MEE12_ARATH
ID MEE12_ARATH Reviewed; 666 AA.
AC Q5XVF0; Q5XVE8; Q5XVE9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit B;
DE AltName: Full=Central cell guidance protein;
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 12;
DE AltName: Full=TATA box-binding protein-associated factor 1B;
DE Short=TBP-associated factor 1B;
GN Name=MEE12 {ECO:0000303|PubMed:15634699}; Synonyms=CCG;
GN OrderedLocusNames=At2g02955; ORFNames=T17M13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH TFIIF,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18055609; DOI=10.1105/tpc.107.053967;
RA Chen Y.H., Li H.J., Shi D.Q., Yuan L., Liu J., Sreenivasan R., Baskar R.,
RA Grossniklaus U., Yang W.C.;
RT "The central cell plays a critical role in pollen tube guidance in
RT Arabidopsis.";
RL Plant Cell 19:3563-3577(2007).
RN [6]
RP FUNCTION, AND INTERACTION WITH MEE14/CBP1; TBP1; TFIIF AND NRPB1.
RX PubMed=26462908; DOI=10.1105/tpc.15.00370;
RA Li H.J., Zhu S.S., Zhang M.X., Wang T., Liang L., Xue Y., Shi D.Q., Liu J.,
RA Yang W.C.;
RT "Arabidopsis CBP1 is a novel regulator of transcription initiation in
RT central cell-mediated pollen tube guidance.";
RL Plant Cell 27:2880-2893(2015).
CC -!- FUNCTION: Component of RNA polymerase I core factor complex that acts
CC as a GTF2B/TFIIB-like factor and plays a key role in multiple steps
CC during transcription initiation such as pre-initiation complex (PIC)
CC assembly and postpolymerase recruitment events in polymerase I (Pol I)
CC transcription. Binds rDNA promoters and plays a role in Pol I
CC recruitment (By similarity). Required for the development of the one-
CC cell zygote and endosperm in embryos (PubMed:15634699). Required for
CC micropylar pollen tube guidance, but has no effect on ovule development
CC and gametophytic cell fate specification (PubMed:18055609). May
CC regulate the transcription of secreted cysteine-rich peptide (CRP)
CC genes in the embryo sac (PubMed:26462908).
CC {ECO:0000250|UniProtKB:P40992, ECO:0000269|PubMed:15634699,
CC ECO:0000269|PubMed:18055609, ECO:0000269|PubMed:26462908}.
CC -!- SUBUNIT: Interacts with TFIIF (PubMed:18055609, PubMed:26462908).
CC Interacts with MEE14/CBP1, TBP1 and NRPB1 (via CTD) (PubMed:26462908).
CC {ECO:0000269|PubMed:18055609, ECO:0000269|PubMed:26462908}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:18055609}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5XVF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XVF0-2; Sequence=VSP_042978, VSP_042979;
CC Name=3;
CC IsoId=Q5XVF0-3; Sequence=VSP_042977;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in seedlings,
CC inflorescences and young siliques and at lower levels in roots. Not
CC detected in leaves and stems. Detected in root tips and shoot apical
CC meristems, in anthers, primarily in microspores with weaker expression
CC in mature pollen grains and in the central cell of the mature female
CC gametophyte. Not expressed in synergids, egg cells, antipodal cells,
CC endosperm cells and fertilized egg cells.
CC {ECO:0000269|PubMed:18055609}.
CC -!- DEVELOPMENTAL STAGE: Expression in central cell of the mature female
CC gametophyte is pollination independent. {ECO:0000269|PubMed:18055609}.
CC -!- DOMAIN: Although it shares weak sequence similarity with GTF2B/TFIIB,
CC displays a similar subdomain organization as GTF2B/TFIIB, with a N-
CC terminal zinc finger, a connecting region (composed of B-reader and B-
CC linker regions), followed by 2 cyclin folds. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Disrupted function of the female gametophyte.
CC Defective in micropylar pollen tube guidance leading to zygotic
CC lethality. {ECO:0000269|PubMed:18055609}.
CC -!- MISCELLANEOUS: Expression of MEE12 in the central cell alone is
CC sufficient to restore the normal pollen tube guidance phenotype.
CC -!- SIMILARITY: Belongs to the RRN7/TAF1B family. {ECO:0000305}.
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DR EMBL; AC004138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC05644.1; -; Genomic_DNA.
DR EMBL; AY735572; AAU44442.1; -; mRNA.
DR EMBL; AY735573; AAU44443.1; -; mRNA.
DR EMBL; AY735574; AAU44444.1; -; mRNA.
DR RefSeq; NP_671769.1; NM_147236.3. [Q5XVF0-1]
DR AlphaFoldDB; Q5XVF0; -.
DR STRING; 3702.AT2G02955.1; -.
DR PaxDb; Q5XVF0; -.
DR PRIDE; Q5XVF0; -.
DR ProteomicsDB; 250637; -. [Q5XVF0-1]
DR EnsemblPlants; AT2G02955.1; AT2G02955.1; AT2G02955. [Q5XVF0-1]
DR GeneID; 814824; -.
DR Gramene; AT2G02955.1; AT2G02955.1; AT2G02955. [Q5XVF0-1]
DR KEGG; ath:AT2G02955; -.
DR Araport; AT2G02955; -.
DR TAIR; locus:504955973; AT2G02955.
DR eggNOG; KOG1988; Eukaryota.
DR HOGENOM; CLU_011285_1_0_1; -.
DR InParanoid; Q5XVF0; -.
DR OMA; MIWFRSL; -.
DR OrthoDB; 867780at2759; -.
DR PhylomeDB; Q5XVF0; -.
DR PRO; PR:Q5XVF0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5XVF0; baseline and differential.
DR GO; GO:0070860; C:RNA polymerase I core factor complex; IBA:GO_Central.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; ISS:UniProtKB.
DR InterPro; IPR033599; TAF1B/Rrn7.
DR InterPro; IPR021752; TF_Rrn7_Zf.
DR PANTHER; PTHR31576; PTHR31576; 1.
DR Pfam; PF11781; zf-RRN7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..666
FT /note="TATA box-binding protein-associated factor RNA
FT polymerase I subunit B"
FT /id="PRO_0000416877"
FT ZN_FING 1..29
FT /note="RRN7-type"
FT REGION 30..64
FT /note="B-reader"
FT /evidence="ECO:0000250"
FT REGION 45..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..80
FT /note="B-linker"
FT /evidence="ECO:0000250"
FT REGION 81..285
FT /note="N-terminal cyclin fold"
FT /evidence="ECO:0000250"
FT REGION 189..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..288
FT /note="C-terminal cyclin fold"
FT /evidence="ECO:0000250"
FT REGION 515..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..140
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_042977"
FT VAR_SEQ 290..293
FT /note="VSIM -> LQTI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_042978"
FT VAR_SEQ 294..666
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_042979"
SQ SEQUENCE 666 AA; 75475 MW; 4435D960808ADFCC CRC64;
MICTECENDA FDEEDDGYYY CQRCGVQVEN LIQTGVDDGD LIGEGGGTQG ALYNPKHRRT
EPQPITPSQP RFTDDTSRYS QFKSQFESEN GNKELPREVK RAPDSYVDKE PTEPVDFAAE
TLSYENYYDE ARDRYVKAFL MMITYQCDAL VDKFNVTPLI IGLVGPISLR YVALSGVYHK
DWANNAIRDS EHQSEDGEVK DAKRLKRHKA EPRNIDGKRA VTIWFGILKK TMPLSSSLVI
SFLACHQAGA PVLPTDIVRW AREGKLPYLS CFLDIREQMG ERSAACPVKV SIMARPFQVI
SAQMLEARAS VIADTIGLPL PPVNFYGIAS NYIKQLSIPE DKILDLARLI QNWSLPPELY
LSTNEQKLPS RVCVMSILIV AIRMLYNING LGVWERSLGF VNASDGDSET NSGTAEKATE
FDTQELLKNL EAKYHEVAAE TLESEKDLVS YLSLGKNEFF AGLEEDSPDD TYRIVDNLWN
GYPKDEDIEC LPKRGRDWDD DVSLNQLSLY DSRFSDGNNP CSSSSRRNES VSIGLDLSSS
EHRESSSPEK LKEIAIKRLI TDMGDDLFCY IPPRVKVKRL DYLQYVRKKE DGALIYAAHA
DYYILLRVCA KVAEIDVRNM HRGVLSFERR LAWIEKRIDQ VLHLTRPLMT CKHCCDDGNI
GEDQDD
