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Zinc finger protein 143 (Zfp-143) (Selenocysteine tRNA gene transcription-activating factor) (mStaf)

 ZN143_MOUSE             Reviewed;         638 AA.
O70230; Q8BGB0; Q8CEI6; Q8CI27;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
30-AUG-2017, entry version 125.
RecName: Full=Zinc finger protein 143;
Short=Zfp-143;
AltName: Full=Selenocysteine tRNA gene transcription-activating factor;
Short=mStaf;
Name=Znf143; Synonyms=Staf, Zfp143;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
STRAIN=129/SvJ; TISSUE=Liver;
PubMed=9535833; DOI=10.1074/jbc.273.15.8598;
Adachi K., Saito H., Tanaka T., Oka T.;
"Molecular cloning and characterization of the murine staf cDNA
encoding a transcription activating factor for the selenocysteine tRNA
gene in mouse mammary gland.";
J. Biol. Chem. 273:8598-8606(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10657238; DOI=10.1042/bj3460045;
Adachi K., Katsuyama M., Song S., Oka T.;
"Genomic organization, chromosomal mapping and promoter analysis of
the mouse selenocysteine tRNA gene transcription-activating factor
(mStaf) gene.";
Biochem. J. 346:45-51(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11528126;
Cichutek A., Brueckmann T., Seipel B., Hauser H., Schlaubitz S.,
Prawitt D., Hankeln T., Schmidt E.R., Winterpacht A., Zabel B.U.;
"Comparative architectural aspects of regions of conserved synteny on
human chromosome 11p15.3 and mouse chromosome 7 (including genes WEE1
and LMO1).";
Cytogenet. Cell Genet. 93:277-283(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Cerebellum, Skin, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Transcriptional activator. Activates the gene for
selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small
nuclear RNA (snRNA) gene promoters. Participates in efficient U6
RNA polymerase III transcription via its interaction with CHD8 (By
similarity). {ECO:0000250, ECO:0000269|PubMed:9535833}.
-!- SUBUNIT: Interacts with CHD8. {ECO:0000250}.
-!- INTERACTION:
Q8BX22:Sall4; NbExp=2; IntAct=EBI-5691478, EBI-2312582;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O70230-1; Sequence=Displayed;
Name=2;
IsoId=O70230-2; Sequence=VSP_036980;
Name=3;
IsoId=O70230-3; Sequence=VSP_036979;
-!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC16899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH37658.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC25726.1; Type=Frameshift; Positions=5; Evidence={ECO:0000305};
Sequence=BAC26281.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAC17144.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF011758; AAC16899.1; ALT_INIT; mRNA.
EMBL; AJ278435; CAC17144.1; ALT_INIT; Genomic_DNA.
EMBL; AK028056; BAC25726.1; ALT_FRAME; mRNA.
EMBL; AK029078; BAC26281.1; ALT_INIT; mRNA.
EMBL; AK029926; BAC26682.1; -; mRNA.
EMBL; BC037658; AAH37658.1; ALT_INIT; mRNA.
CCDS; CCDS57580.1; -. [O70230-2]
RefSeq; NP_033307.2; NM_009281.3. [O70230-2]
RefSeq; XP_006507595.1; XM_006507532.2. [O70230-1]
UniGene; Mm.10815; -.
ProteinModelPortal; O70230; -.
SMR; O70230; -.
BioGrid; 203516; 4.
IntAct; O70230; 3.
STRING; 10090.ENSMUSP00000081778; -.
iPTMnet; O70230; -.
PhosphoSitePlus; O70230; -.
EPD; O70230; -.
MaxQB; O70230; -.
PaxDb; O70230; -.
PeptideAtlas; O70230; -.
PRIDE; O70230; -.
Ensembl; ENSMUST00000084727; ENSMUSP00000081778; ENSMUSG00000061079. [O70230-1]
Ensembl; ENSMUST00000169638; ENSMUSP00000126015; ENSMUSG00000061079. [O70230-3]
Ensembl; ENSMUST00000209505; ENSMUSP00000147673; ENSMUSG00000061079. [O70230-2]
Ensembl; ENSMUST00000211798; ENSMUSP00000148235; ENSMUSG00000061079. [O70230-2]
GeneID; 20841; -.
KEGG; mmu:20841; -.
UCSC; uc009jew.1; mouse. [O70230-2]
UCSC; uc009jex.1; mouse. [O70230-1]
UCSC; uc012fse.1; mouse. [O70230-3]
CTD; 20841; -.
MGI; MGI:1277969; Zfp143.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00760000118771; -.
HOGENOM; HOG000118073; -.
HOVERGEN; HBG053078; -.
InParanoid; O70230; -.
KO; K20828; -.
OMA; KMQIVLQ; -.
OrthoDB; EOG091G0N38; -.
PhylomeDB; O70230; -.
TreeFam; TF333498; -.
Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
PRO; PR:O70230; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000061079; -.
CleanEx; MM_ZFP143; -.
Genevisible; O70230; MM.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 7.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Complete proteome;
DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 638 Zinc finger protein 143.
/FTId=PRO_0000248071.
ZN_FING 237 261 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 267 291 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 297 321 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 327 351 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 357 381 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 387 411 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 417 440 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P52747}.
MOD_RES 352 352 Phosphothreonine.
{ECO:0000250|UniProtKB:P52747}.
CROSSLNK 213 213 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P52747}.
CROSSLNK 406 406 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P52747}.
VAR_SEQ 97 125 TGDSLRLEDGQAVQLEDGTTAFIHHTSKD -> N (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036979.
VAR_SEQ 97 98 TG -> R (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_036980.
CONFLICT 190 190 K -> T (in Ref. 4; BAC25726).
{ECO:0000305}.
CONFLICT 250 250 T -> K (in Ref. 4; BAC25726).
{ECO:0000305}.
CONFLICT 261 261 H -> D (in Ref. 4; BAC25726).
{ECO:0000305}.
CONFLICT 342 342 N -> T (in Ref. 4; BAC25726).
{ECO:0000305}.
CONFLICT 508 508 H -> N (in Ref. 4; BAC25726).
{ECO:0000305}.
CONFLICT 528 528 Q -> K (in Ref. 4; BAC25726).
{ECO:0000305}.
CONFLICT 618 618 L -> V (in Ref. 4; BAC25726).
{ECO:0000305}.
CONFLICT 634 634 P -> A (in Ref. 4; BAC25726).
{ECO:0000305}.
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


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