ZN410_BOVIN
ID ZN410_BOVIN Reviewed; 467 AA.
AC Q5EAC5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Zinc finger protein 410 {ECO:0000305};
GN Name=ZNF410 {ECO:0000250|UniProtKB:Q86VK4};
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Transcription factor that binds to the sequence motif 5'-
CC CATCCCATAATA-3', and is specifically required to silence expression of
CC fetal hemoglobin in adult erythroid cells. Prevents expression of fetal
CC hemoglobin genes HBG1 and HBG2 through CHD4: acts as a direct
CC transcriptional activator of CHD4, a central component of the NuRD
CC complex that represses transcription of fetal hemoglobin genes HBG1 and
CC HBG2 in erythroid cells. May also activate transcription of matrix-
CC remodeling genes such as MMP1 during fibroblast senescence. May
CC activate transcription of the gap junction gene GJC1, perhaps in
CC response to increasing glucose. However, recent studies suggest that
CC ZNF410 is dedicated to regulate expression of a single gene: CHD4.
CC {ECO:0000250|UniProtKB:Q86VK4}.
CC -!- SUBUNIT: Interacts with CDKN2A/p14ARF. {ECO:0000250|UniProtKB:Q86VK4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86VK4}.
CC Chromosome {ECO:0000250|UniProtKB:Q86VK4}. Note=Directly binds to the
CC sequence motif 5'-CATCCCATAATA-3'. {ECO:0000250|UniProtKB:Q86VK4}.
CC -!- DOMAIN: The five zinc finger domains are necessary and sufficient to
CC bind to DNA. {ECO:0000250|UniProtKB:Q86VK4}.
CC -!- PTM: O-glycosylated. O-GlcNAcylation may occur in response to
CC increasing glucose levels and affect transcription factor activity.
CC {ECO:0000250|UniProtKB:Q86VK4}.
CC -!- PTM: Sumoylated. Sumoylation increases its half-life, possibly by
CC blocking ubiquitin-mediated degradation.
CC {ECO:0000250|UniProtKB:Q86VK4}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT020644; AAX08661.1; -; mRNA.
DR RefSeq; NP_001019662.3; NM_001024491.3.
DR RefSeq; NP_001029781.1; NM_001034609.1.
DR AlphaFoldDB; Q5EAC5; -.
DR SMR; Q5EAC5; -.
DR STRING; 9913.ENSBTAP00000040756; -.
DR PaxDb; Q5EAC5; -.
DR PRIDE; Q5EAC5; -.
DR Ensembl; ENSBTAT00000027088; ENSBTAP00000027088; ENSBTAG00000020327.
DR GeneID; 507530; -.
DR KEGG; bta:507530; -.
DR CTD; 57862; -.
DR VEuPathDB; HostDB:ENSBTAG00000020327; -.
DR VGNC; VGNC:37271; ZNF410.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158098; -.
DR HOGENOM; CLU_043629_1_0_1; -.
DR InParanoid; Q5EAC5; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000020327; Expressed in thymus and 106 other tissues.
DR ExpressionAtlas; Q5EAC5; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
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 Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 2: Evidence at transcript level;
KW Activator; Chromosome; DNA-binding; Glycoprotein; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..467
FT /note="Zinc finger protein 410"
FT /id="PRO_0000291553"
FT ZN_FING 219..243
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 249..273
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..303
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..333
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 339..362
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 84..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q86VK4"
SQ SEQUENCE 467 AA; 50860 MW; 1470C0E2E8E20C5F CRC64;
MLSDELESKP ELLVQFVQNT SIPLGQGLVE SEAKDITCLS LLPVTEASEC SRLMLPDDTP
NHTNSSKEVP SSAVLRSLQV NVGPDGEETR AQTVQKSPEF LSTPESPSLL QDLQPSDSTS
FILLNLTRAG LGSSAEHLVF VQDEADDSGN DFLSSESTDS SIPWFLRVQE LAHDSLIAAT
RAQLAKNAKT SSNGENVHLG SGDGQPKDSG PLPQMEKKLK CTVEGCDRTF VWPAHFKYHL
KTHRNDRSFI CPAAGCGKSF YVLQRLKVHM RTHNGEKPFV CPESNCGKQF TTAGNLKNHL
RIHTGEKPFL CEAQGCGRSF AEYSSLRKHL VVHSGEKPHQ CQVCGKTFSQ SGSRNVHMRK
HHLQMGAAGS QEQEPAAEPL MGSSLLEEAS VTSKNLVSMN SQPSLGGESL NLPNTNSILG
VDDEVLAEGS PRPLSSVPDV THHLVTMQSG RQSYELLNQG DLTERRT
