ZN143_RAT
ID ZN143_RAT Reviewed; 638 AA.
AC Q5XIU2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Zinc finger protein 143;
DE Short=Zfp-143;
DE AltName: Full=Selenocysteine tRNA gene transcription-activating factor;
GN Name=Znf143; Synonyms=Staf, Zfp143;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH83578.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC083578; AAH83578.1; ALT_INIT; mRNA.
DR RefSeq; NP_001012169.1; NM_001012169.1.
DR AlphaFoldDB; Q5XIU2; -.
DR SMR; Q5XIU2; -.
DR STRING; 10116.ENSRNOP00000013733; -.
DR iPTMnet; Q5XIU2; -.
DR PhosphoSitePlus; Q5XIU2; -.
DR PaxDb; Q5XIU2; -.
DR PRIDE; Q5XIU2; -.
DR Ensembl; ENSRNOT00000013733; ENSRNOP00000013733; ENSRNOG00000010087.
DR GeneID; 361627; -.
DR KEGG; rno:361627; -.
DR UCSC; RGD:1305662; rat.
DR CTD; 20841; -.
DR RGD; 1305662; Zfp143.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157584; -.
DR HOGENOM; CLU_027168_0_0_1; -.
DR InParanoid; Q5XIU2; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5XIU2; -.
DR TreeFam; TF333498; -.
DR Reactome; R-RNO-212436; Generic Transcription Pathway.
DR PRO; PR:Q5XIU2; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Genevisible; Q5XIU2; RN.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
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..638
FT /note="Zinc finger protein 143"
FT /id="PRO_0000248072"
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"
SQ SEQUENCE 638 AA; 68999 MW; 437CB9B2D77D37DF CRC64;
MLLAQINRDS QGMTEFPGGG MEAQHVTLCL TEAVTVADGD NLENMEGVSL QAVTLADGST
AYIQHNSKDG RLIDGQVIQL EDGSAAYVQH VPIPKSTGDS LRLEDGQAVQ LEDGTTAFIH
HTSKDSYDQS SLQAVQLEDG TTAYIHHAVQ VPQPDTILAI QADGTVAGLH TGDATIDPDT
ISALEQYAAK VSIDGSEGVT STGLIGENEQ 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 TYVTGVEGED
IVSTQVATVT QSGLSQQVTL ISQDGTQHVN ISQADMQAIG NTITMVTQDG TPITVPTHDA
VISSAGTHSV AMVTAEGTEG QQVAIVAQDL AAFHAASSEM GHQPHSHHLV TTETRPLTLV
ATSNGTQIAV QLGEQPSLEE AIRIASRIQQ GETPGLDD
