TTF2_MOUSE
ID TTF2_MOUSE Reviewed; 1138 AA.
AC Q5NC05; Q4V9Y7; Q5M924;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transcription termination factor 2;
DE EC=3.6.4.-;
DE AltName: Full=RNA polymerase II termination factor;
DE AltName: Full=Transcription release factor 2;
GN Name=Ttf2;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic germ cell;
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 PROTEIN SEQUENCE OF 370-379, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: DsDNA-dependent ATPase which acts as a transcription
CC termination factor by coupling ATP hydrolysis with removal of RNA
CC polymerase II from the DNA template. May contribute to mitotic
CC transcription repression. May also be involved in pre-mRNA splicing (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDC5L. Part of the spliceosome (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Cytoplasmic during interphase. Relocates to the nucleus as cells
CC enter mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AL669872; CAM22070.1; -; Genomic_DNA.
DR EMBL; AL669937; CAI26225.2; -; Genomic_DNA.
DR EMBL; BC087733; AAH87733.1; -; mRNA.
DR EMBL; BC096625; AAH96625.1; -; mRNA.
DR CCDS; CCDS17679.1; -.
DR RefSeq; NP_001013044.2; NM_001013026.2.
DR AlphaFoldDB; Q5NC05; -.
DR SMR; Q5NC05; -.
DR BioGRID; 216447; 3.
DR IntAct; Q5NC05; 1.
DR STRING; 10090.ENSMUSP00000076208; -.
DR iPTMnet; Q5NC05; -.
DR PhosphoSitePlus; Q5NC05; -.
DR EPD; Q5NC05; -.
DR jPOST; Q5NC05; -.
DR MaxQB; Q5NC05; -.
DR PaxDb; Q5NC05; -.
DR PeptideAtlas; Q5NC05; -.
DR PRIDE; Q5NC05; -.
DR ProteomicsDB; 297678; -.
DR Antibodypedia; 1775; 190 antibodies from 26 providers.
DR DNASU; 74044; -.
DR Ensembl; ENSMUST00000076941; ENSMUSP00000076208; ENSMUSG00000033222.
DR GeneID; 74044; -.
DR KEGG; mmu:74044; -.
DR UCSC; uc008qrb.2; mouse.
DR CTD; 8458; -.
DR MGI; MGI:1921294; Ttf2.
DR VEuPathDB; HostDB:ENSMUSG00000033222; -.
DR eggNOG; KOG4439; Eukaryota.
DR GeneTree; ENSGT00940000162718; -.
DR HOGENOM; CLU_000315_2_2_1; -.
DR InParanoid; Q5NC05; -.
DR OMA; PEHGTFC; -.
DR OrthoDB; 132523at2759; -.
DR PhylomeDB; Q5NC05; -.
DR TreeFam; TF316297; -.
DR BioGRID-ORCS; 74044; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Ttf2; mouse.
DR PRO; PR:Q5NC05; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q5NC05; protein.
DR Bgee; ENSMUSG00000033222; Expressed in metanephric renal vesicle and 181 other tissues.
DR ExpressionAtlas; Q5NC05; baseline and differential.
DR Genevisible; Q5NC05; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR010666; Znf_GRF.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF06839; zf-GRF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; DNA-binding; Helicase;
KW Hydrolase; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Spliceosome; Transcription; Transcription regulation;
KW Transcription termination; Zinc; Zinc-finger.
FT CHAIN 1..1138
FT /note="Transcription termination factor 2"
FT /id="PRO_0000074377"
FT DOMAIN 559..762
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 971..1133
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 5..41
FT /note="GRF-type"
FT REGION 90..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 713..716
FT /note="DEAH box"
FT COMPBIAS 100..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 572..579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNY4"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNY4"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNY4"
FT CONFLICT 5
FT /note="K -> E (in Ref. 2; AAH87733)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="P -> R (in Ref. 1; CAI26225)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="S -> C (in Ref. 1; CAI26225)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="E -> EE (in Ref. 1; CAI26225)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="K -> E (in Ref. 2; AAH87733)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="T -> P (in Ref. 1; CAI26225)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..292
FT /note="TQR -> AQK (in Ref. 1; CAI26225)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="E -> G (in Ref. 1; CAI26225)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="Q -> K (in Ref. 1; CAI26225)"
FT /evidence="ECO:0000305"
FT CONFLICT 437..438
FT /note="PE -> SD (in Ref. 1; CAI26225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1138 AA; 125530 MW; EA46A8F37DECCC56 CRC64;
MDLVKCPEHG DACFLKTGVR DGPNKGKSFY VCRTNTCGFV QATDIPVSHC LLHEEFVVEL
QGLFLPQDKK EWRLFFRCAR TKAEGKQWCG NVPWRQDPNP KELSVTSKPQ QPSESQLHSP
SQPRNPFRVL NKNQKTLERK QFVEEGERKT ADKKLRENNE QLLDQRKEQK PKSNSRMEKD
PSSDLVATRQ SGGDREEQEK SKFQPKTKKA EGMASKQGHG EVLQGIPKGP HMSESESRGV
PNKPETLREK ETQLLVPSVP GQNPESKVQK EGHVSREPLK NGEAPSAQVT QRGLAQGPLQ
GPSKTWRPVP EAPAAPELCS GMAHHATSSS EDSEDDGVSS RPGSPLLFDS TVDSQKKGSL
QHSDQSVQRQ MPAASGVSKK GDSSDPAAQR ANLTTQLKQK KGTLAAVNIQ ALPDKGEKLL
KQIQALEDAL SALALSPEQG TKEKCSAQEP EQSNITKAAA APLHLVPPQP LPRPLIQPAS
SLGLKAGRQE TPEGASQCSG GHMNQHHLYN VWKITSEAID ELHRSLKSCP GETAVAEDPA
GLKVPLLLHQ KQALAWLLWR ESQKPQGGIL ADDMGLGKTL TMIALILTKK NQQKSKEKER
SEPVTWLSKN DSSVFTSSGT LIVCPASLIH HWKNEVEKRV TSNRLRIYLY HGPNRSRHAK
VLSTYDIVIT TYSLLAKEIP TTKQEGEVPG ANLSVEGTSA PLLQVVWARI ILDEAHNVKN
PRVQTSIAVC KLQAQARWAV TGTPIQNNLL DMYSLMKFLR CSPFDEFSLW KSQVDNGSMK
GGERLSILTK SLLLRRTKDQ LDSTGKPLVA LPARRCQLHR LKLSEDERAV YDIFLARSRS
ALQSYLKRQE GRGSHHGRSP DNPFSRVAQE FGSSVSQGCP AADSQRPSTV HVLSQLLRLR
QCCCHLSLLK SALDPTELES EGLVLSLEEQ LSALTLSKVD VSEPSPTVSL NGTCFKAELF
DDTRRSTKVS SLLAELEAIQ KGPGSQKSVI VSQWTSMLQV VALHLKKNRL TYATIDGSVN
PKQRMDLVEA FNHSQGPQVM LISLLAGGVG LNLTGGNHLF LLDMHWNPSL EDQACDRIYR
VGQKKDVVIH RFVCEGTVEE KILQLQEKKK DLAKQVLSGS EGPVTKLTLA DLKILFGI
