PCEP3_ARATH
ID PCEP3_ARATH Reviewed; 82 AA.
AC O80460;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Precursor of CEP3 {ECO:0000303|PubMed:24179096};
DE Short=PCEP3 {ECO:0000303|PubMed:24179096};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 3 {ECO:0000303|PubMed:24179096};
DE Short=CEP3 {ECO:0000303|PubMed:24179096};
DE Flags: Precursor;
GN Name=CEP3 {ECO:0000303|PubMed:24179096};
GN OrderedLocusNames=At2g23440 {ECO:0000312|Araport:AT2G23440};
GN ORFNames=F26B6.9 {ECO:0000312|EMBL:AEC07455.1};
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].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=18315543; DOI=10.1111/j.1365-313x.2008.03464.x;
RA Ohyama K., Ogawa M., Matsubayashi Y.;
RT "Identification of a biologically active, small, secreted peptide in
RT Arabidopsis by in silico gene screening, followed by LC-MS-based structure
RT analysis.";
RL Plant J. 55:152-160(2008).
RN [5]
RP REVIEW.
RX PubMed=22303274; DOI=10.1199/tab.0150;
RA Matsubayashi Y.;
RT "Small post-translationally modified Peptide signals in Arabidopsis.";
RL Arabidopsis Book 9:E0150-E0150(2011).
RN [6]
RP TISSUE SPECIFICITY, INDUCTION BY AUXIN; POTASSIUM AND NITROGEN, AND GENE
RP FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=24179095; DOI=10.1093/jxb/ert331;
RA Roberts I., Smith S., De Rybel B., Van Den Broeke J., Smet W.,
RA De Cokere S., Mispelaere M., De Smet I., Beeckman T.;
RT "The CEP family in land plants: evolutionary analyses, expression studies,
RT and role in Arabidopsis shoot development.";
RL J. Exp. Bot. 64:5371-5381(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY OSMOTIC STRESS; CARBON
RP DIOXIDE; NITROGEN DEPLETION AND NITRATE DEPLETION, HYDROXYLATION AT PRO-67
RP AND PRO-74, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=24179096; DOI=10.1093/jxb/ert332;
RA Delay C., Imin N., Djordjevic M.A.;
RT "CEP genes regulate root and shoot development in response to environmental
RT cues and are specific to seed plants.";
RL J. Exp. Bot. 64:5383-5394(2013).
RN [8]
RP PROTEIN SEQUENCE OF 64-78, PTM, FUNCTION, HYDROXYLATION AT PRO-67 AND
RP PRO-74, INTERACTION WITH CEPR1, INDUCTION BY NITROGEN DEPLETION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. No-0;
RX PubMed=25324386; DOI=10.1126/science.1257800;
RA Tabata R., Sumida K., Yoshii T., Ohyama K., Shinohara H., Matsubayashi Y.;
RT "Perception of root-derived peptides by shoot LRR-RKs mediates systemic N-
RT demand signaling.";
RL Science 346:343-346(2014).
CC -!- FUNCTION: Extracellular signaling peptide that represses primary root
CC growth rate and significantly inhibits lateral root formation. Promotes
CC shoot growth. Modulates leaf morphology (PubMed:24179096). Regulates
CC systemic nitrogen (N)-demand signaling. Mediates systemic up-regulation
CC of genes involved in N uptake and assimilation pathways
CC (PubMed:25324386). {ECO:0000269|PubMed:24179096,
CC ECO:0000269|PubMed:25324386}.
CC -!- SUBUNIT: Interacts with the CEP receptor CEPR1.
CC {ECO:0000269|PubMed:25324386}.
CC -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 3]: Secreted,
CC extracellular space, apoplast {ECO:0000269|PubMed:25324386}.
CC Note=Accumulates in xylem sap under nitrogen (N)-starved conditions.
CC {ECO:0000269|PubMed:25324386}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots (PubMed:18315543).
CC Present in lateral roots (especially in vasculature), root-hypocotyl
CC junction and cotyledons (PubMed:24179095).
CC {ECO:0000269|PubMed:18315543, ECO:0000269|PubMed:24179095}.
CC -!- INDUCTION: Induced by auxin, but repressed by potassium (K) and
CC nitrogen (N) (PubMed:24179095). Accumulates strongly in the roots under
CC nitrogen depletion, and in the shoots under nitrate limitation
CC (PubMed:24179095, PubMed:25324386). Also induced by osmotic stress
CC (e.g. mannitol and NaCl). Strongly repressed in roots by carbon dioxide
CC CO(2) (PubMed:24179095). {ECO:0000269|PubMed:24179095,
CC ECO:0000269|PubMed:25324386}.
CC -!- PTM: The mature small signaling peptide is generated by proteolytic
CC processing of the longer precursor. {ECO:0000269|PubMed:25324386}.
CC -!- DISRUPTION PHENOTYPE: Larger root systems when grown under nitrogen-
CC limiting, acidic, osmotic stress (e.g. mannitol) and high salt
CC conditions, as well as in the presence of sucrose and under decreased
CC or increased light irradiance. Reduced the lateral root density at low
CC temperature (16 degrees Celsius). Increased root and shoot growth when
CC grown hydroponically. {ECO:0000269|PubMed:24179096}.
CC -!- SIMILARITY: Belongs to the C-terminally encoded plant signaling peptide
CC (CEP) family. {ECO:0000305}.
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DR EMBL; AC003040; AAC23759.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07455.1; -; Genomic_DNA.
DR EMBL; BT010787; AAR24154.1; -; mRNA.
DR EMBL; BT011268; AAR92304.1; -; mRNA.
DR PIR; T01133; T01133.
DR RefSeq; NP_179925.1; NM_127908.2.
DR AlphaFoldDB; O80460; -.
DR PaxDb; O80460; -.
DR EnsemblPlants; AT2G23440.1; AT2G23440.1; AT2G23440.
DR GeneID; 816876; -.
DR Gramene; AT2G23440.1; AT2G23440.1; AT2G23440.
DR KEGG; ath:AT2G23440; -.
DR Araport; AT2G23440; -.
DR TAIR; locus:2046798; AT2G23440.
DR eggNOG; ENOG502SXXE; Eukaryota.
DR HOGENOM; CLU_175062_1_0_1; -.
DR InParanoid; O80460; -.
DR OMA; VNVYLFA; -.
DR OrthoDB; 1568083at2759; -.
DR PhylomeDB; O80460; -.
DR PRO; PR:O80460; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80460; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IDA:UniProtKB.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:UniProtKB.
DR GO; GO:1902025; P:nitrate import; IDA:UniProtKB.
DR GO; GO:2000023; P:regulation of lateral root development; IDA:UniProtKB.
DR GO; GO:1901371; P:regulation of leaf morphogenesis; IMP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IDA:UniProtKB.
DR GO; GO:0048831; P:regulation of shoot system development; IMP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0010037; P:response to carbon dioxide; IEP:UniProtKB.
DR GO; GO:0009642; P:response to light intensity; IMP:UniProtKB.
DR GO; GO:0090548; P:response to nitrate starvation; IEP:UniProtKB.
DR GO; GO:1901698; P:response to nitrogen compound; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0035864; P:response to potassium ion; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IMP:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IDA:TAIR.
DR InterPro; IPR033250; CEP.
DR PANTHER; PTHR33348; PTHR33348; 1.
PE 1: Evidence at protein level;
KW Apoplast; Developmental protein; Direct protein sequencing; Hormone;
KW Hydroxylation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..63
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439968"
FT PEPTIDE 64..78
FT /note="C-terminally encoded peptide 3"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439969"
FT PROPEP 79..82
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439970"
FT REGION 40..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:24179096,
FT ECO:0000269|PubMed:25324386"
FT MOD_RES 70
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:Q058G9"
FT MOD_RES 74
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:24179096,
FT ECO:0000269|PubMed:25324386"
SQ SEQUENCE 82 AA; 8693 MW; AE26B2D03EADF4CA CRC64;
MATINVYVFA FIFLLTISVG SIEGRKLTKF TVTTSEEIRA GGSVLSSSPP TEPLESPPSH
GVDTFRPTEP GHSPGIGHSV HN
