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Precursor of CEP5 (PCEP5) [Cleaved into: C-terminally encoded peptide 5 (CEP5)]

 PCEP5_ARATH             Reviewed;         105 AA.
Q058G9; Q8LEN0;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
14-NOV-2006, sequence version 1.
31-JAN-2018, entry version 73.
RecName: Full=Precursor of CEP5 {ECO:0000303|PubMed:24179096};
Short=PCEP5 {ECO:0000303|PubMed:24179096};
Contains:
RecName: Full=C-terminally encoded peptide 5 {ECO:0000303|PubMed:24179096};
Short=CEP5 {ECO:0000303|PubMed:24179096};
Flags: Precursor;
Name=CEP5 {ECO:0000303|PubMed:24179096};
OrderedLocusNames=At5g66815 {ECO:0000312|Araport:AT5G66815};
ORFNames=MUD21 {ECO:0000305};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF Clones.";
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
TISSUE SPECIFICITY.
PubMed=18315543; DOI=10.1111/j.1365-313X.2008.03464.x;
Ohyama K., Ogawa M., Matsubayashi Y.;
"Identification of a biologically active, small, secreted peptide in
Arabidopsis by in silico gene screening, followed by LC-MS-based
structure analysis.";
Plant J. 55:152-160(2008).
[6]
REVIEW.
PubMed=22303274; DOI=10.1199/tab.0150;
Matsubayashi Y.;
"Small post-translationally modified Peptide signals in Arabidopsis.";
Arabidopsis Book 9:E0150-E0150(2011).
[7]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY
GIBBERELLIC ACID; PHOSPHORUS; BRASSINOSTEROIDS; AUXIN; SALICYLIC ACID
AND NITROGEN, AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=24179095; DOI=10.1093/jxb/ert331;
Roberts I., Smith S., De Rybel B., Van Den Broeke J., Smet W.,
De Cokere S., Mispelaere M., De Smet I., Beeckman T.;
"The CEP family in land plants: evolutionary analyses, expression
studies, and role in Arabidopsis shoot development.";
J. Exp. Bot. 64:5371-5381(2013).
[8]
FUNCTION, INDUCTION BY OSMOTIC STRESS; AMMONIUM CHLORIDE STARVATION;
NITROGEN DEPLETION AND NITRATE DEPLETION, HYDROXYLATION AT PRO-89 AND
PRO-96, GENE FAMILY, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=24179096; DOI=10.1093/jxb/ert332;
Delay C., Imin N., Djordjevic M.A.;
"CEP genes regulate root and shoot development in response to
environmental cues and are specific to seed plants.";
J. Exp. Bot. 64:5383-5394(2013).
[9]
PROTEIN SEQUENCE OF 86-100, PTM, FUNCTION, HYDROXYLATION AT PRO-89;
PRO-92 AND PRO-96, INTERACTION WITH CEPR1, AND INDUCTION BY NITROGEN
DEPLETION.
STRAIN=cv. No-0;
PubMed=25324386; DOI=10.1126/science.1257800;
Tabata R., Sumida K., Yoshii T., Ohyama K., Shinohara H.,
Matsubayashi Y.;
"Perception of root-derived peptides by shoot LRR-RKs mediates
systemic N-demand signaling.";
Science 346:343-346(2014).
[10]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 88-ARG--GLY-99,
REPRESSION BY AUXIN, TISSUE SPECIFICITY, AND HYDROXYLATION AT PRO-89;
PRO-92 AND PRO-96.
PubMed=27296247; DOI=10.1093/jxb/erw231;
Roberts I., Smith S., Stes E., De Rybel B., Staes A., van de Cotte B.,
Njo M.F., Dedeyne L., Demol H., Lavenus J., Audenaert D., Gevaert K.,
Beeckman T., De Smet I.;
"CEP5 and XIP1/CEPR1 regulate lateral root initiation in
Arabidopsis.";
J. Exp. Bot. 67:4889-4899(2016).
-!- FUNCTION: Extracellular signaling peptide that represses plant
growth rate. Regulates shoot gravitropic responses
(PubMed:24179095). Represses primary root length and lateral root
initiation, probably by repressing the CEP receptor CEPR1
(PubMed:24179096, PubMed:27296247). Regulates systemic nitrogen
(N)-demand signaling. Mediates up-regulation of genes involved in
N uptake and assimilation pathways (PubMed:25324386).
{ECO:0000269|PubMed:24179095, ECO:0000269|PubMed:24179096,
ECO:0000269|PubMed:25324386, ECO:0000269|PubMed:27296247}.
-!- SUBUNIT: Interacts with the CEP receptor CEPR1.
{ECO:0000269|PubMed:25324386}.
-!- SUBCELLULAR LOCATION: C-terminally encoded peptide 5: Secreted,
extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}.
Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
-!- TISSUE SPECIFICITY: Mostly expressed in roots, and, at lower
levels, in stems, leaves and flowers (PubMed:18315543,
PubMed:24179095). Present in lateral root primordia (especially in
vasculature and in the basal meristem) (PubMed:24179095,
PubMed:27296247). Predominantly expressed in the phloem pole-
associated pericycle (PPP) cells, and, to a lower extent, in the
adjacent phloem (PubMed:27296247). Observed in lateral roots
(especially in vasculature), root-hypocotyl junction, leaves,
inflorescence stems and flowers (PubMed:24179095).
{ECO:0000269|PubMed:18315543, ECO:0000269|PubMed:24179095,
ECO:0000269|PubMed:27296247}.
-!- INDUCTION: Induced by gibberellic acid (GA) and phosphorus (P),
but repressed by brassinosteroids (BR), salicylic acid (SA) and
nitrogen (N) (PubMed:24179095). Repressed by auxin (e.g. IAA and
NAA) (PubMed:24179095, PubMed:27296247). Accumulates in roots in
response to nitrate, nitrogen and ammonium chloride NH(4)Cl
depletion (PubMed:24179096, PubMed:25324386). Induced in shoots by
osmotic stress (e.g. mannitol) (PubMed:24179096).
{ECO:0000269|PubMed:24179095, ECO:0000269|PubMed:24179096,
ECO:0000269|PubMed:25324386, ECO:0000269|PubMed:27296247}.
-!- PTM: The mature small signaling peptide is generated by
proteolytic processing of the longer precursor.
{ECO:0000269|PubMed:25324386}.
-!- PTM: Hydroxylated peptide is more active than non-hydroxylated
peptide. {ECO:0000269|PubMed:27296247}.
-!- DISRUPTION PHENOTYPE: Increased plant height with abnormal shoot
gravitropic responses (PubMed:24179095). Longer primary root
length and increased number of lateral roots initiation and
primordia (PubMed:27296247). {ECO:0000269|PubMed:24179095,
ECO:0000269|PubMed:27296247}.
-!- SIMILARITY: Belongs to the C-terminally encoded plant signaling
peptide (CEP) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM62571.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB010700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED98266.1; -; Genomic_DNA.
EMBL; BT029249; ABJ98581.1; -; mRNA.
EMBL; AY085340; AAM62571.1; ALT_INIT; mRNA.
RefSeq; NP_569039.1; NM_126080.2.
UniGene; At.28847; -.
STRING; 3702.AT5G66815.1; -.
PaxDb; Q058G9; -.
EnsemblPlants; AT5G66815.1; AT5G66815.1; AT5G66815.
GeneID; 836815; -.
Gramene; AT5G66815.1; AT5G66815.1; AT5G66815.
KEGG; ath:AT5G66815; -.
Araport; AT5G66815; -.
TAIR; locus:505006719; AT5G66815.
eggNOG; ENOG410JSCU; Eukaryota.
eggNOG; ENOG41108XF; LUCA.
HOGENOM; HOG000090622; -.
OMA; IFSHIIQ; -.
OrthoDB; EOG09360WS8; -.
PRO; PR:Q058G9; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q058G9; baseline and differential.
GO; GO:0048046; C:apoplast; ISS:UniProtKB.
GO; GO:0005179; F:hormone activity; IDA:UniProtKB.
GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:UniProtKB.
GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
GO; GO:1905614; P:negative regulation of developmental vegetative growth; IMP:UniProtKB.
GO; GO:1902025; P:nitrate import; IDA:UniProtKB.
GO; GO:0080022; P:primary root development; IMP:UniProtKB.
GO; GO:2000280; P:regulation of root development; IDA:UniProtKB.
GO; GO:0060359; P:response to ammonium ion; IEP:UniProtKB.
GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
GO; GO:0009741; P:response to brassinosteroid; IEP:UniProtKB.
GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
GO; GO:0090548; P:response to nitrate starvation; IEP:UniProtKB.
GO; GO:1901698; P:response to nitrogen compound; IEP:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
InterPro; IPR033250; CEP.
PANTHER; PTHR33348; PTHR33348; 1.
1: Evidence at protein level;
Apoplast; Complete proteome; Developmental protein;
Direct protein sequencing; Hormone; Hydroxylation; Reference proteome;
Secreted; Signal.
SIGNAL 1 30 {ECO:0000255}.
PROPEP 31 85 {ECO:0000305}.
/FTId=PRO_0000439974.
PEPTIDE 86 100 C-terminally encoded peptide 5.
{ECO:0000269|PubMed:25324386}.
/FTId=PRO_0000439975.
PROPEP 101 105 {ECO:0000305}.
/FTId=PRO_0000439976.
COMPBIAS 69 76 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
MOD_RES 89 89 Hydroxyproline.
{ECO:0000269|PubMed:24179096,
ECO:0000269|PubMed:25324386,
ECO:0000269|PubMed:27296247}.
MOD_RES 92 92 Hydroxyproline.
{ECO:0000269|PubMed:25324386,
ECO:0000269|PubMed:27296247}.
MOD_RES 96 96 Hydroxyproline.
{ECO:0000269|PubMed:24179096,
ECO:0000269|PubMed:25324386,
ECO:0000269|PubMed:27296247}.
MUTAGEN 88 99 RPTTPGHSPGIG->LPHTPGHVPGIS: Impaired
repression of root growth and lateral
root initiation.
{ECO:0000269|PubMed:27296247}.
CONFLICT 69 69 Missing (in Ref. 4; AAM62571).
{ECO:0000305}.
SEQUENCE 105 AA; 11585 MW; 835C5E3A78B90FC9 CRC64;
MESFMGQKKT LYACYFLMLV FFLGFNCVHG RTLKVDDKIN GGHYDSKTMM ALAKHNDMMV
DDKAMQFSPP PPPPPPSQSG GKDAEDFRPT TPGHSPGIGH SLSHN


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