GFI1_CANLF
ID GFI1_CANLF Reviewed; 422 AA.
AC Q5DWN0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Zinc finger protein Gfi-1;
DE AltName: Full=Growth factor independence 1;
GN Name=GFI1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Okayama T., Masuda K., Ohno K., Tsujimoto H.;
RT "Molecular cloning of proto-oncogene Gfi-1 in dog and its expression.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription repressor essential for hematopoiesis.
CC Functions in a cell-context and development-specific manner. Binds to
CC 5'-TAAATCAC[AT]GCA-3' in the promoter region of a large number of
CC genes. Component of several complexes, including the EHMT2-GFI1-HDAC1,
CC AJUBA-GFI1-HDAC1 and RCOR-GFI-KDM1A-HDAC complexes, that suppress, via
CC histone deacetylase (HDAC) recruitment, a number of genes implicated in
CC multilineage blood cell development. Regulates neutrophil
CC differentiation, promotes proliferation of lymphoid cells, and is
CC required for granulocyte development. Mediates, together with U2AF1L4,
CC the alternative splicing of CD45 and controls T-cell receptor
CC signaling. Regulates the endotoxin-mediated Toll-like receptor (TLR)
CC inflammatory response by antagonizing RELA. Cooperates with CBFA2T2 to
CC regulate ITGB1-dependent neurite growth. Controls cell-cycle
CC progression by repressing CDKNIA/p21 transcription in response to TGFB1
CC via recruitment of GFI1 by ZBTB17 to the CDKNIA/p21 and CDKNIB
CC promoters. Required for the maintenance of inner ear hair cells (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with U2AF1L4. Component of RCOR-GFI-KDM1A-HDAC
CC complexes. Interacts directly with RCOR1, KDM1A and HDAC2. Also
CC interacts with HDAC1 and HDAC3. Interacts (via the zinc-finger domain)
CC with ARIH2; the interaction prevents GFI1 ubiquitination and
CC proteasomal degradation. Interacts with PIAS3; the interaction relieves
CC the inhibitory effect of PIAS3 on STAT3-mediated transcriptional
CC activity. Forms a complex with EHMT2 and HDAC1 to promote 'Lys-9'
CC dimethylation of H3 (H3K9Me2) and repress expression of target genes.
CC Interacts directly with EHMT2. Component of the GFI1-AJUBA-HDAC1
CC repressor complex. Interacts directly with AJUBA (via ITS LIM domains);
CC the interaction results in the HDAC-dependent corepression of a subset
CC of GFI1 target genes and, occurs independently of the SNAG domain.
CC Interacts with SPI1; the interaction inhibits SPI1 transcriptional
CC activity and represses SPI1-regulated macrophage-specific genes
CC required for proper granulocyte development. Interacts with RUNX1T1;
CC the interaction represses HDAC-mediated transcriptional activity.
CC Interacts with RELA; the interaction occurs on liposaccharide (LPS)
CC stimulation and controls RELA DNA binding activity and regulates
CC endotoxin-mediated TOLL-like receptor inflammatory response. Interacts
CC (via the C-terminal zinc fingers) with ZBTB17; the interaction results
CC in the recruitment of GFI1 to the CDKN1A/p21 and CDKNIB promoters and
CC repression of transcription (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with
CC PIAS3 and RUNX1T1 in nuclear dots. {ECO:0000250}.
CC -!- DOMAIN: Zinc fingers 3, 4 and 5 are required for DNA-binding and for
CC interaction with SPI1. {ECO:0000250}.
CC -!- DOMAIN: The SNAG domain of GFIs is required for nuclear location and
CC for interaction with some corepressors. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
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DR EMBL; AB178767; BAD90602.1; -; mRNA.
DR RefSeq; NP_001012737.1; NM_001012719.1.
DR AlphaFoldDB; Q5DWN0; -.
DR SMR; Q5DWN0; -.
DR STRING; 9612.ENSCAFP00000043191; -.
DR PaxDb; Q5DWN0; -.
DR Ensembl; ENSCAFT00030016956; ENSCAFP00030014818; ENSCAFG00030009151.
DR Ensembl; ENSCAFT00040010001; ENSCAFP00040008672; ENSCAFG00040005332.
DR Ensembl; ENSCAFT00845027512; ENSCAFP00845021646; ENSCAFG00845015425.
DR GeneID; 490156; -.
DR KEGG; cfa:490156; -.
DR CTD; 2672; -.
DR VEuPathDB; HostDB:ENSCAFG00845015425; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156166; -.
DR HOGENOM; CLU_002678_94_9_1; -.
DR InParanoid; Q5DWN0; -.
DR OMA; KPYMWNS; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF350784; -.
DR Proteomes; UP000002254; Chromosome 6.
DR Bgee; ENSCAFG00000020154; Expressed in thymus and 46 other tissues.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
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:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0030097; P:hemopoiesis; IEA:InterPro.
DR GO; GO:0010956; P:negative regulation of calcidiol 1-monooxygenase activity; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0070105; P:positive regulation of interleukin-6-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IEA:InterPro.
DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR029840; GFI1/1B.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24404:SF46; PTHR24404:SF46; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..422
FT /note="Zinc finger protein Gfi-1"
FT /id="PRO_0000047192"
FT ZN_FING 255..278
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..306
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..334
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 340..362
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 368..390
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 396..419
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..20
FT /note="SNAG domain"
FT /evidence="ECO:0000250"
FT REGION 140..257
FT /note="Required for interaction with RELA"
FT /evidence="ECO:0000250"
FT COMPBIAS 42..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07120"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07120"
SQ SEQUENCE 422 AA; 44977 MW; ECCDF378B70D7E54 CRC64;
MPRSFLVKSK KAHSYHQPRS PGPDYSLRLE NVLAPGGADG TSSAGGAQTE PRGRLSPESQ
LTEAPDRSSA SPGSCEGSVC DRSSEFEDFW RPPSPSVSPA SEKSVCPSLD EAQPFPLPFK
PYSWRGLAGS DLRHLVHSYR PCAALDRGAG LGLFCERAPE PGHPAALYGP ERAAGGAGAG
APGGGSAGGG AAGGSGLGLY GDFGPAAAGL YERPTAAAGG LYSERGHGLH ADKGAGVKVE
SELLCTRLLL GGGSYKCIKC SKVFSTPHGL EVHVRRSHSG TRPFACEMCG KTFGHAVSLE
QHKAVHSQER SFDCKICGKS FKRSSTLSTH LLIHSDTRPY PCQYCGKRFH QKSDMKKHTF
IHTGEKPHKC QVCGKAFSQS SNLITHSRKH TGFKPFGCDL CGKGFQRKVD LRRHRETQHG
LK
