ZN536_MOUSE
ID ZN536_MOUSE Reviewed; 1302 AA.
AC Q8K083; Q80U15;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Zinc finger protein 536;
GN Name=Znf536; Synonyms=Kiaa0390, Zfp536;
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 MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Pituitary;
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].
RC TISSUE=Eye;
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19398580; DOI=10.1128/mcb.00362-09;
RA Qin Z., Ren F., Xu X., Ren Y., Li H., Wang Y., Zhai Y., Chang Z.;
RT "ZNF536, a novel zinc finger protein specifically expressed in the brain,
RT negatively regulates neuron differentiation by repressing retinoic acid-
RT induced gene transcription.";
RL Mol. Cell. Biol. 29:3633-3643(2009).
CC -!- FUNCTION: Transcriptional repressor that negatively regulates neuron
CC differentiation by repressing retinoic acid-induced gene transcription
CC (PubMed:19398580). Binds and interrupts RARA from binding to retinoic
CC acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites
CC known as DR1-DR5 (PubMed:19398580). Recognizes and binds 2 copies of
CC the core DNA sequence 5'-CCCCCA-3' (By similarity).
CC {ECO:0000250|UniProtKB:O15090, ECO:0000269|PubMed:19398580}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19398580}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the brain, while a weak
CC signal is also detected in the heart and testis (PubMed:19398580).
CC Expression is abundant in neuronal cells of the cerebral cortex,
CC hippocampus and hypothalamic area (at protein level) (PubMed:19398580).
CC {ECO:0000269|PubMed:19398580}.
CC -!- DEVELOPMENTAL STAGE: From 9.5 dpc to 12.5 dpc, expressed in the
CC developing central nervous system, dorsal root ganglia, eye vesicles
CC and limbs. At 9.5 dpc, expressed in the developing forebrain, midbrain,
CC hindbrain neural folds and spinal cord. When the embryo developed to
CC 10.5 dpc, expressed in the telencephalic vesicles, midbrain, hindbrain,
CC and spinal cord and is detectable in the dorsal root ganglia region and
CC somites. Similar expression patterns at 11.5 dpc and 12.5 dpc, with
CC significant expression in the telencephalic vesicles, midbrain,
CC hindbrain and spinal cord. {ECO:0000269|PubMed:19398580}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65552.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122270; BAC65552.1; ALT_INIT; mRNA.
DR EMBL; AK030633; BAC27055.1; -; mRNA.
DR EMBL; AK034508; BAC28735.1; -; mRNA.
DR EMBL; BC033594; AAH33594.1; -; mRNA.
DR CCDS; CCDS21156.1; -.
DR RefSeq; NP_759017.1; NM_172385.2.
DR AlphaFoldDB; Q8K083; -.
DR BioGRID; 232588; 1.
DR STRING; 10090.ENSMUSP00000058468; -.
DR iPTMnet; Q8K083; -.
DR PhosphoSitePlus; Q8K083; -.
DR EPD; Q8K083; -.
DR jPOST; Q8K083; -.
DR MaxQB; Q8K083; -.
DR PaxDb; Q8K083; -.
DR PeptideAtlas; Q8K083; -.
DR PRIDE; Q8K083; -.
DR ProteomicsDB; 275085; -.
DR Antibodypedia; 15575; 87 antibodies from 21 providers.
DR Ensembl; ENSMUST00000056338; ENSMUSP00000058468; ENSMUSG00000043456.
DR Ensembl; ENSMUST00000175941; ENSMUSP00000134778; ENSMUSG00000043456.
DR Ensembl; ENSMUST00000176114; ENSMUSP00000135681; ENSMUSG00000043456.
DR Ensembl; ENSMUST00000176205; ENSMUSP00000135068; ENSMUSG00000043456.
DR GeneID; 243937; -.
DR KEGG; mmu:243937; -.
DR UCSC; uc009gkk.1; mouse.
DR CTD; 243937; -.
DR MGI; MGI:1926102; Zfp536.
DR VEuPathDB; HostDB:ENSMUSG00000043456; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156397; -.
DR HOGENOM; CLU_008125_0_0_1; -.
DR InParanoid; Q8K083; -.
DR OMA; SDAPGEC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8K083; -.
DR TreeFam; TF332241; -.
DR BioGRID-ORCS; 243937; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp536; mouse.
DR PRO; PR:Q8K083; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K083; protein.
DR Bgee; ENSMUSG00000043456; Expressed in epithelium of lens and 181 other tissues.
DR ExpressionAtlas; Q8K083; baseline and differential.
DR Genevisible; Q8K083; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1302
FT /note="Zinc finger protein 536"
FT /id="PRO_0000271042"
FT ZN_FING 130..152
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 158..180
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 274..297
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..323
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 631..653
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 753..775
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 781..803
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15090"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15090"
FT CONFLICT 590
FT /note="N -> Y (in Ref. 1; BAC65552)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="Y -> F (in Ref. 1; BAC65552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036
FT /note="T -> A (in Ref. 1; BAC65552)"
FT /evidence="ECO:0000305"
FT CONFLICT 1207
FT /note="G -> S (in Ref. 1; BAC65552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1302 AA; 141576 MW; A9AF82D1D9481465 CRC64;
MEEASLCLGV SSTAPEAEPH LSGPVLNGQY AMSQKLHQIT SQLSHAFPEL HPRPNPEEKT
PAALEEKAHV PMSGQSMGSQ MALLANQLGR DVDNSLNGRV DLQQFLNGQN LGIMSQMSDI
EDDARKNRKY PCPLCGKRFR FNSILSLHMR THTGEKPFKC PYCDHRAAQK GNLKIHLRTH
KLGNLGKGRG RVREENRLLH ELEERAILRD KQMKGSLLQP RSDLKPLAHA QQAPLATCNL
ALPPNHSVPD VAHPAPSPKP ANLQEDSVTP AAGFRCTFCK GKFKKREELD RHIRILHKPY
KCTLCDFAAS QEEELISHVE KAHITAESAQ GQGPNGGGEQ SANEFRCEVC GQVFSQAWFL
KGHMRKHKDS FEHCCQICGR RFKEPWFLKN HMKVHLNKLS VKNKSPTEPE VAVPMGGLSQ
EAHANLYSRY LSCLQSGFMA PDKASLNEPS QLYGKGELPA KEKEVLGKLL SPISSMAHSV
PEGDKHSLLG CLNLVPPLKS SCIERLQAAA KAAEMDPVNS YQAWQLMARG MAMEHGFLSK
EHQLSRNHED PLANTGVLFD KEKREYVLVG ADGSKQKMPA DLVHSTKVGN QRDLPNKLDP
LEGSREFLSH GLNQTLDYNL QGPGNMKEKP TECPDCGRVF RTYHQVVVHS RVHKRDRKSD
EDALHVGVGL EERRGSGSDQ ESQSVSRSTT PGSSNVTEES GAGGGLSQTG SAQEDSPHPS
SPSSSDIGEE AGRAGGVQQQ ALLRDRNLGS AMKDCPYCGK TFRTSHHLKV HLRIHTGEKP
YKCPHCDYAG TQSASLKYHL ERHHRERQNG AGPLSGQPPN QEHKDETSSK APMFIRPDIL
RGAFKGLPGI DFRGGPASQQ WTAGMLSSGD HSGQATGMPS ELSSDALKGS DLPSKSSHYS
EIGRAYQNIV SNGVNFQGSL QAFMDSFVLS SLKKKDTKDK VPSDAHPMKA HTAEGGEEKA
SMKPSQRKSE KSQYEPLDLS VRPDAPTLPG SSVTVQDSIA WHGCLFCAFT TSSMELMALH
LQANHLGRAK RKDHPTGVTV NCKEQGREAS KVSVLPSLQS NKEMALPSAV GVLDSAPEKL
AQGPAKETLG DPKSGQWPNH MDPAFCTFPS DFYKQFGVYP AMVGSGAPGS CLNKNTEGKT
HPDDDAPILI PETTNKNTTD DLSDIASSED MDSSKGENNE DEELDTEPEM TSKPLSALSK
DGSSEGGDSL LSPGAPQPIQ GLVSPLAQAA EEQWHSPGLL PAQDPSAGLP KPERGPPGLE
KPMSMLSVLR AYSADGLAAF NGLASSTANS GCIKRPDLCG KF
