EBP1_SOLTU
ID EBP1_SOLTU Reviewed; 387 AA.
AC M1CZC0; A0FH76;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=ERBB-3 BINDING PROTEIN 1 {ECO:0000303|PubMed:17024182};
DE Short=StEBP1 {ECO:0000303|PubMed:17024182};
GN Name=EBP1 {ECO:0000303|PubMed:17024182};
GN ORFNames=PGSC0003DMG400030365
GN {ECO:0000312|EnsemblPlants:PGSC0003DMT400078068};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000312|Proteomes:UP000011115};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Karnico;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
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.
CC {ECO:0000250|UniProtKB:Q9UQ80}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96327,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- TISSUE SPECIFICITY: Expressed during tuberisation and in roots, nodes,
CC internodes, petioles, leaves, stolons, tubers and sprouts.
CC {ECO:0000269|PubMed:17024182}.
CC -!- DEVELOPMENTAL STAGE: Expression correlated with organs growth and cell
CC division activities. {ECO:0000269|PubMed:17024182}.
CC -!- DISRUPTION PHENOTYPE: Growth retardation leading to small dwarfed plant
CC and reduced tuber yield. Young developing leaves contains a reduced
CC number of larger cells than controls, whereas at later stages, during
CC expansion growth, the cell size is abnormally small.
CC {ECO:0000269|PubMed:17024182}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ995336; ABJ97690.1; -; mRNA.
DR RefSeq; NP_001275188.1; NM_001288259.1.
DR RefSeq; XP_015165673.1; XM_015310187.1.
DR AlphaFoldDB; M1CZC0; -.
DR SMR; M1CZC0; -.
DR STRING; 4113.PGSC0003DMT400078068; -.
DR MEROPS; M24.973; -.
DR PRIDE; M1CZC0; -.
DR EnsemblPlants; PGSC0003DMT400078068; PGSC0003DMT400078068; PGSC0003DMG400030365.
DR GeneID; 102577813; -.
DR Gramene; PGSC0003DMT400078068; PGSC0003DMT400078068; PGSC0003DMG400030365.
DR KEGG; sot:102577813; -.
DR eggNOG; KOG2776; Eukaryota.
DR HOGENOM; CLU_041451_2_0_1; -.
DR InParanoid; M1CZC0; -.
DR OMA; HTVLLMP; -.
DR OrthoDB; 834026at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0044843; P:cell cycle G1/S phase transition; ISS: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 2: Evidence at transcript level;
KW Auxin signaling pathway; Developmental protein; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing.
FT CHAIN 1..387
FT /note="ERBB-3 BINDING PROTEIN 1"
FT /id="PRO_0000432962"
FT REGION 1..49
FT /note="Necessary for nucleolar localization"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ80"
FT REGION 47..55
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ80"
FT REGION 297..387
FT /note="Necessary for nucleolar localization"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ80"
FT REGION 337..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..373
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P50580"
FT MOTIF 360..369
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 370..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 44
FT /note="A -> V (in Ref. 1; ABJ97690)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="V -> I (in Ref. 1; ABJ97690)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="T -> A (in Ref. 1; ABJ97690)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="S -> N (in Ref. 1; ABJ97690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 42740 MW; EFBC848EF20FDAD6 CRC64;
MSDDEREEKE LDLTSPEVVT KYKSAAEIVN KALQLVLSEC KPKAKIVDLC EKGDAFIKEQ
TGNMYKNVKK KIERGVAFPT CISVNNTVCH FSPLASDETV VEEGDILKID MGCHIDGFIA
VVGHTHVLHE GPVTGRAADV IAATNTAAEV ALRLVRPGKK NSDVTEAIQK VAAAYDCKIV
EGVLSHQMKQ FVIDGNKVVL SVSNPDTRVD EAEFEENEVY SIDIVTSTGD GKPKLLDEKQ
TTIYKRAVDK SYNLKMKASR FIFSEISQKF PIMPFTARDL EEKRARLGLV ECVNHELLQP
YPVLHEKPGD LVAHIKFTVL LMPNGSDRVT SHALQELQPT KTTENEPEIK AWLALPTKTK
KKGGGKKKKG KKGDKVEEAS QAEPMEG
