TOE1_PONAB
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