EBP1_ARATH
ID EBP1_ARATH Reviewed; 392 AA.
AC Q96327; B9DFJ0; F4J4J3; F4J4J5; Q9C5I5;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=ERBB-3 BINDING PROTEIN 1 {ECO:0000303|PubMed:17024182};
DE Short=AtEBP1 {ECO:0000303|PubMed:17024182};
DE AltName: Full=Proliferation-associated protein G2p {ECO:0000303|PubMed:17024182};
DE Short=AtG2 {ECO:0000303|PubMed:10645728};
DE AltName: Full=Protein CELL-PROLIFERATION-RELATED {ECO:0000303|PubMed:15689342};
DE Short=AtCPR {ECO:0000303|PubMed:15689342};
GN Name=EBP1 {ECO:0000303|PubMed:17024182};
GN Synonyms=CAM1 {ECO:0000312|EMBL:AAL25197.1},
GN CPR {ECO:0000303|PubMed:15689342};
GN OrderedLocusNames=At3g51800 {ECO:0000312|Araport:AT3G51800};
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 {ECO:0000312|EMBL:AAB18127.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Grellet F., Gaubier P., Wu H.-J., Laudie M., Berger C., Delseny M.;
RT "Structure of the Arabidopsis thaliana Em1 locus.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yiguo S., Shouyi C.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, INDUCTION,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15689342; DOI=10.1093/jxb/eri075;
RA Zhang W.-K., Shen Y.-G., He X.-J., Du B.-X., Xie Z.-M., Luo G.-Z.,
RA Zhang J.-S., Chen S.-Y.;
RT "Characterization of a novel cell cycle-related gene from Arabidopsis.";
RL J. Exp. Bot. 56:807-816(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10645728; DOI=10.1023/a:1006395324818;
RA Comella P., Wu H.-J., Laudie M., Berger C., Cooke R., Delseny M.,
RA Grellet F.;
RT "Fine sequence analysis of 60 kb around the Arabidopsis thaliana AtEm1
RT locus on chromosome III.";
RL Plant Mol. Biol. 41:687-700(1999).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH19507.1};
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 229-392 (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=10907847; DOI=10.1093/dnares/7.3.175;
RA Asamizu E., Nakamura Y., Sato S., Tabata S.;
RT "A large scale analysis of cDNA in Arabidopsis thaliana: generation of
RT 12,028 non-redundant expressed sequence tags from normalized and size-
RT selected cDNA libraries.";
RL DNA Res. 7:175-180(2000).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND INDUCTION BY
RP AUXIN.
RC STRAIN=cv. Columbia;
RX PubMed=17024182; DOI=10.1038/sj.emboj.7601362;
RA Horvath B.M., Magyar Z., Zhang Y., Hamburger A.W., Bako L., Visser R.G.F.,
RA Bachem C.W.B., Boegre L.;
RT "EBP1 regulates organ size through cell growth and proliferation in
RT plants.";
RL EMBO J. 25:4909-4920(2006).
RN [10]
RP INTERACTION WITH REIL1 AND REIL2.
RX PubMed=24603461; DOI=10.4161/psb.28224;
RA Schmidt S., Dethloff F., Beine-Golovchuk O., Kopka J.;
RT "REIL proteins of Arabidopsis thaliana interact in yeast-2-hybrid assays
RT with homologs of the yeast Rlp24, Rpl24A, Rlp24B, Arx1, and Jjj1
RT proteins.";
RL Plant Signal. Behav. 9:E28224-E28224(2014).
CC -!- FUNCTION: Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs,
CC several rRNA precursors and probably U3 small nucleolar RNA. May be
CC involved in regulation of intermediate and late steps of rRNA
CC processing. May be involved in ribosome assembly (By similarity).
CC Required for expression of cell cycle genes such as CYCD3-1, RNR2A and
CC CDKB1-1. Promotes, in a dose- and auxin-dependent manner, organ growth
CC by stimulating both cell proliferation and expansion, via the
CC regulation of RBR1 levels (PubMed:17024182).
CC {ECO:0000250|UniProtKB:Q9UQ80, ECO:0000269|PubMed:17024182}.
CC -!- SUBUNIT: Component of a ribonucleoprotein complex (By similarity).
CC Interacts with REIL1 AND REIL2 (PubMed:24603461).
CC {ECO:0000250|UniProtKB:Q9UQ80, ECO:0000269|PubMed:24603461}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15689342}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96327-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96327-2; Sequence=VSP_057636;
CC Name=3;
CC IsoId=Q96327-3; Sequence=VSP_057634;
CC Name=4;
CC IsoId=Q96327-4; Sequence=VSP_057635;
CC -!- TISSUE SPECIFICITY: Strongly expressed in calls, roots and flowers, to
CC a lower extent, in stems and siliques, but hardly detectable in leaves.
CC {ECO:0000269|PubMed:15689342}.
CC -!- DEVELOPMENTAL STAGE: Accumulates mostly in developing organs. During
CC early stages of organ development, promotes cell proliferation,
CC influences cell-size threshold for division and shortens the period of
CC meristematic activity. In postmitotic cells, enhances cell expansion.
CC {ECO:0000269|PubMed:17024182}.
CC -!- INDUCTION: Cell-cycle regulated expression with accumulation during the
CC G1-to-S phase (PubMed:15689342). Accumulates in response to auxin.
CC Expression levels correlate with genes involved in ribosome biogenesis
CC and function (PubMed:17024182). {ECO:0000269|PubMed:15689342,
CC ECO:0000269|PubMed:17024182}.
CC -!- DISRUPTION PHENOTYPE: Distorted reduced growth leading to small plants,
CC and impaired fertility. At the seedling stage, a delay in leaf
CC initiation and distorted leaf shape were characteristic of the silenced
CC lines. {ECO:0000269|PubMed:17024182}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. {ECO:0000305}.
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DR EMBL; U72503; AAB18127.1; -; mRNA.
DR EMBL; AF422841; AAM46648.1; -; mRNA.
DR EMBL; AY056616; AAL25197.1; -; mRNA.
DR EMBL; AY056617; AAL25198.1; -; Genomic_DNA.
DR EMBL; AF049236; AAC14407.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78844.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78845.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78846.1; -; Genomic_DNA.
DR EMBL; AF360226; AAK25936.1; -; mRNA.
DR EMBL; AY040067; AAK64125.1; -; mRNA.
DR EMBL; AY142627; AAN13085.1; -; mRNA.
DR EMBL; AK316789; BAH19507.1; -; mRNA.
DR EMBL; AV544387; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T51151; T51151.
DR RefSeq; NP_001190060.1; NM_001203131.1. [Q96327-4]
DR RefSeq; NP_190748.1; NM_115039.4. [Q96327-1]
DR RefSeq; NP_850679.1; NM_180348.3. [Q96327-3]
DR AlphaFoldDB; Q96327; -.
DR SMR; Q96327; -.
DR STRING; 3702.AT3G51800.2; -.
DR MEROPS; M24.978; -.
DR iPTMnet; Q96327; -.
DR MetOSite; Q96327; -.
DR SwissPalm; Q96327; -.
DR PaxDb; Q96327; -.
DR PRIDE; Q96327; -.
DR ProteomicsDB; 224715; -. [Q96327-1]
DR EnsemblPlants; AT3G51800.1; AT3G51800.1; AT3G51800. [Q96327-1]
DR EnsemblPlants; AT3G51800.2; AT3G51800.2; AT3G51800. [Q96327-3]
DR EnsemblPlants; AT3G51800.3; AT3G51800.3; AT3G51800. [Q96327-4]
DR GeneID; 824343; -.
DR Gramene; AT3G51800.1; AT3G51800.1; AT3G51800. [Q96327-1]
DR Gramene; AT3G51800.2; AT3G51800.2; AT3G51800. [Q96327-3]
DR Gramene; AT3G51800.3; AT3G51800.3; AT3G51800. [Q96327-4]
DR KEGG; ath:AT3G51800; -.
DR Araport; AT3G51800; -.
DR TAIR; locus:2074373; AT3G51800.
DR eggNOG; KOG2776; Eukaryota.
DR OMA; GMGPYIG; -.
DR OrthoDB; 834026at2759; -.
DR PhylomeDB; Q96327; -.
DR PRO; PR:Q96327; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96327; baseline and differential.
DR Genevisible; Q96327; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0044843; P:cell cycle G1/S phase transition; IEP:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR004545; PA2G4.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00495; crvDNA_42K; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Auxin signaling pathway; Developmental protein;
KW Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW rRNA processing.
FT CHAIN 1..392
FT /note="ERBB-3 BINDING PROTEIN 1"
FT /id="PRO_0000432961"
FT REGION 1..50
FT /note="Necessary for nucleolar localization"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ80"
FT REGION 48..56
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ80"
FT REGION 298..392
FT /note="Necessary for nucleolar localization"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ80"
FT REGION 355..372
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P50580"
FT REGION 358..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 357..367
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT VAR_SEQ 308
FT /note="K -> KPGSCRFGFL (in isoform 3)"
FT /id="VSP_057634"
FT VAR_SEQ 357..363
FT /note="Missing (in isoform 4)"
FT /id="VSP_057635"
FT VAR_SEQ 363..392
FT /note="Missing (in isoform 2)"
FT /id="VSP_057636"
FT CONFLICT 52
FT /note="E -> D (in Ref. 6; AAK25936/AAK64125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 42979 MW; 67B1468F0A73E27A CRC64;
MSSDDERDEK ELSLTSPEVV TKYKSAAEIV NKALQVVLAE CKPKAKIVDI CEKGDSFIKE
QTASMYKNSK KKIERGVAFP TCISVNNTVG HFSPLASDES VLEDGDMVKI DMGCHIDGFI
ALVGHTHVLQ EGPLSGRKAD VIAAANTAAD VALRLVRPGK KNTDVTEAIQ KVAAAYDCKI
VEGVLSHQLK QHVIDGNKVV LSVSSPETTV DEVEFEENEV YAIDIVASTG DGKPKLLDEK
QTTIYKKDES VNYQLKMKAS RFIISEIKQN FPRMPFTARS LEEKRARLGL VECVNHGHLQ
PYPVLYEKPG DFVAQIKFTV LLMPNGSDRI TSHTLQELPK KTIEDPEIKG WLALGIKKKK
GGGKKKKAQK AGEKGEASTE AEPMDASSNA QE
