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PCP15_ARATH
ID   PCP15_ARATH             Reviewed;         105 AA.
AC   O22882; Q8LEI2;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Precursor of CEP15 {ECO:0000303|PubMed:24179096};
DE            Short=PCEP15 {ECO:0000303|PubMed:24179096};
DE   Contains:
DE     RecName: Full=C-terminally encoded peptide 15 {ECO:0000303|PubMed:24179096};
DE              Short=CEP15 {ECO:0000303|PubMed:24179096};
DE   Flags: Precursor;
GN   Name=CEP15 {ECO:0000303|PubMed:24179096};
GN   OrderedLocusNames=At2g40530 {ECO:0000312|Araport:AT2G40530};
GN   ORFNames=T2P4.12 {ECO:0000312|EMBL:AAB87584.1};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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 MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   INDUCTION BY BRASSINOSTEROIDS; ABSCISIC ACID AND SALICYLIC ACID, AND GENE
RP   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   [6]
RP   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).
CC   -!- FUNCTION: Extracellular signaling peptide that may regulate primary
CC       root growth rate and systemic nitrogen (N)-demand signaling.
CC       {ECO:0000250|UniProtKB:Q8L8Y3}.
CC   -!- SUBUNIT: Interacts with CEP receptors (e.g. CEPR1 and CEPR2).
CC       {ECO:0000250|UniProtKB:Q8L8Y3}.
CC   -!- SUBCELLULAR LOCATION: [C-terminally encoded peptide 15]: Secreted,
CC       extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}.
CC       Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
CC   -!- INDUCTION: Induced by brassinosteroids (BR) but repressed by abscisic
CC       acid (ABA) and salicylic acid (SA). {ECO:0000269|PubMed:24179095}.
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=AAM62632.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC002336; AAB87584.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09844.1; -; Genomic_DNA.
DR   EMBL; BT024670; ABD57495.1; -; mRNA.
DR   EMBL; AY085405; AAM62632.1; ALT_INIT; mRNA.
DR   PIR; F84830; F84830.
DR   RefSeq; NP_565935.1; NM_129615.4.
DR   AlphaFoldDB; O22882; -.
DR   STRING; 3702.AT2G40530.1; -.
DR   PaxDb; O22882; -.
DR   PRIDE; O22882; -.
DR   EnsemblPlants; AT2G40530.1; AT2G40530.1; AT2G40530.
DR   GeneID; 818648; -.
DR   Gramene; AT2G40530.1; AT2G40530.1; AT2G40530.
DR   KEGG; ath:AT2G40530; -.
DR   Araport; AT2G40530; -.
DR   TAIR; locus:2061853; AT2G40530.
DR   eggNOG; ENOG502R1PC; Eukaryota.
DR   HOGENOM; CLU_2281408_0_0_1; -.
DR   InParanoid; O22882; -.
DR   OMA; ESEAFQG; -.
DR   OrthoDB; 1593797at2759; -.
DR   PRO; PR:O22882; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22882; baseline and differential.
DR   GO; GO:0048046; C:apoplast; ISS:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR   GO; GO:1902025; P:nitrate import; ISS:UniProtKB.
DR   GO; GO:2000280; P:regulation of root development; ISS:UniProtKB.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR   GO; GO:0009741; P:response to brassinosteroid; IEP:UniProtKB.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
PE   2: Evidence at transcript level;
KW   Apoplast; Developmental protein; Hormone; Hydroxylation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..90
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000440014"
FT   PEPTIDE         91..105
FT                   /note="C-terminally encoded peptide 15"
FT                   /evidence="ECO:0000250|UniProtKB:Q058G9"
FT                   /id="PRO_0000440015"
FT   REGION          68..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         99
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q058G9"
FT   MOD_RES         101
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L8Y3"
FT   CONFLICT        9
FT                   /note="D -> E (in Ref. 4; AAM62632)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="V -> M (in Ref. 4; AAM62632)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   105 AA;  11373 MW;  45B8A865A471258C CRC64;
     MDATKIKFDV ILLSFLLIIS GIPSNLGLST SVRGTTRSEP EAFHGGKFPA MKMRKLMAPN
     MEVDYSSDYY DGGSSSSTTS PSPPVPDYDD IYRRQGDVPS PGIGH
 
 
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