PCEP2_ARATH
ID PCEP2_ARATH Reviewed; 126 AA.
AC Q3ECM0; A0MED5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Precursor of CEP2 {ECO:0000303|PubMed:24179096};
DE Short=PCEP2 {ECO:0000303|PubMed:24179096};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 2.1 {ECO:0000303|PubMed:24179096};
DE Short=CEP2.1 {ECO:0000303|PubMed:24179096};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 2.2 {ECO:0000303|PubMed:24179096};
DE Short=CEP2.2 {ECO:0000303|PubMed:24179096};
DE Flags: Precursor;
GN Name=CEP2 {ECO:0000303|PubMed:24179096};
GN OrderedLocusNames=At1g59835 {ECO:0000312|Araport:AT1G59835};
GN ORFNames=F23H11 {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=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 [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].
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 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 [5]
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 [6]
RP TISSUE SPECIFICITY, 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 [7]
RP FUNCTION, INDUCTION BY OSMOTIC STRESS; AMMONIUM CHLORIDE STARVATION;
RP NITROGEN DEPLETION AND NITRATE DEPLETION, 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 [8]
RP FUNCTION.
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. Regulates negatively leaves number and flowering, and
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 2.1]: Secreted,
CC extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}.
CC Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
CC -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 2.2]: 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 (PubMed:18315543).
CC Present in cotyledons, shoot apical meristem (SAM), leaves,
CC inflorescence stems and flowers (PubMed:24179095).
CC {ECO:0000269|PubMed:18315543, ECO:0000269|PubMed:24179095}.
CC -!- INDUCTION: Accumulates in shoots in response to nitrate depletion and
CC to osmotic stress (e.g. mannitol), but repressed by ammonium chloride
CC NH(4)Cl and nitrogen starvation. {ECO:0000269|PubMed:24179096}.
CC -!- PTM: The mature small signaling peptide is generated by proteolytic
CC processing of the longer precursor. {ECO:0000250|UniProtKB:Q8L8Y3}.
CC -!- SIMILARITY: Belongs to the C-terminally encoded plant signaling peptide
CC (CEP) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28151.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE33625.1; -; Genomic_DNA.
DR EMBL; DQ446377; ABE65412.1; -; Genomic_DNA.
DR EMBL; DQ652905; ABK28151.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_683452.1; NM_148611.2.
DR AlphaFoldDB; Q3ECM0; -.
DR STRING; 3702.AT1G59835.1; -.
DR PaxDb; Q3ECM0; -.
DR PRIDE; Q3ECM0; -.
DR EnsemblPlants; AT1G59835.1; AT1G59835.1; AT1G59835.
DR GeneID; 842277; -.
DR Gramene; AT1G59835.1; AT1G59835.1; AT1G59835.
DR KEGG; ath:AT1G59835; -.
DR Araport; AT1G59835; -.
DR TAIR; locus:504956267; AT1G59835.
DR HOGENOM; CLU_1984620_0_0_1; -.
DR OMA; HEHFNEY; -.
DR OrthoDB; 1414667at2759; -.
DR PhylomeDB; Q3ECM0; -.
DR PRO; PR:Q3ECM0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q3ECM0; baseline.
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; ISS: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:1901371; P:regulation of leaf morphogenesis; IMP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0048831; P:regulation of shoot system development; IMP:UniProtKB.
DR GO; GO:0060359; P:response to ammonium ion; IEP:UniProtKB.
DR GO; GO:0090548; P:response to nitrate starvation; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0048364; P:root development; IEA:InterPro.
DR InterPro; IPR033250; CEP.
DR PANTHER; PTHR33348; PTHR33348; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Developmental protein; Hormone; Hydroxylation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..80
FT /evidence="ECO:0000305"
FT /id="PRO_0000439963"
FT PEPTIDE 81..95
FT /note="C-terminally encoded peptide 2.2"
FT /evidence="ECO:0000250|UniProtKB:Q058G9"
FT /id="PRO_0000439964"
FT PROPEP 96..105
FT /evidence="ECO:0000305"
FT /id="PRO_0000439965"
FT PEPTIDE 106..120
FT /note="C-terminally encoded peptide 2.1"
FT /evidence="ECO:0000250|UniProtKB:Q058G9"
FT /id="PRO_0000439966"
FT PROPEP 121..126
FT /evidence="ECO:0000305"
FT /id="PRO_0000439967"
FT MOD_RES 84
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:Q8L8Y3"
FT MOD_RES 87
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:Q058G9"
FT MOD_RES 109
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:Q8L8Y3"
FT MOD_RES 112
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:Q058G9"
FT MOD_RES 116
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:Q8L8Y3"
SQ SEQUENCE 126 AA; 14118 MW; CFB80CEACF272AFC CRC64;
MKLFIITVVT ILTISRVFDK TPATTEARKS KKMVGHEHFN EYLDPTFAGH TFGVVKEDFL
EVKKLKKIGD ENNLKNRFIN EFAPTNPEDS LGIGHPRVLN NKFTNDFAPT NPGDSPGIRH
PGVVNV
