
KDEYSERDEN VLKPEPMGNA EEPEIPYSYS REYNEYENIK LERHVVSYDS SRPTSGKMNC
DVCGLSCISF NVLMVHKRSH TGERPFQCNQ CGASFTQKGN LLRHIKLHTG EKPFKCHLCN
YACQRRDALT GHLRTHSVEK PYKCEFCGRS YKQRSSLEEH KERCRTFLQS TDLGETASVE
ARHIKAEMGS ERALVLDRLA SNVAKRKSSM PQKFIGEKRH CFDVSYNPSY MYEKESEMIQ
TRMMDQAINN AISYLGAEAL RPLVQTPPAP TSEMVPVISS MYPIALTRAE MPNGAPQELE
KKNIHLPEKS LPSERGLSPT NSGHDSTDTD SNHEERQNHI YQQNPMVPPR ARNGMPLLKE
GPRSYDLLKP PPICPRDSIK VINKEGEVTD VYRCDHCRVL FLDYVMFTIH MGCHGFRDPF
ECNMCGYRSH DRYEFSSHIA RGEHRAMLK
