PCEP1_ARATH
ID PCEP1_ARATH Reviewed; 91 AA.
AC Q8L8Y3; A0MEB7;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Precursor of CEP1 {ECO:0000303|PubMed:24179096};
DE Short=PCEP1 {ECO:0000303|PubMed:24179096};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 1 {ECO:0000303|PubMed:24179096};
DE Short=CEP1 {ECO:0000303|PubMed:24179096};
DE Flags: Precursor;
GN Name=CEP1 {ECO:0000303|PubMed:24179096};
GN OrderedLocusNames=At1g47485 {ECO:0000312|Araport:AT1G47485};
GN ORFNames=F16N3 {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 [MRNA], PROTEIN SEQUENCE OF 72-86, FUNCTION,
RP SUBCELLULAR LOCATION, PTM, HYDROXYLATION AT PRO-75 AND PRO-82, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
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 [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=14573523; DOI=10.1242/dev.00842;
RA Schmid M., Uhlenhaut N.H., Godard F., Demar M., Bressan R., Weigel D.,
RA Lohmann J.U.;
RT "Dissection of floral induction pathways using global expression
RT analysis.";
RL Development 130:6001-6012(2003).
RN [7]
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 [8]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY AUXIN AND NITROGEN,
RP 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 [9]
RP INDUCTION BY OSMOTIC STRESS; NITROGEN DEPLETION AND NITRATE DEPLETION, GENE
RP 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 [10]
RP FUNCTION, INTERACTION WITH CEPR1 AND CEPR2, INDUCTION BY NITROGEN
RP DEPLETION, AND 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, in a dose-
CC dependent manner, primary root growth rate and lateral root elongation
CC by inhibiting both cell division in meristems and cell growth in
CC elongation zones. Prevents also slightly growth of above-ground parts
CC (PubMed:18315543). Regulates systemic nitrogen (N)-demand signaling.
CC Mediates systemic up-regulation of genes involved in N uptake and
CC assimilation pathways (e.g. NRT1.1, NRT2.1 and NRT3.1)
CC (PubMed:25324386). {ECO:0000269|PubMed:18315543,
CC ECO:0000269|PubMed:25324386}.
CC -!- SUBUNIT: Interacts with the CEP receptors CEPR1 and CEPR2.
CC {ECO:0000269|PubMed:25324386}.
CC -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 1]: Secreted,
CC extracellular space, apoplast {ECO:0000269|PubMed:18315543}.
CC Note=Accumulates in xylem sap under nitrogen (N)-starved conditions.
CC {ECO:0000250|UniProtKB:O80460}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the lateral root primordia
CC (PubMed:18315543). Also present in the shoot apical meristem (SAM)
CC (PubMed:18315543, PubMed:24179095). Detected in the primary root apical
CC meristem, at the root-hypocotyl junction, roots, leaves (in the small
CC dentations at the leaf margin), siliques and flowers (PubMed:24179095).
CC {ECO:0000269|PubMed:18315543, ECO:0000269|PubMed:24179095}.
CC -!- DEVELOPMENTAL STAGE: In young seedlings, only observed in lateral root
CC primordia, first in the core region at stage VI, in which cells of
CC outer layer 2 undergo a periclinal division, creating a new internal
CC layer (PubMed:18315543, PubMed:24179095). Maximum levels are reached at
CC the emergence stage, and steeply decrease after elongation of lateral
CC roots, except for residual expression in the region of vascular
CC connection. In two weeks old seedlings, also present in the shoot
CC apical mersitem (SAM) (PubMed:18315543). Accumulates during flower
CC development and during lateral root development. In flowers, present in
CC the gynoecium (PubMed:24179095). Repressed upon floral induction
CC (PubMed:14573523). {ECO:0000269|PubMed:14573523,
CC ECO:0000269|PubMed:18315543, ECO:0000269|PubMed:24179095}.
CC -!- INDUCTION: Induced by auxin and nitrogen (N) (PubMed:24179095). Induced
CC in shoots in response to nitrogen and nitrate starvation
CC (PubMed:24179096, PubMed:25324386). Accumulates also under osmotic
CC stress (e.g. mannitol and NaCl) (PubMed:24179096).
CC {ECO:0000269|PubMed:24179095, ECO:0000269|PubMed:24179096,
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:18315543}.
CC -!- SIMILARITY: Belongs to the C-terminally encoded plant signaling peptide
CC (CEP) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28436.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB333778; BAG34615.1; -; mRNA.
DR EMBL; AC007519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE32172.1; -; Genomic_DNA.
DR EMBL; DQ446335; ABE65696.1; -; mRNA.
DR EMBL; DQ652886; ABK28436.1; ALT_SEQ; mRNA.
DR EMBL; AY088738; AAM67056.1; -; mRNA.
DR RefSeq; NP_564508.1; NM_103641.2.
DR AlphaFoldDB; Q8L8Y3; -.
DR SMR; Q8L8Y3; -.
DR PaxDb; Q8L8Y3; -.
DR PRIDE; Q8L8Y3; -.
DR EnsemblPlants; AT1G47485.1; AT1G47485.1; AT1G47485.
DR GeneID; 841156; -.
DR Gramene; AT1G47485.1; AT1G47485.1; AT1G47485.
DR KEGG; ath:AT1G47485; -.
DR Araport; AT1G47485; -.
DR TAIR; locus:505006171; AT1G47485.
DR HOGENOM; CLU_2430047_0_0_1; -.
DR InParanoid; Q8L8Y3; -.
DR OMA; IAHPTDF; -.
DR OrthoDB; 1568083at2759; -.
DR PhylomeDB; Q8L8Y3; -.
DR PRO; PR:Q8L8Y3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L8Y3; baseline and differential.
DR GO; GO:0048046; C:apoplast; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IC:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IDA:UniProtKB.
DR GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; IDA:UniProtKB.
DR GO; GO:0071242; P:cellular response to ammonium ion; IEP:UniProtKB.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:UniProtKB.
DR GO; GO:0048527; P:lateral root development; IEP:TAIR.
DR GO; GO:0051782; P:negative regulation of cell division; IMP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:1902025; P:nitrate import; IDA:UniProtKB.
DR GO; GO:0048573; P:photoperiodism, flowering; IEP:UniProtKB.
DR GO; GO:1901371; P:regulation of leaf morphogenesis; IBA:GO_Central.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; 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:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP: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..28
FT /evidence="ECO:0000255"
FT PROPEP 29..71
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439960"
FT PEPTIDE 72..86
FT /note="C-terminally encoded peptide 1"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439961"
FT PROPEP 87..91
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439962"
FT REGION 69..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:18315543"
FT MOD_RES 78
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:Q058G9"
FT MOD_RES 82
FT /note="Hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:18315543"
SQ SEQUENCE 91 AA; 10080 MW; 0F9B56B9AEA2B559 CRC64;
MGMSNRSVST SIFFLALVVL HGIQDTEERH LKTTSLEIEG IYKKTEAEHP SIVVTYTRRG
VLQKEVIAHP TDFRPTNPGN SPGVGHSNGR H
