TA15B_ARATH
ID TA15B_ARATH Reviewed; 422 AA.
AC Q94KD0; Q6S7B1; Q9FGH5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Transcription initiation factor TFIID subunit 15b;
DE AltName: Full=TBP-associated factor 15b;
DE Short=AtTAF15b;
GN Name=TAF15B; OrderedLocusNames=At5g58470; ORFNames=MQJ2.60, MQJ2.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, NOMENCLATURE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15527982; DOI=10.1016/j.gene.2004.08.023;
RA Lago C., Clerici E., Mizzi L., Colombo L., Kater M.M.;
RT "TBP-associated factors in Arabidopsis.";
RL Gene 342:231-241(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-383, AND INTERACTION WITH TAF4; TAF4B;
RP TAF5; TAF12B AND TAF14.
RC STRAIN=cv. Columbia;
RX PubMed=17340043; DOI=10.1007/s11103-007-9135-1;
RA Lawit S.J., O'Grady K., Gurley W.B., Czarnecka-Verner E.;
RT "Yeast two-hybrid map of Arabidopsis TFIID.";
RL Plant Mol. Biol. 64:73-87(2007).
CC -!- FUNCTION: TAFs are components of the transcription factor IID (TFIID)
CC complex that is essential for mediating regulation of RNA polymerase
CC transcription. {ECO:0000250}.
CC -!- SUBUNIT: Component of the TFIID complex. TFIID is composed of TATA
CC binding protein (TBP) and a number of TBP-associated factors (TAFs)
CC whose MWs range from 14-217 kDa. Interacts with TAF4, TAF4B, TAF5,
CC TAF12B and TAF14. {ECO:0000269|PubMed:17340043}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and inflorescences.
CC {ECO:0000269|PubMed:15527982}.
CC -!- SIMILARITY: Belongs to the TAF15 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10262.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025632; BAB10262.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97056.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97057.1; -; Genomic_DNA.
DR EMBL; AF367294; AAK56282.1; -; mRNA.
DR EMBL; AY075677; AAL77684.1; -; mRNA.
DR EMBL; AK316814; BAH19528.1; -; mRNA.
DR EMBL; AY463619; AAR28021.1; -; mRNA.
DR RefSeq; NP_568879.3; NM_125233.4.
DR RefSeq; NP_851215.1; NM_180884.2.
DR AlphaFoldDB; Q94KD0; -.
DR SMR; Q94KD0; -.
DR BioGRID; 21204; 6.
DR IntAct; Q94KD0; 5.
DR STRING; 3702.AT5G58470.2; -.
DR iPTMnet; Q94KD0; -.
DR PaxDb; Q94KD0; -.
DR PRIDE; Q94KD0; -.
DR ProteomicsDB; 234113; -.
DR EnsemblPlants; AT5G58470.1; AT5G58470.1; AT5G58470.
DR EnsemblPlants; AT5G58470.2; AT5G58470.2; AT5G58470.
DR GeneID; 835960; -.
DR Gramene; AT5G58470.1; AT5G58470.1; AT5G58470.
DR Gramene; AT5G58470.2; AT5G58470.2; AT5G58470.
DR KEGG; ath:AT5G58470; -.
DR Araport; AT5G58470; -.
DR TAIR; locus:2171248; AT5G58470.
DR eggNOG; KOG1995; Eukaryota.
DR HOGENOM; CLU_050310_0_1_1; -.
DR InParanoid; Q94KD0; -.
DR OMA; QRENGSY; -.
DR OrthoDB; 1506052at2759; -.
DR PhylomeDB; Q94KD0; -.
DR PRO; PR:Q94KD0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94KD0; baseline and differential.
DR Genevisible; Q94KD0; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW Activator; Metal-binding; Nucleus; Reference proteome; RNA-binding;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..422
FT /note="Transcription initiation factor TFIID subunit 15b"
FT /id="PRO_0000424055"
FT DOMAIN 280..371
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 84..115
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 42316 MW; 0ED75C7F73575133 CRC64;
MAGMYNQDGG GGAPIPSYGG DGYGGGGGYG GGDAGYGGRG ASGGGSYGGR GGYGGGGGRG
NRGGGGGGYQ GGDRGGRGSG GGGRDGDWRC PNPSCGNVNF ARRVECNKCG ALAPSGTSSG
ANDRGGGGYS RGGGDSDRGG GRGGRNDSGR SYESSRYDGG SRSGGSYGSG SQRENGSYGQ
APPPAAAIPS YDGSGSYPPP TGYGMEAVPP PTSYSGGPPS YGGPRGGYGS DAPSTGGRGG
RSGGYDGGSA PRRQEASYED AATEKVKQCD ADCDDNCDNA RIYISNLPPD VTTDELKDLF
GGIGQVGRIK QKRGYKDQWP YNIKIYTDEK GNYKGDACLA YEDPSAAHSA GGFFNNYEMR
GNKISVTMAE KSAPRAPTFD QRGGGRGGGG GGYGGGGGDR RRDNYSSGPD RNHHGGNRSR
PY
