PCEP9_ARATH
ID PCEP9_ARATH Reviewed; 243 AA.
AC A0A1I9LMX5; A0MF19; Q9SCR4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Precursor of CEP9 {ECO:0000303|PubMed:24179096};
DE Short=PCEP9 {ECO:0000303|PubMed:24179096};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 9.1 {ECO:0000303|PubMed:24179096};
DE Short=CEP9.1 {ECO:0000303|PubMed:24179096};
DE Short=CEP9a {ECO:0000303|PubMed:25324386};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 9.2 {ECO:0000303|PubMed:24179096};
DE Short=CEP9.2 {ECO:0000303|PubMed:24179096};
DE Short=CEP9b {ECO:0000303|PubMed:25324386};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 9.3 {ECO:0000303|PubMed:24179096};
DE Short=CEP9.3 {ECO:0000303|PubMed:24179096};
DE Short=CEP9c {ECO:0000303|PubMed:25324386};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 9.4 {ECO:0000303|PubMed:24179096};
DE Short=CEP9.4 {ECO:0000303|PubMed:24179096};
DE Short=CEP9d {ECO:0000303|PubMed:25324386};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 9.5 {ECO:0000303|PubMed:24179096};
DE Short=CEP9.5 {ECO:0000303|PubMed:24179096};
DE Short=CEP9e {ECO:0000303|PubMed:25324386};
DE Flags: Precursor;
GN Name=CEP9 {ECO:0000303|PubMed:24179096};
GN OrderedLocusNames=At3g50610 {ECO:0000312|Araport:AT3G50610};
GN ORFNames=T20E23.210 {ECO:0000312|EMBL:CAB62490.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 GENOMIC DNA] OF 15-243.
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP INDUCTION BY NITROGEN; POTASSIUM AND AUXIN, 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 [5]
RP FUNCTION, INDUCTION BY AMMONIUM CHLORIDE AND OSMOTIC STRESS, HYDROXYLATION
RP AT PRO-48 AND PRO-55, PTM, 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 [6]
RP PROTEIN SEQUENCE OF 45-59; 97-111; 149-163; 201-215 AND 220-234, PTM,
RP FUNCTION, HYDROXYLATION AT PRO-48; PRO-51; PRO-55; PRO-100; PRO-103;
RP PRO-107; PRO-152; PRO-155; PRO-159; PRO-204; PRO-207; PRO-211; PRO-226 AND
RP PRO-230, TISSUE SPECIFICITY, 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.
CC Modulates leaf morphology (PubMed:24179096). Regulates systemic
CC nitrogen (N)-demand signaling. Mediates up-regulation of genes involved
CC in N uptake and assimilation pathways (PubMed:25324386).
CC {ECO:0000269|PubMed:24179096, ECO:0000269|PubMed:25324386}.
CC -!- SUBUNIT: Interacts with CEP receptors (e.g. CEPR1 and CEPR2).
CC {ECO:0000250|UniProtKB:Q8L8Y3}.
CC -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.2]: 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 -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.3]: 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 -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.4]: 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 -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.5]: 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 -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 9.1]: Secreted,
CC extracellular space, apoplast {ECO:0000305|PubMed:25324386}.
CC Note=Accumulates in xylem sap. {ECO:0000305|PubMed:25324386}.
CC -!- TISSUE SPECIFICITY: Expressed in lateral root primordia and in lateral
CC roots excluding the meristem region. Also present in the aerial
CC tissues, such as leaf petioles and the shoot apex region.
CC {ECO:0000269|PubMed:25324386}.
CC -!- INDUCTION: Induced by nitrogen (N) and potassium (K), but repressed by
CC auxin (PubMed:24179095). Repressed in shoots in response to ammonium
CC chloride NH(4)Cl and osmotic stress (e.g. mannitol) (PubMed:24179096).
CC Triggered by nitrogen depletion (PubMed:25324386).
CC {ECO:0000269|PubMed:24179095, ECO:0000269|PubMed:24179096,
CC ECO:0000269|PubMed:25324386}.
CC -!- PTM: Hydroxylated peptide is more active than non-hydroxylated peptide.
CC {ECO:0000269|PubMed:24179096}.
CC -!- PTM: The mature small signaling peptide is generated by proteolytic
CC processing of the longer precursor. {ECO:0000269|PubMed:25324386}.
CC -!- SIMILARITY: Belongs to the C-terminally encoded plant signaling peptide
CC (CEP) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28235.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=AEE78685.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB62490.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP002686; AEE78685.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL133363; CAB62490.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; ANM63933.1; -; Genomic_DNA.
DR EMBL; DQ446754; ABE65503.1; -; Genomic_DNA.
DR EMBL; DQ653143; ABK28235.1; ALT_SEQ; Genomic_DNA.
DR PIR; T46092; T46092.
DR RefSeq; NP_001325993.1; NM_001339475.1.
DR RefSeq; NP_190630.1; NM_114921.1.
DR AlphaFoldDB; A0A1I9LMX5; -.
DR STRING; 3702.AT3G50610.1; -.
DR EnsemblPlants; AT3G50610.2; AT3G50610.2; AT3G50610.
DR GeneID; 824224; -.
DR Gramene; AT3G50610.2; AT3G50610.2; AT3G50610.
DR KEGG; ath:AT3G50610; -.
DR Araport; AT3G50610; -.
DR TAIR; locus:2098695; AT3G50610.
DR eggNOG; ENOG502S6UF; Eukaryota.
DR OMA; TNGQDHF; -.
DR OrthoDB; 1414667at2759; -.
DR PRO; PR:A0A1I9LMX5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; A0A1I9LMX5; 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; IEP: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:0060359; P:response to ammonium ion; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; 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:0048364; P:root development; IEA:InterPro.
DR InterPro; IPR033250; CEP.
DR PANTHER; PTHR33348; PTHR33348; 2.
PE 1: Evidence at protein level;
KW Apoplast; Developmental protein; Direct protein sequencing; Hormone;
KW Hydroxylation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 28..44
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439986"
FT PEPTIDE 45..59
FT /note="C-terminally encoded peptide 9.1"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439987"
FT PROPEP 60..96
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439988"
FT PEPTIDE 97..111
FT /note="C-terminally encoded peptide 9.2"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439989"
FT PROPEP 112..148
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439990"
FT PEPTIDE 149..163
FT /note="C-terminally encoded peptide 9.3"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439991"
FT PROPEP 164..200
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439992"
FT PEPTIDE 201..215
FT /note="C-terminally encoded peptide 9.4"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439993"
FT PROPEP 216..219
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439994"
FT PEPTIDE 220..234
FT /note="C-terminally encoded peptide 9.5"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439995"
FT PROPEP 235..243
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439996"
FT REGION 42..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:24179096,
FT ECO:0000269|PubMed:25324386"
FT MOD_RES 51
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 55
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:24179096,
FT ECO:0000269|PubMed:25324386"
FT MOD_RES 100
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 103
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 107
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 152
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 155
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 159
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 204
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 207
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 211
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 223
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:Q8L8Y3"
FT MOD_RES 226
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 230
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
SQ 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
