TCEA3_MOUSE
ID TCEA3_MOUSE Reviewed; 347 AA.
AC P23881; A2AW46; O88710; Q9CTZ8; Q9DCZ5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Transcription elongation factor A protein 3;
DE AltName: Full=Transcription elongation factor S-II protein 3;
DE AltName: Full=Transcription elongation factor TFIIS.h;
GN Name=Tcea3; Synonyms=Tfiish;
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=1917889; DOI=10.1093/oxfordjournals.jbchem.a123439;
RA Kanai A., Kuzuhara T., Sekimizu K., Natori S.;
RT "Heterogeneity and tissue-specific expression of eukaryotic transcription
RT factor S-II-related protein mRNA.";
RL J. Biochem. 109:674-677(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hirashima S., Hirai H., Nakanishi Y., Natori S.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetus;
RX PubMed=9790746; DOI=10.1006/geno.1998.5449;
RA Labhart P., Morgan G.T.;
RT "Identification of novel genes encoding transcription elongation factor
RT TFIIS (TCEA) in vertebrates: conservation of three distinct TFIIS isoforms
RT in frog, mouse, and human.";
RL Genomics 52:278-288(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Pancreas;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
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).
RN [8]
RP STRUCTURE BY NMR OF 1-90.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal domain I of mouse transcription
RT elongation factor S-II protein 3.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Necessary for efficient RNA polymerase II transcription
CC elongation past template-encoded arresting sites. The arresting sites
CC in DNA have the property of trapping a certain fraction of elongating
CC RNA polymerases that pass through, resulting in locked ternary
CC complexes. Cleavage of the nascent transcript by S-II allows the
CC resumption of elongation from the new 3'-terminus.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Liver, kidney and heart.
CC -!- SIMILARITY: Belongs to the TFS-II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA28177.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. The sequence from position 1 to 95 is due to a chimeric cDNA.; Evidence={ECO:0000305};
CC Sequence=BAB31514.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; D00926; BAA28177.1; ALT_SEQ; mRNA.
DR EMBL; AJ223472; CAA11392.1; -; mRNA.
DR EMBL; AK002319; BAB22010.1; -; mRNA.
DR EMBL; AK007437; BAB25037.1; -; mRNA.
DR EMBL; AK019024; BAB31514.2; ALT_SEQ; mRNA.
DR EMBL; AL935264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010807; AAH10807.1; -; mRNA.
DR CCDS; CCDS18803.1; -.
DR RefSeq; NP_035672.1; NM_011542.2.
DR PDB; 1WJT; NMR; -; A=1-90.
DR PDBsum; 1WJT; -.
DR AlphaFoldDB; P23881; -.
DR BMRB; P23881; -.
DR SMR; P23881; -.
DR BioGRID; 203997; 3.
DR STRING; 10090.ENSMUSP00000099592; -.
DR iPTMnet; P23881; -.
DR PhosphoSitePlus; P23881; -.
DR MaxQB; P23881; -.
DR PaxDb; P23881; -.
DR PeptideAtlas; P23881; -.
DR PRIDE; P23881; -.
DR ProteomicsDB; 254678; -.
DR Antibodypedia; 8084; 203 antibodies from 24 providers.
DR DNASU; 21401; -.
DR Ensembl; ENSMUST00000102533; ENSMUSP00000099592; ENSMUSG00000001604.
DR GeneID; 21401; -.
DR KEGG; mmu:21401; -.
DR UCSC; uc008vhv.2; mouse.
DR CTD; 6920; -.
DR MGI; MGI:1196908; Tcea3.
DR VEuPathDB; HostDB:ENSMUSG00000001604; -.
DR eggNOG; KOG1105; Eukaryota.
DR GeneTree; ENSGT00940000157034; -.
DR HOGENOM; CLU_037637_2_0_1; -.
DR InParanoid; P23881; -.
DR OMA; RKNMEGA; -.
DR OrthoDB; 1579101at2759; -.
DR PhylomeDB; P23881; -.
DR TreeFam; TF314970; -.
DR BioGRID-ORCS; 21401; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Tcea3; mouse.
DR EvolutionaryTrace; P23881; -.
DR PRO; PR:P23881; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P23881; protein.
DR Bgee; ENSMUSG00000001604; Expressed in hindlimb stylopod muscle and 160 other tissues.
DR ExpressionAtlas; P23881; baseline and differential.
DR Genevisible; P23881; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035100; TF_IIS-typ.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR036575; TFIIS_cen_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR006289; TFSII.
DR InterPro; IPR001222; Znf_TFIIS.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR PIRSF; PIRSF006704; TF_IIS; 1.
DR SMART; SM00510; TFS2M; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF46942; SSF46942; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR TIGRFAMs; TIGR01385; TFSII; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..347
FT /note="Transcription elongation factor A protein 3"
FT /id="PRO_0000121453"
FT DOMAIN 5..82
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 186..302
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 305..345
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT REGION 83..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75764"
FT CONFLICT 7
FT /note="L -> P (in Ref. 4; BAB25037)"
FT /evidence="ECO:0000305"
FT CONFLICT 63..64
FT /note="EV -> VL (in Ref. 4; BAB25037)"
FT /evidence="ECO:0000305"
FT CONFLICT 96..99
FT /note="KKEK -> RREE (in Ref. 4; BAB25037)"
FT /evidence="ECO:0000305"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:1WJT"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:1WJT"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:1WJT"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1WJT"
FT HELIX 63..78
FT /evidence="ECO:0007829|PDB:1WJT"
SQ SEQUENCE 347 AA; 38850 MW; A1711D4C5DAF8CC8 CRC64;
MGLEEELLRI AKKLEKMVSR KKTEGALDLL KKLNSCQMSI QLLQTTRIGV AVNGVRKHCS
DKEVVSLAKV LIKNWKRLLD SPRTTKGERE EREKAKKEKG LGCSDWKPEA GLSPPRKKGG
GEPKTRRDSV DSRSSTTSSP KRPSLERSNS SKSKVETPTT PSSPSTPTFA PAVCLLAPCY
LTGDSVRDKC VEMLSAALKA EDNFKDYGVN CDKLASEIED HIYQELKSTD MKYRNRVRSR
ISNLKDPRNP GLRRNVLSGA ISPELIAKMT AEEMASDELR ELRNAMTQEA IREHQMAKTG
GTTTDLLRCS KCKKKNCTYN QVQTRSADEP MTTFVLCNEC GNRWKFC
