IKZF5_BOVIN
ID IKZF5_BOVIN Reviewed; 419 AA.
AC A4IFJ6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Zinc finger protein Pegasus;
DE AltName: Full=Ikaros family zinc finger protein 5;
GN Name=IKZF5;
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=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional repressor that binds the core 5'GNNTGTNG-3'
CC DNA consensus sequence (By similarity). Involved in megakaryocyte
CC differentiation (By similarity). {ECO:0000250|UniProtKB:Q9H5V7}.
CC -!- SUBUNIT: Self-associates. Interacts with other family members; IKZF1,
CC IKZF2, IKZF3 AND IKZF4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H5V7}.
CC -!- DOMAIN: The N-terminal zinc fingers are involved in sequence-specific
CC DNA binding and heterotypic associations with other family members.
CC {ECO:0000250}.
CC -!- DOMAIN: C-terminal zinc fingers mediate homodimerization.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: 'Pegasus' was the winged horse in Greek mythology.
CC -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; BC134611; AAI34612.1; -; mRNA.
DR RefSeq; NP_001077182.1; NM_001083713.1.
DR RefSeq; XP_005225909.1; XM_005225852.3.
DR AlphaFoldDB; A4IFJ6; -.
DR STRING; 9913.ENSBTAP00000032681; -.
DR PaxDb; A4IFJ6; -.
DR PRIDE; A4IFJ6; -.
DR Ensembl; ENSBTAT00000032752; ENSBTAP00000032681; ENSBTAG00000023847.
DR Ensembl; ENSBTAT00000083563; ENSBTAP00000064053; ENSBTAG00000023847.
DR GeneID; 531250; -.
DR KEGG; bta:531250; -.
DR CTD; 64376; -.
DR VEuPathDB; HostDB:ENSBTAG00000023847; -.
DR VGNC; VGNC:30106; IKZF5.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155035; -.
DR HOGENOM; CLU_734778_0_0_1; -.
DR InParanoid; A4IFJ6; -.
DR OMA; THNQRNY; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF331860; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000023847; Expressed in spermatid and 106 other tissues.
DR ExpressionAtlas; A4IFJ6; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..419
FT /note="Zinc finger protein Pegasus"
FT /id="PRO_0000299470"
FT ZN_FING 82..104
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 110..132
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 138..161
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 364..386
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..416
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 223..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H5V7"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H5V7"
SQ SEQUENCE 419 AA; 46541 MW; CC03B1EA7020D9D2 CRC64;
MGEKKPEPLD FVKDFQEYLT QQTHHVNMIS GSVSGDKEAE ALQGAGTDGD QNGLDHPSVE
VSLDENSGML VDGFERTFDG KLKCRYCNYA SKGTARLIEH IRIHTGEKPH RCHLCPFASA
YERHLEAHMR SHTGEKPYKC ELCSFRCSDR SNLSHHRRRK HKMVPIKGTR SSLSSKKMWG
VLQKKTSNLN YSRRALINLS PPSMVVQKPD YLNDFTHEIP NIQTDSYESM AKTTPTGGLP
RDPQELMVDN PLNQLSTLAG QLSSLPPENQ NPASPDVVPC AEEKPFMMQQ PSAQAVVSAV
SASLPQSSSP ASPEPRPPHG QRNYSPVAGP SSEPSAHTST PSMGNSQPST PAPTLPVQDP
QLLHHCQHCD MYFADNILYT IHMGCHGYEN PFQCNICGCK CKNKYDFACH FARGQHNQH
