ID   TOE1_PONAB              Reviewed;         510 AA.
AC   Q5RAR6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Target of EGR1 protein 1;
GN   Name=TOE1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR858946; CAH91144.1; -; mRNA.
DR   RefSeq; NP_001125670.1; NM_001132198.1.
DR   AlphaFoldDB; Q5RAR6; -.
DR   SMR; Q5RAR6; -.
DR   STRING; 9601.ENSPPYP00000001640; -.
DR   GeneID; 100456899; -.
DR   KEGG; pon:100456899; -.
DR   CTD; 114034; -.
DR   eggNOG; KOG1990; Eukaryota.
DR   InParanoid; Q5RAR6; -.
DR   OrthoDB; 1402758at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProt.
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; -; 1.
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..510
FT                   /note="Target of EGR1 protein 1"
FT                   /id="PRO_0000270835"
FT   ZN_FING         294..322
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           335..347
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
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         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GM8"
SQ   SEQUENCE   510 AA;  56482 MW;  444564BA7FBEA9D0 CRC64;
     MAADSDDGAV PAPAASDGGV SKSTTSGEEL VVQVPVVDVQ SNNFREMWPS LLLAIKTANF
     VAVDTELSGL GDRKSLLNQC SEERYKAVCH AARTRSILSL GLACFKRQPD KGEHSYLAQV
     FNLTLLCMEE YVIEPKSVQF LIQHGFNFNQ QYAQGIPYHK GNDKGDESQS QSVRTLFLEL
     IRARRPLVLH NGLIDLVFLY QNFYAHLPES LGTFTADLCE MFPAGIYDTK YAAEFHARFV
     ASYLEYAFRK CERENGKQRA AGSPHLTLEF CNYPSSMRDH IDYRCCLPPA THRPHPTSIC
     DNFSAYGWCP LGPQCPQSHD IDLIIDTDEA AAEDKRRRRR RREKRKMALL NLPGTQTSGE
     AKDGPPKKQV CGDSLKAEET EQEVAEDETR NLPHSKQGNK NDLEMGIKAA RPEIADTATS
     EVPGSQASPN PVPGDGLHRA GFDAFMTGYV MAYVEVSQGP QPCSSGPWLP ECHNKVYLSG
     KAVPLTVAKS QFSRSSKAHN QKMKLAWGSS