PCEP6_ARATH
ID PCEP6_ARATH Reviewed; 101 AA.
AC B3H5A9;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Precursor of CEP6 {ECO:0000303|PubMed:24179096};
DE Short=PCEP6 {ECO:0000303|PubMed:24179096};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 6.1 {ECO:0000303|PubMed:24179096};
DE Short=CEP6.1 {ECO:0000303|PubMed:24179096};
DE Short=CEP6a {ECO:0000303|PubMed:25324386};
DE Contains:
DE RecName: Full=C-terminally encoded peptide 6.2 {ECO:0000303|PubMed:24179096};
DE Short=CEP6.2 {ECO:0000303|PubMed:24179096};
DE Short=CEP6b {ECO:0000303|PubMed:25324386};
DE Flags: Precursor;
GN Name=CEP6 {ECO:0000303|PubMed:24179096};
GN OrderedLocusNames=At5g66816 {ECO:0000312|Araport:AT5G66816};
GN ORFNames=MUD21 {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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 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 [4]
RP FUNCTION, 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 [5]
RP PROTEIN SEQUENCE OF 49-63 AND 78-92, PTM, FUNCTION, HYDROXYLATION AT
RP PRO-52; PRO-55; PRO-59; PRO-84 AND PRO-88, TISSUE SPECIFICITY, INDUCTION BY
RP NITROGEN 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 primary root
CC growth rate. Modulates leaf morphology (PubMed:24179096). Regulates
CC systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes
CC involved 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 6.2]: 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 6.1]: 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: Triggered by nitrogen depletion.
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:25324386}.
CC -!- SIMILARITY: Belongs to the C-terminally encoded plant signaling peptide
CC (CEP) family. {ECO:0000305}.
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DR EMBL; AB010700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED98267.1; -; Genomic_DNA.
DR RefSeq; NP_001119514.1; NM_001126042.2.
DR AlphaFoldDB; B3H5A9; -.
DR SMR; B3H5A9; -.
DR STRING; 3702.AT5G66816.1; -.
DR PaxDb; B3H5A9; -.
DR PRIDE; B3H5A9; -.
DR EnsemblPlants; AT5G66816.1; AT5G66816.1; AT5G66816.
DR GeneID; 6240245; -.
DR Gramene; AT5G66816.1; AT5G66816.1; AT5G66816.
DR KEGG; ath:AT5G66816; -.
DR Araport; AT5G66816; -.
DR TAIR; locus:4515103770; AT5G66816.
DR eggNOG; ENOG502S6UF; Eukaryota.
DR HOGENOM; CLU_2295563_0_0_1; -.
DR InParanoid; B3H5A9; -.
DR OMA; GHKMKEN; -.
DR OrthoDB; 1414667at2759; -.
DR PhylomeDB; B3H5A9; -.
DR PRO; PR:B3H5A9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B3H5A9; 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; 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:0048364; P:root development; IEA:InterPro.
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..26
FT /evidence="ECO:0000255"
FT PROPEP 27..48
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439977"
FT PEPTIDE 49..63
FT /note="C-terminally encoded peptide 6.1"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439978"
FT PROPEP 64..77
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439979"
FT PEPTIDE 78..92
FT /note="C-terminally encoded peptide 6.2"
FT /evidence="ECO:0000269|PubMed:25324386"
FT /id="PRO_0000439980"
FT PROPEP 93..101
FT /evidence="ECO:0000305|PubMed:25324386"
FT /id="PRO_0000439981"
FT REGION 29..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 55
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 59
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 81
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:Q8L8Y3"
FT MOD_RES 84
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
FT MOD_RES 88
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25324386"
SQ SEQUENCE 101 AA; 11222 MW; 4623F2E6710D9C26 CRC64;
MKLSVYIILS ILFISTVFYE IQFTEARQLR KTDDQDHDDH HFTVGYTDDF GPTSPGNSPG
IGHKMKENEE NAGGYKDDFE PTTPGHSPGV GHAVKNNEPN A
