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Precursor of CEP9 (PCEP9) [Cleaved into: C-terminally encoded peptide 9.1 (CEP9.1) (CEP9a); C-terminally encoded peptide 9.2 (CEP9.2) (CEP9b); C-terminally encoded peptide 9.3 (CEP9.3) (CEP9c); C-terminally encoded peptide 9.4 (CEP9.4) (CEP9d); C-terminally encoded peptide 9.5 (CEP9.5) (CEP9e)]

 PCEP9_ARATH             Reviewed;         243 AA.
A0A1I9LMX5; A0MF19; Q9SCR4;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
15-FEB-2017, sequence version 1.
23-MAY-2018, entry version 13.
RecName: Full=Precursor of CEP9 {ECO:0000303|PubMed:24179096};
Short=PCEP9 {ECO:0000303|PubMed:24179096};
Contains:
RecName: Full=C-terminally encoded peptide 9.1 {ECO:0000303|PubMed:24179096};
Short=CEP9.1 {ECO:0000303|PubMed:24179096};
Short=CEP9a {ECO:0000303|PubMed:25324386};
Contains:
RecName: Full=C-terminally encoded peptide 9.2 {ECO:0000303|PubMed:24179096};
Short=CEP9.2 {ECO:0000303|PubMed:24179096};
Short=CEP9b {ECO:0000303|PubMed:25324386};
Contains:
RecName: Full=C-terminally encoded peptide 9.3 {ECO:0000303|PubMed:24179096};
Short=CEP9.3 {ECO:0000303|PubMed:24179096};
Short=CEP9c {ECO:0000303|PubMed:25324386};
Contains:
RecName: Full=C-terminally encoded peptide 9.4 {ECO:0000303|PubMed:24179096};
Short=CEP9.4 {ECO:0000303|PubMed:24179096};
Short=CEP9d {ECO:0000303|PubMed:25324386};
Contains:
RecName: Full=C-terminally encoded peptide 9.5 {ECO:0000303|PubMed:24179096};
Short=CEP9.5 {ECO:0000303|PubMed:24179096};
Short=CEP9e {ECO:0000303|PubMed:25324386};
Flags: Precursor;
Name=CEP9 {ECO:0000303|PubMed:24179096};
OrderedLocusNames=At3g50610 {ECO:0000312|Araport:AT3G50610};
ORFNames=T20E23.210 {ECO:0000312|EMBL:CAB62490.1};
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=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 15-243.
STRAIN=cv. Columbia;
PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
"Simultaneous high-throughput recombinational cloning of open reading
frames in closed and open configurations.";
Plant Biotechnol. J. 4:317-324(2006).
[4]
INDUCTION BY NITROGEN; POTASSIUM AND AUXIN, 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).
[5]
FUNCTION, INDUCTION BY AMMONIUM CHLORIDE AND OSMOTIC STRESS,
HYDROXYLATION AT PRO-48 AND PRO-55, PTM, 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).
[6]
PROTEIN SEQUENCE OF 45-59; 97-111; 149-163; 201-215 AND 220-234, PTM,
FUNCTION, HYDROXYLATION AT PRO-48; PRO-51; PRO-55; PRO-100; PRO-103;
PRO-107; PRO-152; PRO-155; PRO-159; PRO-204; PRO-207; PRO-211; PRO-226
AND PRO-230, TISSUE SPECIFICITY, INDUCTION BY NITROGEN DEPLETION, AND
SUBCELLULAR LOCATION.
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).
-!- FUNCTION: Extracellular signaling peptide that represses primary
root growth rate and significantly inhibits lateral root
formation. Modulates leaf morphology (PubMed:24179096). Regulates
systemic nitrogen (N)-demand signaling. Mediates up-regulation of
genes involved in N uptake and assimilation pathways
(PubMed:25324386). {ECO:0000269|PubMed:24179096,
ECO:0000269|PubMed:25324386}.
-!- SUBUNIT: Interacts with CEP receptors (e.g. CEPR1 and CEPR2).
{ECO:0000250|UniProtKB:Q8L8Y3}.
-!- SUBCELLULAR LOCATION: C-terminally encoded peptide 9.2: Secreted,
extracellular space, apoplast {ECO:0000269|PubMed:25324386}.
Note=Accumulates in xylem sap under nitrogen (N)-starved
conditions. {ECO:0000269|PubMed:25324386}.
-!- SUBCELLULAR LOCATION: C-terminally encoded peptide 9.3: Secreted,
extracellular space, apoplast {ECO:0000269|PubMed:25324386}.
Note=Accumulates in xylem sap under nitrogen (N)-starved
conditions. {ECO:0000269|PubMed:25324386}.
-!- SUBCELLULAR LOCATION: C-terminally encoded peptide 9.4: Secreted,
extracellular space, apoplast {ECO:0000269|PubMed:25324386}.
Note=Accumulates in xylem sap under nitrogen (N)-starved
conditions. {ECO:0000269|PubMed:25324386}.
-!- SUBCELLULAR LOCATION: C-terminally encoded peptide 9.5: Secreted,
extracellular space, apoplast {ECO:0000269|PubMed:25324386}.
Note=Accumulates in xylem sap under nitrogen (N)-starved
conditions. {ECO:0000269|PubMed:25324386}.
-!- SUBCELLULAR LOCATION: C-terminally encoded peptide 9.1: Secreted,
extracellular space, apoplast {ECO:0000305|PubMed:25324386}.
Note=Accumulates in xylem sap. {ECO:0000305|PubMed:25324386}.
-!- TISSUE SPECIFICITY: Expressed in lateral root primordia and in
lateral roots excluding the meristem region. Also present in the
aerial tissues, such as leaf petioles and the shoot apex region.
{ECO:0000269|PubMed:25324386}.
-!- INDUCTION: Induced by nitrogen (N) and potassium (K), but
repressed by auxin (PubMed:24179095). Repressed in shoots in
response to ammonium chloride NH(4)Cl and osmotic stress (e.g.
mannitol) (PubMed:24179096). Triggered by nitrogen depletion
(PubMed:25324386). {ECO:0000269|PubMed:24179095,
ECO:0000269|PubMed:24179096, ECO:0000269|PubMed:25324386}.
-!- PTM: Hydroxylated peptide is more active than non-hydroxylated
peptide. {ECO:0000269|PubMed:24179096}.
-!- PTM: The mature small signaling peptide is generated by
proteolytic processing of the longer precursor.
{ECO:0000269|PubMed:25324386}.
-!- SIMILARITY: Belongs to the C-terminally encoded plant signaling
peptide (CEP) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABK28235.1; Type=Erroneous termination; Positions=244; Note=Translated as stop.; Evidence={ECO:0000305};
Sequence=AEE78685.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB62490.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; CP002686; AEE78685.1; ALT_INIT; Genomic_DNA.
EMBL; AL133363; CAB62490.1; ALT_INIT; Genomic_DNA.
EMBL; CP002686; ANM63933.1; -; Genomic_DNA.
EMBL; DQ446754; ABE65503.1; -; Genomic_DNA.
EMBL; DQ653143; ABK28235.1; ALT_SEQ; Genomic_DNA.
PIR; T46092; T46092.
RefSeq; NP_001325993.1; NM_001339475.1.
RefSeq; NP_190630.1; NM_114921.1.
UniGene; At.65271; -.
EnsemblPlants; AT3G50610.2; AT3G50610.2; AT3G50610.
GeneID; 824224; -.
Gramene; AT3G50610.2; AT3G50610.2; AT3G50610.
KEGG; ath:AT3G50610; -.
Araport; AT3G50610; -.
TAIR; locus:2098695; AT3G50610.
eggNOG; ENOG410J4EW; Eukaryota.
eggNOG; ENOG410ZPHN; LUCA.
HOGENOM; HOG000202491; -.
OrthoDB; EOG09360M1V; -.
PRO; PR:A0A1I9LMX5; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; A0A1I9LMX5; differential.
GO; GO:0048046; C:apoplast; IDA:UniProtKB.
GO; GO:0005179; F:hormone activity; IDA:UniProtKB.
GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:UniProtKB.
GO; GO:1902025; P:nitrate import; IDA:UniProtKB.
GO; GO:2000023; P:regulation of lateral root development; IDA:UniProtKB.
GO; GO:1901371; P:regulation of leaf morphogenesis; 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:1901698; P:response to nitrogen compound; IEP:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
GO; GO:0035864; P:response to potassium ion; IEP:UniProtKB.
GO; GO:0048364; P:root development; IEA:InterPro.
InterPro; IPR033250; CEP.
PANTHER; PTHR33348; PTHR33348; 4.
1: Evidence at protein level;
Apoplast; Complete proteome; Developmental protein;
Direct protein sequencing; Hormone; Hydroxylation; Reference proteome;
Secreted; Signal.
SIGNAL 1 26 {ECO:0000255}.
PROPEP 28 44 {ECO:0000305|PubMed:25324386}.
/FTId=PRO_0000439986.
PEPTIDE 45 59 C-terminally encoded peptide 9.1.
{ECO:0000269|PubMed:25324386}.
/FTId=PRO_0000439987.
PROPEP 60 96 {ECO:0000305|PubMed:25324386}.
/FTId=PRO_0000439988.
PEPTIDE 97 111 C-terminally encoded peptide 9.2.
{ECO:0000269|PubMed:25324386}.
/FTId=PRO_0000439989.
PROPEP 112 148 {ECO:0000305|PubMed:25324386}.
/FTId=PRO_0000439990.
PEPTIDE 149 163 C-terminally encoded peptide 9.3.
{ECO:0000269|PubMed:25324386}.
/FTId=PRO_0000439991.
PROPEP 164 200 {ECO:0000305|PubMed:25324386}.
/FTId=PRO_0000439992.
PEPTIDE 201 215 C-terminally encoded peptide 9.4.
{ECO:0000269|PubMed:25324386}.
/FTId=PRO_0000439993.
PROPEP 216 219 {ECO:0000305|PubMed:25324386}.
/FTId=PRO_0000439994.
PEPTIDE 220 234 C-terminally encoded peptide 9.5.
{ECO:0000269|PubMed:25324386}.
/FTId=PRO_0000439995.
PROPEP 235 243 {ECO:0000305|PubMed:25324386}.
/FTId=PRO_0000439996.
MOD_RES 48 48 Hydroxyproline; partial.
{ECO:0000269|PubMed:24179096,
ECO:0000269|PubMed:25324386}.
MOD_RES 51 51 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 55 55 Hydroxyproline; partial.
{ECO:0000269|PubMed:24179096,
ECO:0000269|PubMed:25324386}.
MOD_RES 100 100 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 103 103 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 107 107 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 152 152 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 155 155 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 159 159 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 204 204 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 207 207 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 211 211 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 223 223 Hydroxyproline.
{ECO:0000250|UniProtKB:Q8L8Y3}.
MOD_RES 226 226 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
MOD_RES 230 230 Hydroxyproline.
{ECO:0000269|PubMed:25324386}.
SEQUENCE 243 AA; 26206 MW; 012DEE9D92D9109C CRC64;
MKLLSITLTS IVISMVFYQT PITTEARSLR KTNDQDHFKA GFTDDFVPTS PGNSPGVGHK
KGNVNVEGFQ DDFKPTEGRK LLKTNVQDHF KTGSTDDFAP TSPGHSPGVG HKKGNVNVES
SEDDFKHKEG RKLQQTNGQN HFKTGSTDDF APTSPGNSPG IGHKKGHANV KGFKDDFAPT
EEIRLQKMNG QDHFKTGSTD DFAPTTPGNS PGMGHKKGDD FKPTTPGHSP GVGHAVKNDE
PKA


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