ZN143_MOUSE
ID ZN143_MOUSE Reviewed; 638 AA.
AC O70230; Q8BGB0; Q8CEI6; Q8CI27;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Zinc finger protein 143;
DE Short=Zfp-143;
DE AltName: Full=Selenocysteine tRNA gene transcription-activating factor;
DE Short=mStaf;
GN Name=Znf143; Synonyms=Staf, Zfp143;
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), AND FUNCTION.
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=9535833; DOI=10.1074/jbc.273.15.8598;
RA Adachi K., Saito H., Tanaka T., Oka T.;
RT "Molecular cloning and characterization of the murine staf cDNA encoding a
RT transcription activating factor for the selenocysteine tRNA gene in mouse
RT mammary gland.";
RL J. Biol. Chem. 273:8598-8606(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10657238; DOI=10.1042/bj3460045;
RA Adachi K., Katsuyama M., Song S., Oka T.;
RT "Genomic organization, chromosomal mapping and promoter analysis of the
RT mouse selenocysteine tRNA gene transcription-activating factor (mStaf)
RT gene.";
RL Biochem. J. 346:45-51(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11528126; DOI=10.1159/000056998;
RA Cichutek A., Brueckmann T., Seipel B., Hauser H., Schlaubitz S.,
RA Prawitt D., Hankeln T., Schmidt E.R., Winterpacht A., Zabel B.U.;
RT "Comparative architectural aspects of regions of conserved synteny on human
RT chromosome 11p15.3 and mouse chromosome 7 (including genes WEE1 and
RT LMO1).";
RL Cytogenet. Cell Genet. 93:277-283(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Skin, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcriptional activator. Activates the gene for
CC selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear
CC RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase
CC III transcription via its interaction with CHD8 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:9535833}.
CC -!- SUBUNIT: Interacts with CHD8. {ECO:0000250}.
CC -!- INTERACTION:
CC O70230; Q8BX22: Sall4; NbExp=2; IntAct=EBI-5691478, EBI-2312582;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O70230-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O70230-2; Sequence=VSP_036980;
CC Name=3;
CC IsoId=O70230-3; Sequence=VSP_036979;
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC16899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH37658.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25726.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC26281.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC17144.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF011758; AAC16899.1; ALT_INIT; mRNA.
DR EMBL; AJ278435; CAC17144.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK028056; BAC25726.1; ALT_FRAME; mRNA.
DR EMBL; AK029078; BAC26281.1; ALT_INIT; mRNA.
DR EMBL; AK029926; BAC26682.1; -; mRNA.
DR EMBL; BC037658; AAH37658.1; ALT_INIT; mRNA.
DR CCDS; CCDS57580.1; -. [O70230-2]
DR CCDS; CCDS90307.1; -. [O70230-1]
DR RefSeq; NP_033307.2; NM_009281.3. [O70230-2]
DR RefSeq; XP_006507595.1; XM_006507532.2.
DR AlphaFoldDB; O70230; -.
DR SMR; O70230; -.
DR BioGRID; 203516; 7.
DR IntAct; O70230; 4.
DR MINT; O70230; -.
DR STRING; 10090.ENSMUSP00000081778; -.
DR iPTMnet; O70230; -.
DR PhosphoSitePlus; O70230; -.
DR EPD; O70230; -.
DR MaxQB; O70230; -.
DR PaxDb; O70230; -.
DR PeptideAtlas; O70230; -.
DR PRIDE; O70230; -.
DR ProteomicsDB; 274999; -. [O70230-1]
DR ProteomicsDB; 275000; -. [O70230-2]
DR ProteomicsDB; 275001; -. [O70230-3]
DR Antibodypedia; 927; 90 antibodies from 24 providers.
DR DNASU; 20841; -.
DR Ensembl; ENSMUST00000084727; ENSMUSP00000081778; ENSMUSG00000061079. [O70230-1]
DR Ensembl; ENSMUST00000169638; ENSMUSP00000126015; ENSMUSG00000061079. [O70230-3]
DR Ensembl; ENSMUST00000209505; ENSMUSP00000147673; ENSMUSG00000061079. [O70230-2]
DR Ensembl; ENSMUST00000211798; ENSMUSP00000148235; ENSMUSG00000061079. [O70230-2]
DR GeneID; 20841; -.
DR KEGG; mmu:20841; -.
DR UCSC; uc009jew.1; mouse. [O70230-2]
DR UCSC; uc009jex.1; mouse. [O70230-1]
DR UCSC; uc012fse.1; mouse. [O70230-3]
DR CTD; 20841; -.
DR MGI; MGI:1277969; Zfp143.
DR VEuPathDB; HostDB:ENSMUSG00000061079; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157584; -.
DR HOGENOM; CLU_027168_0_0_1; -.
DR InParanoid; O70230; -.
DR OMA; GTEGQQX; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O70230; -.
DR TreeFam; TF333498; -.
DR BioGRID-ORCS; 20841; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp143; mouse.
DR PRO; PR:O70230; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O70230; protein.
DR Bgee; ENSMUSG00000061079; Expressed in cleaving embryo and 242 other tissues.
DR Genevisible; O70230; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031519; C:PcG protein complex; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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; IDA:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; 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; 5.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..638
FT /note="Zinc finger protein 143"
FT /id="PRO_0000248071"
FT ZN_FING 237..261
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 267..291
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 297..321
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..351
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 357..381
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 387..411
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 417..440
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P52747"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52747"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52747"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52747"
FT VAR_SEQ 97..125
FT /note="TGDSLRLEDGQAVQLEDGTTAFIHHTSKD -> N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036979"
FT VAR_SEQ 97..98
FT /note="TG -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036980"
FT CONFLICT 190
FT /note="K -> T (in Ref. 4; BAC25726)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="T -> K (in Ref. 4; BAC25726)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="H -> D (in Ref. 4; BAC25726)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="N -> T (in Ref. 4; BAC25726)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="H -> N (in Ref. 4; BAC25726)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="Q -> K (in Ref. 4; BAC25726)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="L -> V (in Ref. 4; BAC25726)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="P -> A (in Ref. 4; BAC25726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 69040 MW; 9BDA0B6C0EBC0634 CRC64;
MLLAQINRDS QGMTEFPGGG MEAQHVTLCL TEAVTVADGD NLENMEGVSL QAVTLADGST
AYIQHNSKDG RLIDGQVIQL EDGSAAYVQH VPIPKSTGDS LRLEDGQAVQ LEDGTTAFIH
HTSKDSYDQS SLQAVQLEDG TTAYIHHAVQ VPQSDTILAI QADGTVAGLH TGDATIDPDT
ISALEQYAAK VSIDGSDGVT STGMIGENEQ EKKMQIVLQG HATRVTPKSQ QSGEKAFRCK
YDGCGKLYTT AHHLKVHERS HTGDRPYQCE HSGCGKAFAT GYGLKSHFRT HTGEKPYRCS
EDNCTKSFKT SGDLQKHIRT HTGERPFKCP IEGCGRSFTT SNIRKVHIRT HTGERPYYCT
EPGCGRAFAS ATNYKNHVRI HTGEKPYVCT VPGCDKRFTE YSSLYKHHVV HTHSKPYNCN
HCGKTYKQIS TLAMHKRTAH NDTEPIEEEQ EAFFEPPPGQ GDDVLKGSQI TYVTGVDGED
IVSTQVATVT QSGLSQQVTL ISQDGTQHVN ISQADMQAIG NTITMVTQDG TPITVPTHDA
VISSAGTHSV AMVTAEGTEG QQVAIVAQDL AAFHTASSEM GHQQHSHHLV TTETRPLTLV
ATSNGTQIAV QLGEQPSLEE AIRIASRIQQ GETPGLDD
