ZBT43_MOUSE
ID ZBT43_MOUSE Reviewed; 467 AA.
AC Q9DAI4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Zinc finger and BTB domain-containing protein 43;
DE AltName: Full=Zinc finger protein 297B;
GN Name=Zbtb43; Synonyms=Kiaa0414, Zfp297b, Znf297b;
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 STRAIN=C57BL/6J; TISSUE=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBUNIT: Interacts with BDP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24254.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC65559.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK005818; BAB24254.2; ALT_INIT; mRNA.
DR EMBL; AK122277; BAC65559.1; ALT_INIT; mRNA.
DR EMBL; BC043117; AAH43117.1; -; mRNA.
DR CCDS; CCDS15943.1; -.
DR RefSeq; NP_001020765.1; NM_001025594.1.
DR RefSeq; NP_082223.2; NM_027947.2.
DR RefSeq; XP_006498411.1; XM_006498348.3.
DR RefSeq; XP_006498412.1; XM_006498349.2.
DR AlphaFoldDB; Q9DAI4; -.
DR SMR; Q9DAI4; -.
DR BioGRID; 214963; 9.
DR IntAct; Q9DAI4; 2.
DR STRING; 10090.ENSMUSP00000028125; -.
DR PhosphoSitePlus; Q9DAI4; -.
DR jPOST; Q9DAI4; -.
DR PaxDb; Q9DAI4; -.
DR PRIDE; Q9DAI4; -.
DR ProteomicsDB; 298494; -.
DR Antibodypedia; 16550; 141 antibodies from 18 providers.
DR DNASU; 71834; -.
DR Ensembl; ENSMUST00000028125; ENSMUSP00000028125; ENSMUSG00000026788.
DR GeneID; 71834; -.
DR KEGG; mmu:71834; -.
DR UCSC; uc008jhw.1; mouse.
DR CTD; 23099; -.
DR MGI; MGI:1919084; Zbtb43.
DR VEuPathDB; HostDB:ENSMUSG00000026788; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160616; -.
DR HOGENOM; CLU_029118_2_0_1; -.
DR InParanoid; Q9DAI4; -.
DR PhylomeDB; Q9DAI4; -.
DR TreeFam; TF333162; -.
DR BioGRID-ORCS; 71834; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Zbtb43; mouse.
DR PRO; PR:Q9DAI4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DAI4; protein.
DR Bgee; ENSMUSG00000026788; Expressed in otolith organ and 222 other tissues.
DR ExpressionAtlas; Q9DAI4; baseline and differential.
DR Genevisible; Q9DAI4; MM.
DR GO; GO:0005634; C:nucleus; 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:0001025; F:RNA polymerase III general transcription initiation factor binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..467
FT /note="Zinc finger and BTB domain-containing protein 43"
FT /id="PRO_0000047520"
FT DOMAIN 33..97
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 373..394
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..450
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 134..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43298"
FT MOD_RES 423
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43298"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43298"
FT CROSSLNK 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43298"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43298"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43298"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43298"
FT CONFLICT 258
FT /note="M -> T (in Ref. 1; BAB24254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 52652 MW; 79F7882A93128110 CRC64;
MEPGTNSFQV EFPDFSSTIL QKLNQQRQQG QLCDVSIVVQ GHIFQAHKAV LAASSPYFCD
QVLLKNSRRI VLPDVMNPRV FENILLFSYT GRLVMPAPEI VSYLTAASFL QMWHVVDKCT
EVLEGNPTVL CQKLNHGSDH QSPSSSNYNG LVESFELGSG GHTDFPKAQE LRDGENEEES
TKDELSSQVT EHEYLPSNSS TEHDRLSTEM ASQDGEEGTN DSTEFHYTRP LYSKPSIMAH
RRWIHVKPER LEQAWDGMDV HAAYDEHQVT ESVNTMQTDH SAQPSGAEEE FQIVEKKVEV
EFDEQAEGSS YDEQVDFYGS SMEEFSGEKL GGNLIGHKQE AALAAGYSEN IEMAMGIKEE
ASHLGFSATD KLYPCQCGKS FTHKSQRDRH MSMHLGLRPY GCSVCGKKFK MKHHLVGHMK
IHTGIKPYEC NICAKRFMWR DSFHRHVTSC TKSYEAAKAE QNTTEAN
