ZN436_MOUSE
ID ZN436_MOUSE Reviewed; 452 AA.
AC Q8BPP0; Q03309; Q69ZC6; Q8BQC2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc finger protein 436;
DE AltName: Full=Zinc finger protein 46;
DE Short=Zfp-46;
DE AltName: Full=Zinc finger protein MLZ-4;
GN Name=Znf436; Synonyms=Kiaa1710, Mlz-4, Zfp46;
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=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Mammary gland;
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 [MRNA] OF 36-452, AND TISSUE SPECIFICITY.
RC TISSUE=Lens;
RX PubMed=8444344; DOI=10.1016/0378-1119(93)90395-j;
RA Brady J.P., Piatigorsky J.;
RT "Cloning and characterization of a novel zinc-finger protein-encoding cDNA
RT from the mouse eye lens.";
RL Gene 124:207-214(1993).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Lens, liver, heart, kidney, spleen and brain.
CC {ECO:0000269|PubMed:8444344}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32518.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173240; BAD32518.1; ALT_INIT; mRNA.
DR EMBL; AK051031; BAC34503.1; -; mRNA.
DR EMBL; AK053652; BAC35464.1; -; mRNA.
DR EMBL; AK136405; BAE22966.1; -; mRNA.
DR EMBL; AK148255; BAE28441.1; -; mRNA.
DR EMBL; M98502; AAA39949.1; ALT_INIT; mRNA.
DR CCDS; CCDS18804.1; -.
DR PIR; JN0533; JN0533.
DR RefSeq; NP_033583.2; NM_009557.3.
DR RefSeq; XP_006538794.1; XM_006538731.1.
DR RefSeq; XP_006538795.1; XM_006538732.1.
DR AlphaFoldDB; Q8BPP0; -.
DR SMR; Q8BPP0; -.
DR STRING; 10090.ENSMUSP00000070216; -.
DR iPTMnet; Q8BPP0; -.
DR PhosphoSitePlus; Q8BPP0; -.
DR PaxDb; Q8BPP0; -.
DR PRIDE; Q8BPP0; -.
DR ProteomicsDB; 275288; -.
DR Antibodypedia; 15569; 139 antibodies from 24 providers.
DR DNASU; 22704; -.
DR Ensembl; ENSMUST00000069195; ENSMUSP00000070216; ENSMUSG00000051351.
DR GeneID; 22704; -.
DR KEGG; mmu:22704; -.
DR UCSC; uc008vhw.1; mouse.
DR CTD; 22704; -.
DR MGI; MGI:99192; Zfp46.
DR VEuPathDB; HostDB:ENSMUSG00000051351; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000153587; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q8BPP0; -.
DR OMA; EAHTGIR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BPP0; -.
DR TreeFam; TF337055; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 22704; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp46; mouse.
DR PRO; PR:Q8BPP0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BPP0; protein.
DR Bgee; ENSMUSG00000051351; Expressed in vas deferens and 249 other tissues.
DR ExpressionAtlas; Q8BPP0; baseline and differential.
DR Genevisible; Q8BPP0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..452
FT /note="Zinc finger protein 436"
FT /id="PRO_0000047585"
FT DOMAIN 1..100
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 120..142
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 148..170
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 176..198
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 204..226
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 232..254
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 260..282
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..310
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 316..338
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 344..366
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 372..394
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..450
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 43..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9C0F3"
FT CONFLICT 3
FT /note="M -> I (in Ref. 2; BAC34503)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..217
FT /note="GKSFCRLS -> AKASAASP (in Ref. 3; AAA39949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 52363 MW; 46614D72AF7EB1AC CRC64;
MAMYLTREEW RPLDPTQRDL YRDVMQENYG NVVSLDFEIR SENEANPKQE FSDDVEFATM
SEEPLENAEK NPGSEEAFES GDQAERPWGD LTAEEWVSYP LQQVTDLLVH KEAHAGIRYH
ICSQCGKAFS QISDLNRHQK THTGDRPYKC YECGKGFSRS SHLIQHQRTH TGERPYDCNE
CGKSFGRSSH LIQHQTIHTG EKPHKCTECG KSFCRLSHLI QHQRTHSGEK PYECEECGKS
FSRSSHLAQH QRTHTGEKPY ECHECGRGFS ERSDLIKHYR VHTGERPYKC DECGKNFSQN
SDLVRHRRAH TGEKPYHCNE CGENFSRISH LVQHQRTHTG EKPYECTACG KSFSRSSHLI
THQKIHTGEK PYECNECWRS FGERSDLIKH QRTHTGEKPY ECVQCGKGFT QSSNLITHQR
VHTGEKPYEC TECDKSFSRS SALIKHKRVH TD
