ZN711_MOUSE
ID ZN711_MOUSE Reviewed; 761 AA.
AC A2ANX9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Zinc finger protein 711;
GN Name=Znf711; Synonyms=Zfp711;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Transcription regulator required for brain development.
CC Probably acts as a transcription factor that binds to the promoter of
CC target genes and recruits PHF8 histone demethylase, leading to activate
CC expression of genes involved in neuron development, such as KDM5C (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PHF8. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AL831771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A2ANX9; -.
DR SMR; A2ANX9; -.
DR STRING; 10090.ENSMUSP00000109036; -.
DR iPTMnet; A2ANX9; -.
DR PhosphoSitePlus; A2ANX9; -.
DR MaxQB; A2ANX9; -.
DR PeptideAtlas; A2ANX9; -.
DR PRIDE; A2ANX9; -.
DR ProteomicsDB; 302142; -.
DR MGI; MGI:3045342; Zfp711.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; A2ANX9; -.
DR ChiTaRS; Zfp711; mouse.
DR PRO; PR:A2ANX9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A2ANX9; protein.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR006794; Transcrp_activ_Zfx/Zfy-dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 7.
DR Pfam; PF04704; Zfx_Zfy_act; 2.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 3: Inferred from homology;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..761
FT /note="Zinc finger protein 711"
FT /id="PRO_0000399819"
FT ZN_FING 383..408
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..499
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 505..527
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 533..556
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 562..584
FT /note="C2H2-type 6; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 590..613
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 619..641
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 647..670
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 676..698
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 704..727
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 733..755
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y462"
FT CROSSLNK 235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y462"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y462"
SQ SEQUENCE 761 AA; 86415 MW; ABC48F04740540E8 CRC64;
MESGGGSLGL HTSDARMAHT MIMQDFVAGM AGTAHIDGDH IVVSVPEAVL VSDVVTDDGI
TLDHGLAAEV VHGPDIITET DVVTEGVIVP EAVLEADVAI EEDLEEDDGD HILTSELITE
TVRVPEQVFV ADLVSGPDGH LEHVVQDCVS GVDSPTMVSE EVLVTNSDTE TVIQAGGGVP
GSTVTIKTEE DDDDDVKSTS EDYLMISLDD VGEKLEHMGN TPLKIASDGS QEDVKEDAFG
SEVIKVYIFK AEAEDDVEIG GTEIVTESEY SSGHSVAGVL DQSRMQREKM VYMAVKDSSQ
EQDDIRDERR VSRRYEECQA PGNTFDSALE NRNTTAAQYL QICDSMNTNK VLKQKIKKRR
RGETRQWQTA VIIGPDGQPL TVYPCHICTK KFKSRGFLKR HMKNHPDHLM RKKYQCTDCD
FTTNKKVSFH NHLESHKLIN KVDKTHEFTE YTRRYREASP LSSNKLILRD KEPKMHKCKY
CDYETAEQGL LNRHLLAVHS KSFPHVCVEC GKGFRHPSEL KKHMRTHTGE KPYQCQYCAF
RCADQSNLKT HIKSKHGSNL PYKCEHCPQA FGDERELQRH LDLFQGHKTH QCPHCDHKST
NSSDLKRHII SVHTKDFPHK CEVCDKGFHR PSELKKHSDI HKGRKIHQCR HCDFKTSDPF
ILSGHILSVH TKDQSLKCKR CKRGFRQQNE LKKHMKTHTG RKIYQCEYCE YSTTDASGFK
RHVISIHTKD YPHRCEFCKK GFRRPSEKKQ HIMRHHKETL M
