ID   TOE1_BOVIN              Reviewed;         524 AA.
AC   Q17QN2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Target of EGR1 protein 1;
GN   Name=TOE1;
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=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits cell growth rate and cell cycle. Induces CDKN1A
CC       expression as well as TGF-beta expression. Mediates the inhibitory
CC       growth effect of EGR1. Involved in the maturation of snRNAs and snRNA
CC       3'-tail processing. {ECO:0000250|UniProtKB:Q96GM8}.
CC   -!- SUBUNIT: Interacts with U1, U2, U4, U5 and U6 snRNAs.
CC       {ECO:0000250|UniProtKB:Q96GM8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q96GM8}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:Q96GM8}. Note=Localizes to nuclear speckles.
CC       {ECO:0000250|UniProtKB:Q96GM8}.
CC   -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR   EMBL; BC118261; AAI18262.1; -; mRNA.
DR   RefSeq; NP_001069062.1; NM_001075594.1.
DR   AlphaFoldDB; Q17QN2; -.
DR   SMR; Q17QN2; -.
DR   STRING; 9913.ENSBTAP00000040666; -.
DR   PaxDb; Q17QN2; -.
DR   PeptideAtlas; Q17QN2; -.
DR   PRIDE; Q17QN2; -.
DR   Ensembl; ENSBTAT00000043071; ENSBTAP00000040666; ENSBTAG00000011243.
DR   GeneID; 513052; -.
DR   KEGG; bta:513052; -.
DR   CTD; 114034; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011243; -.
DR   VGNC; VGNC:49580; TOE1.
DR   eggNOG; KOG1990; Eukaryota.
DR   GeneTree; ENSGT00940000153167; -.
DR   HOGENOM; CLU_044804_1_0_1; -.
DR   InParanoid; Q17QN2; -.
DR   OMA; LLCTEDY; -.
DR   OrthoDB; 1402758at2759; -.
DR   TreeFam; TF314502; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000011243; Expressed in semen and 107 other tissues.
DR   GO; GO:0015030; C:Cajal body; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0017069; F:snRNA binding; ISS:UniProtKB.
DR   GO; GO:0034472; P:snRNA 3'-end processing; ISS:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 2.
DR   InterPro; IPR006941; RNase_CAF1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Pfam; PF04857; CAF1; 2.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GM8"
FT   CHAIN           2..524
FT                   /note="Target of EGR1 protein 1"
FT                   /id="PRO_0000270832"
FT   ZN_FING         294..322
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           335..347
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        361..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GM8"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GM8"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GM8"
FT   MOD_RES         442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GM8"
SQ   SEQUENCE   524 AA;  58546 MW;  D629A11C38892A91 CRC64;
     MAADSDDGAA SAPTVSDDGV RQSTKSGEEL VVQVPVVDVQ SDNFKEMWPS LLLAIKTANF
     VAVDTELSGL GDRKCLLNQC IEERYKAVCH AARTRSILSL GLACFKQQPD KGEHSYLAQV
     FNLTLLCMEE YVIEPKSVQF LVQHGFNFNR QYAQGIPYHK GNDKGDESQR QSVRTLFLEL
     IRARRPLVLH NGLIDLVFLY QNFYAHLPEN LGTFTADLCE MFPAGIYDTK YAAEFHARFL
     ASYLEYAFRK CERENGKQRA AGSPHLTLEF CSYPSSMRAH IDYRCCAPPP TYRTHSTSIC
     DNFSAYGWCP LGPQCPRSHD IDLIIDTDEA ALEDKRRRRR RKEKRRRALL GLPGKQPSRE
     AEDSPPTKQV CKDNRKPEET EQEVAEDETG TQPGSEQGHT NDLEMEPKAT SAETTDTATS
     EAPERQVTTD MATSEAPERQ VSPNPVPGDG LHRAGFDAFM TGYVMAYVGV SQGSHPCSSE
     PWLPECHNKV YLSGKAVPLT VVKSQFSRSS KAHNQKMKLA WGSS