PCEP5_ARATH
ID PCEP5_ARATH Reviewed; 105 AA.
AC Q058G9; Q8LEN0;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Precursor of CEP5 {ECO:0000303|PubMed:24179096};
DE Short=PCEP5 {ECO:0000303|PubMed:24179096};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 5 {ECO:0000303|PubMed:24179096};
DE Short=CEP5 {ECO:0000303|PubMed:24179096};
DE Flags: Precursor;
GN Name=CEP5 {ECO:0000303|PubMed:24179096};
GN OrderedLocusNames=At5g66815 {ECO:0000312|Araport:AT5G66815};
GN ORFNames=MUD21 {ECO:0000305};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY
RP GIBBERELLIC ACID; PHOSPHORUS; BRASSINOSTEROIDS; AUXIN; SALICYLIC ACID AND
RP NITROGEN, AND GENE 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 [8]
RP FUNCTION, INDUCTION BY OSMOTIC STRESS; AMMONIUM CHLORIDE STARVATION;
RP NITROGEN DEPLETION AND NITRATE DEPLETION, HYDROXYLATION AT PRO-89 AND
RP PRO-96, 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 [9]
RP PROTEIN SEQUENCE OF 86-100, PTM, FUNCTION, HYDROXYLATION AT PRO-89; PRO-92
RP AND PRO-96, INTERACTION WITH CEPR1, AND INDUCTION BY NITROGEN DEPLETION.
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).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 88-ARG--GLY-99, REPRESSION
RP BY AUXIN, TISSUE SPECIFICITY, AND HYDROXYLATION AT PRO-89; PRO-92 AND
RP PRO-96.
RX PubMed=27296247; DOI=10.1093/jxb/erw231;
RA Roberts I., Smith S., Stes E., De Rybel B., Staes A., van de Cotte B.,
RA Njo M.F., Dedeyne L., Demol H., Lavenus J., Audenaert D., Gevaert K.,
RA Beeckman T., De Smet I.;
RT "CEP5 and XIP1/CEPR1 regulate lateral root initiation in Arabidopsis.";
RL J. Exp. Bot. 67:4889-4899(2016).
CC -!- FUNCTION: Extracellular signaling peptide that represses plant growth
CC rate. Regulates shoot gravitropic responses (PubMed:24179095).
CC Represses primary root length and lateral root initiation, probably by
CC repressing the CEP receptor CEPR1 (PubMed:24179096, PubMed:27296247).
CC Regulates systemic nitrogen (N)-demand signaling. Mediates up-
CC regulation of genes involved in N uptake and assimilation pathways
CC (PubMed:25324386). {ECO:0000269|PubMed:24179095,
CC ECO:0000269|PubMed:24179096, ECO:0000269|PubMed:25324386,
CC ECO:0000269|PubMed:27296247}.
CC -!- SUBUNIT: Interacts with the CEP receptor CEPR1.
CC {ECO:0000269|PubMed:25324386}.
CC -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 5]: Secreted,
CC extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}.
CC Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, and, at lower levels, in
CC stems, leaves and flowers (PubMed:18315543, PubMed:24179095). Present
CC in lateral root primordia (especially in vasculature and in the basal
CC meristem) (PubMed:24179095, PubMed:27296247). Predominantly expressed
CC in the phloem pole-associated pericycle (PPP) cells, and, to a lower
CC extent, in the adjacent phloem (PubMed:27296247). Observed in lateral
CC roots (especially in vasculature), root-hypocotyl junction, leaves,
CC inflorescence stems and flowers (PubMed:24179095).
CC {ECO:0000269|PubMed:18315543, ECO:0000269|PubMed:24179095,
CC ECO:0000269|PubMed:27296247}.
CC -!- INDUCTION: Induced by gibberellic acid (GA) and phosphorus (P), but
CC repressed by brassinosteroids (BR), salicylic acid (SA) and nitrogen
CC (N) (PubMed:24179095). Repressed by auxin (e.g. IAA and NAA)
CC (PubMed:24179095, PubMed:27296247). Accumulates in roots in response to
CC nitrate, nitrogen and ammonium chloride NH(4)Cl depletion
CC (PubMed:24179096, PubMed:25324386). Induced in shoots by osmotic stress
CC (e.g. mannitol) (PubMed:24179096). {ECO:0000269|PubMed:24179095,
CC ECO:0000269|PubMed:24179096, ECO:0000269|PubMed:25324386,
CC ECO:0000269|PubMed:27296247}.
CC -!- PTM: The mature small signaling peptide is generated by proteolytic
CC processing of the longer precursor. {ECO:0000269|PubMed:25324386}.
CC -!- PTM: Hydroxylated peptide is more active than non-hydroxylated peptide.
CC {ECO:0000269|PubMed:27296247}.
CC -!- DISRUPTION PHENOTYPE: Increased plant height with abnormal shoot
CC gravitropic responses (PubMed:24179095). Longer primary root length and
CC increased number of lateral roots initiation and primordia
CC (PubMed:27296247). {ECO:0000269|PubMed:24179095,
CC ECO:0000269|PubMed:27296247}.
CC -!- SIMILARITY: Belongs to the C-terminally encoded plant signaling peptide
CC (CEP) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM62571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB010700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED98266.1; -; Genomic_DNA.
DR EMBL; BT029249; ABJ98581.1; -; mRNA.
DR EMBL; AY085340; AAM62571.1; ALT_INIT; mRNA.
DR RefSeq; NP_569039.1; NM_126080.2.
DR AlphaFoldDB; Q058G9; -.
DR STRING; 3702.AT5G66815.1; -.
DR PaxDb; Q058G9; -.
DR PRIDE; Q058G9; -.
DR EnsemblPlants; AT5G66815.1; AT5G66815.1; AT5G66815.
DR GeneID; 836815; -.
DR Gramene; AT5G66815.1; AT5G66815.1; AT5G66815.
DR KEGG; ath:AT5G66815; -.
DR Araport; AT5G66815; -.
DR TAIR; locus:505006719; AT5G66815.
DR eggNOG; ENOG502SCM9; Eukaryota.
DR HOGENOM; CLU_175062_0_0_1; -.
DR InParanoid; Q058G9; -.
DR OMA; FFLGFNC; -.
DR OrthoDB; 1590642at2759; -.
DR PhylomeDB; Q058G9; -.
DR PRO; PR:Q058G9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q058G9; baseline and differential.
DR GO; GO:0048046; C:apoplast; ISS: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; IEP:UniProtKB.
DR GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
DR GO; GO:1905614; P:negative regulation of developmental vegetative growth; IMP:UniProtKB.
DR GO; GO:1902025; P:nitrate import; IDA:UniProtKB.
DR GO; GO:0080022; P:primary root development; IMP:UniProtKB.
DR GO; GO:1901371; P:regulation of leaf morphogenesis; IBA:GO_Central.
DR GO; GO:2000280; P:regulation of root development; IDA:UniProtKB.
DR GO; GO:0060359; P:response to ammonium ion; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IDA:TAIR.
DR GO; GO:0009741; P:response to brassinosteroid; IEP:UniProtKB.
DR GO; GO:0009739; P:response to gibberellin; IEP: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:0009751; P:response to salicylic acid; IEP: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..30
FT /evidence="ECO:0000255"
FT PROPEP 31..85
FT /evidence="ECO:0000305"
FT /id="PRO_0000439974"
FT PEPTIDE 86..100
FT /note="C-terminally encoded peptide 5"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439975"
FT PROPEP 101..105
FT /evidence="ECO:0000305"
FT /id="PRO_0000439976"
FT REGION 61..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:24179096,
FT ECO:0000269|PubMed:25324386, ECO:0000269|PubMed:27296247"
FT MOD_RES 92
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386,
FT ECO:0000269|PubMed:27296247"
FT MOD_RES 96
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:24179096,
FT ECO:0000269|PubMed:25324386, ECO:0000269|PubMed:27296247"
FT MUTAGEN 88..99
FT /note="RPTTPGHSPGIG->LPHTPGHVPGIS: Impaired repression of
FT root growth and lateral root initiation."
FT /evidence="ECO:0000269|PubMed:27296247"
FT CONFLICT 69
FT /note="Missing (in Ref. 4; AAM62571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 105 AA; 11585 MW; 835C5E3A78B90FC9 CRC64;
MESFMGQKKT LYACYFLMLV FFLGFNCVHG RTLKVDDKIN GGHYDSKTMM ALAKHNDMMV
DDKAMQFSPP PPPPPPSQSG GKDAEDFRPT TPGHSPGIGH SLSHN
