ID   ZN143_BOVIN             Reviewed;         613 AA.
AC   A6QQW0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Zinc finger protein 143;
DE   AltName: Full=Selenocysteine tRNA gene transcription-activating factor;
GN   Name=ZNF143; Synonyms=STAF;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SUBUNIT: Interacts with CHD8. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; BC150013; AAI50014.1; -; mRNA.
DR   RefSeq; NP_001095624.1; NM_001102154.1.
DR   AlphaFoldDB; A6QQW0; -.
DR   SMR; A6QQW0; -.
DR   STRING; 9913.ENSBTAP00000021394; -.
DR   PaxDb; A6QQW0; -.
DR   PRIDE; A6QQW0; -.
DR   Ensembl; ENSBTAT00000064671; ENSBTAP00000054556; ENSBTAG00000016074.
DR   GeneID; 533243; -.
DR   KEGG; bta:533243; -.
DR   CTD; 7702; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016074; -.
DR   VGNC; VGNC:58348; ZNF143.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000157584; -.
DR   InParanoid; A6QQW0; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000016074; Expressed in oocyte and 106 other tissues.
DR   ExpressionAtlas; A6QQW0; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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; 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   2: Evidence at transcript level;
KW   Acetylation; Activator; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..613
FT                   /note="Zinc finger protein 143"
FT                   /id="PRO_0000370717"
FT   ZN_FING         212..236
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         242..266
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         272..296
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         302..326
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         332..356
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         362..386
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         392..415
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         327
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P52747"
FT   CROSSLNK        188
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52747"
FT   CROSSLNK        381
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P52747"
SQ   SEQUENCE   613 AA;  66079 MW;  2AA5227B8D7F372B CRC64;
     MLLAQINRDS QGMTEFPGGG MEAQHVTLCL TEAVTVADGD NLENMEGVSL QAVTLADGST
     AYIQHNSKDG SAAYVQHVPI PKTTGDSLRL EDGQAVQLED SYDQSALQAV QLEDGTTAYI
     HHAVQVPQSD TILAIQADGT VAGLHTGDAA IDPDTISALE QYAAKVSIDG SEGVTGSGII
     GENEQEKKMQ IVLQGHATRV TAKSQQSGEK AFRCGYDGCG KLYTTAHHLK VHERSHTGDR
     PYQCEHAGCG KAFATGYGLK SHVRTHTGEK PYRCSEDNCT KSFKTSGDLQ KHIRTHTGER
     PFKCHFEGCG RSFTTSNIRK VHIRTHTGER PYYCTEPGCG RAFASATNYK NHVRIHTGEK
     PYVCTVPGCD KRFTEYSSLY KHHVVHTHSK PYNCNHCGKT YKQISTLAMH KRTAHNDTEP
     IEEEQEAFFE PPPGQGEDVL KGSQITYVTG VEGDDVVSTQ VATVTQSGLS QQVTLISQDG
     TQHVNISQAD MQAIGNTITM VTQDGTPITV PAHDAVISSA GAHSVAMVTA EGTEGQQVAI
     VAQDLAAFHT ASSEMGHQQH SHHLVTTETR PLTLVATSNG TQIAVQLGEQ PSLEEAIRIA
     SRIQQGETPG LDD