ZN410_MOUSE
ID ZN410_MOUSE Reviewed; 478 AA.
AC Q8BKX7; Q8BWB3; Q8BZZ7; Q8R5L2; Q8VDL2;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Zinc finger protein 410;
DE AltName: Full=Another partner for ARF 1 {ECO:0000303|PubMed:12370286};
GN Name=Znf410 {ECO:0000312|MGI:MGI:1289280};
GN Synonyms=Apa1 {ECO:0000303|PubMed:12370286},
GN D12Ertd748e {ECO:0000312|MGI:MGI:1289280},
GN Zfp410 {ECO:0000312|MGI:MGI:1289280};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=12370286; DOI=10.1128/mcb.22.21.7385-7397.2002;
RA Benanti J.A., Williams D.K., Robinson K.L., Ozer H.L., Galloway D.A.;
RT "Induction of extracellular matrix-remodeling genes by the senescence-
RT associated protein APA-1.";
RL Mol. Cell. Biol. 22:7385-7397(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Embryonic testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=33859416; DOI=10.1038/s41588-021-00843-w;
RA Vinjamur D.S., Yao Q., Cole M.A., McGuckin C., Ren C., Zeng J., Hossain M.,
RA Luk K., Wolfe S.A., Pinello L., Bauer D.E.;
RT "ZNF410 represses fetal globin by singular control of CHD4.";
RL Nat. Genet. 53:719-728(2021).
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 (PubMed:33859416). Prevents
CC expression of fetal hemoglobin genes HBG1 and HBG2 through CHD4: acts
CC as a direct transcriptional activator of CHD4, a central component of
CC the NuRD complex that represses transcription of fetal hemoglobin genes
CC HBG1 and HBG2 in erythroid cells (PubMed:33859416). May also activate
CC transcription of matrix-remodeling genes such as MMP1 during fibroblast
CC senescence (By similarity). May activate transcription of the gap
CC junction gene GJC1, perhaps in response to increasing glucose (By
CC similarity). However, recent studies suggest that ZNF410 is dedicated
CC to regulate expression of a single gene: CHD4 (By similarity).
CC {ECO:0000250|UniProtKB:Q86VK4, ECO:0000269|PubMed:33859416}.
CC -!- SUBUNIT: Interacts with CDKN2A/p14ARF. {ECO:0000250|UniProtKB:Q86VK4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:33859416}. Chromosome
CC {ECO:0000305|PubMed:33859416}. Note=Directly binds to the sequence
CC motif 5'-CATCCCATAATA-3'. {ECO:0000305|PubMed:33859416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BKX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BKX7-2; Sequence=VSP_008490, VSP_008491;
CC Name=3;
CC IsoId=Q8BKX7-3; Sequence=VSP_008492, VSP_008493;
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 -!- DISRUPTION PHENOTYPE: Mice are viable and healthy, but display reduced
CC expression of Chd4, leading to rerepression of fetal hemoglobin genes
CC Hbg1 and Hbg2. {ECO:0000269|PubMed:33859416}.
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DR EMBL; AF295806; AAL82191.1; -; mRNA.
DR EMBL; AK033090; BAC28148.1; -; mRNA.
DR EMBL; AK053001; BAC35235.1; -; mRNA.
DR EMBL; BC021528; AAH21528.1; -; mRNA.
DR EMBL; BC052080; AAH52080.1; -; mRNA.
DR CCDS; CCDS26042.1; -. [Q8BKX7-1]
DR CCDS; CCDS88368.1; -. [Q8BKX7-3]
DR CCDS; CCDS88369.1; -. [Q8BKX7-2]
DR RefSeq; NP_001239511.1; NM_001252582.1. [Q8BKX7-2]
DR RefSeq; NP_001239512.1; NM_001252583.1. [Q8BKX7-3]
DR RefSeq; NP_659082.1; NM_144833.3. [Q8BKX7-1]
DR RefSeq; XP_006516148.1; XM_006516085.2. [Q8BKX7-1]
DR RefSeq; XP_006516149.1; XM_006516086.3. [Q8BKX7-1]
DR AlphaFoldDB; Q8BKX7; -.
DR SMR; Q8BKX7; -.
DR STRING; 10090.ENSMUSP00000045550; -.
DR iPTMnet; Q8BKX7; -.
DR PhosphoSitePlus; Q8BKX7; -.
DR EPD; Q8BKX7; -.
DR MaxQB; Q8BKX7; -.
DR PaxDb; Q8BKX7; -.
DR PRIDE; Q8BKX7; -.
DR Antibodypedia; 126; 191 antibodies from 22 providers.
DR DNASU; 52708; -.
DR Ensembl; ENSMUST00000045931; ENSMUSP00000045550; ENSMUSG00000042472. [Q8BKX7-1]
DR Ensembl; ENSMUST00000220931; ENSMUSP00000152098; ENSMUSG00000042472. [Q8BKX7-3]
DR Ensembl; ENSMUST00000222258; ENSMUSP00000152441; ENSMUSG00000042472. [Q8BKX7-2]
DR GeneID; 52708; -.
DR KEGG; mmu:52708; -.
DR UCSC; uc007oet.2; mouse. [Q8BKX7-2]
DR UCSC; uc007oev.2; mouse. [Q8BKX7-1]
DR UCSC; uc007oew.2; mouse. [Q8BKX7-3]
DR CTD; 52708; -.
DR MGI; MGI:1289280; Zfp410.
DR VEuPathDB; HostDB:ENSMUSG00000042472; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158098; -.
DR HOGENOM; CLU_043629_1_0_1; -.
DR InParanoid; Q8BKX7; -.
DR OMA; XNDRSFI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BKX7; -.
DR TreeFam; TF333498; -.
DR BioGRID-ORCS; 52708; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp410; mouse.
DR PRO; PR:Q8BKX7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BKX7; protein.
DR Bgee; ENSMUSG00000042472; Expressed in metanephric loop of Henle and 262 other tissues.
DR ExpressionAtlas; Q8BKX7; baseline and differential.
DR Genevisible; Q8BKX7; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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; Alternative splicing; Chromosome; DNA-binding; Glycoprotein;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..478
FT /note="Zinc finger protein 410"
FT /id="PRO_0000047572"
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..113
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..113
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"
FT VAR_SEQ 335..347
FT /note="GEKPHQCQVCGKT -> GTRTCAICRPQIQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008490"
FT VAR_SEQ 335..345
FT /note="GEKPHQCQVCG -> ELEIEPRASRV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_008492"
FT VAR_SEQ 346..478
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_008493"
FT VAR_SEQ 348..478
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008491"
FT CONFLICT 52
FT /note="R -> P (in Ref. 1; AAL82191)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="V -> G (in Ref. 1; AAL82191)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="Q -> K (in Ref. 2; BAC28148)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="Q -> P (in Ref. 1; AAL82191)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="G -> A (in Ref. 1; AAL82191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 52208 MW; 187BE9F24D9609CB CRC64;
MLSDELESKP ELLVQFVQNT SIPLGQGLVE SEAKDITCLS LLPVTEASEC SRLMLPDETP
NHANSSKEVP SSAVLRSLQV NVGPDGEETR AQTVQKSPEF LTTPESPSLL QDLQPSDSTS
FILLNLTRAG LGSSAEHFVF VQDETEDSGA DFLSAESTDS SIPWFLRVQE LAHDSLIAAT
RAQLAKNAKT GSNGENVHLG SGDGQPKDSG PLPQAEKKLK CTVEGCDRTF VWPAHFKYHL
KTHRNERSFI CPAEGCGKSF YVLQRLKVHM RTHNGEKPFM CHESGCGKQF TTAGNLKNHR
RIHTGEKPFL CEAQGCGRSF AEYSSLRKHL VVHSGEKPHQ CQVCGKTFSQ SGSRNVHMRK
HHLQLGTTGS QEQDQTAEPL MGSSLLEDAS VPNKNLVSMN SQSSLGGESL NLSNTNSILG
VDDEVLTERA SRPLSSVPDV THHLVTMQSG RQSYEVSVLT AVNPQELLNQ GDLTERQT
