TOE1_MOUSE
ID TOE1_MOUSE Reviewed; 511 AA.
AC Q9D2E2; Q3UFD8; Q8R5A4; Q9D412;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Target of EGR1 protein 1;
GN Name=Toe1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Spinal cord, Sympathetic ganglion, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D2E2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D2E2-2; Sequence=VSP_022242, VSP_022243;
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; AK016889; BAB30482.1; -; mRNA.
DR EMBL; AK019829; BAB31871.1; -; mRNA.
DR EMBL; AK046576; BAC32792.1; -; mRNA.
DR EMBL; AK082975; BAC38718.1; -; mRNA.
DR EMBL; AK148609; BAE28623.1; -; mRNA.
DR EMBL; BC023109; AAH23109.1; -; mRNA.
DR CCDS; CCDS18517.1; -. [Q9D2E2-1]
DR RefSeq; NP_080930.1; NM_026654.2. [Q9D2E2-1]
DR AlphaFoldDB; Q9D2E2; -.
DR SMR; Q9D2E2; -.
DR BioGRID; 212779; 2.
DR IntAct; Q9D2E2; 2.
DR STRING; 10090.ENSMUSP00000030451; -.
DR iPTMnet; Q9D2E2; -.
DR PhosphoSitePlus; Q9D2E2; -.
DR EPD; Q9D2E2; -.
DR jPOST; Q9D2E2; -.
DR MaxQB; Q9D2E2; -.
DR PaxDb; Q9D2E2; -.
DR PeptideAtlas; Q9D2E2; -.
DR PRIDE; Q9D2E2; -.
DR ProteomicsDB; 259486; -. [Q9D2E2-1]
DR ProteomicsDB; 259487; -. [Q9D2E2-2]
DR Antibodypedia; 18606; 191 antibodies from 28 providers.
DR Ensembl; ENSMUST00000030451; ENSMUSP00000030451; ENSMUSG00000028688. [Q9D2E2-1]
DR Ensembl; ENSMUST00000106455; ENSMUSP00000102063; ENSMUSG00000028688. [Q9D2E2-2]
DR GeneID; 68276; -.
DR KEGG; mmu:68276; -.
DR UCSC; uc008uhk.1; mouse. [Q9D2E2-1]
DR CTD; 114034; -.
DR MGI; MGI:1915526; Toe1.
DR VEuPathDB; HostDB:ENSMUSG00000028688; -.
DR eggNOG; KOG1990; Eukaryota.
DR GeneTree; ENSGT00940000153167; -.
DR HOGENOM; CLU_044804_1_0_1; -.
DR InParanoid; Q9D2E2; -.
DR OMA; LLCTEDY; -.
DR OrthoDB; 1402758at2759; -.
DR PhylomeDB; Q9D2E2; -.
DR TreeFam; TF314502; -.
DR BioGRID-ORCS; 68276; 27 hits in 76 CRISPR screens.
DR ChiTaRS; Toe1; mouse.
DR PRO; PR:Q9D2E2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D2E2; protein.
DR Bgee; ENSMUSG00000028688; Expressed in humerus cartilage element and 239 other tissues.
DR ExpressionAtlas; Q9D2E2; baseline and differential.
DR Genevisible; Q9D2E2; MM.
DR GO; GO:0015030; C:Cajal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0017069; F:snRNA binding; ISS:UniProtKB.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96GM8"
FT CHAIN 2..511
FT /note="Target of EGR1 protein 1"
FT /id="PRO_0000270834"
FT ZN_FING 295..323
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 336..348
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 367..394
FT /note="Basic and acidic 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 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GM8"
FT VAR_SEQ 306..329
FT /note="AYGWCPLGPQCPQSHDIDLIIDTD -> HTRSRFTGQLWETTIFPVEKLKDI
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022242"
FT VAR_SEQ 330..511
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022243"
FT CONFLICT 8
FT /note="D -> G (in Ref. 2; AAH23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="P -> S (in Ref. 2; AAH23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="P -> S (in Ref. 2; AAH23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="I -> M (in Ref. 2; AAH23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="R -> W (in Ref. 1; BAB30482)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="S -> R (in Ref. 2; AAH23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> V (in Ref. 2; AAH23109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 56871 MW; B7E9946A352BED90 CRC64;
MAADSDDDVP PVPTPSDGGV NKNTQPAEEF VVRVPVVDVQ SDNFKEIWPS LLLALKTASF
VAVDTELSGL GDRKSLLNQC IEERYKAVCH AARTRSVLSL GLACFRQQPD KGENSYLAQV
FNLTLLCIEE YVIEPKSVQF LVQHGFNFNR QYAQGIPYHK GNDKGDESQS QSVRTLFLEL
IRARRPLVLH NGLIDLVFLY QNFYAHLPEN LGTFTADLCE MFPAGIYDTK YAAEFHARFV
ASYLEYAFRK CERENGKQRA AGSPHLALEF CSYPSSMSGH IDYRCCMSPG TCRRSRTTGI
CDKFSAYGWC PLGPQCPQSH DIDLIIDTDE AVAEDKRRRR RRKDKRKRSL QSQPGTQTLA
EAEDGPPTKQ VCEDSLETEK MEQKVAEGEA GDQPGSREGH TSSLEMAHRR TSAETADVAT
SELLVNQAST NPVPGDGLHR AGFDAFMTGY VMAYVGLSQG LQLCSSEPWL PECHNKVYLS
GKTVPLTVTK SQFSRPSKAH NQKMKLAWGS S
