ID DCP1_ARATH Reviewed; 367 AA.
AC Q9SJF3; O64895;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=mRNA-decapping enzyme-like protein;
DE EC=3.-.-.-;
DE AltName: Full=DCP1 homolog;
GN OrderedLocusNames=At1g08370; ORFNames=T27G7.7;
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].
RC STRAIN=cv. Columbia;
RA van Hoof A., Green P.J.;
RT "Putative homolog of yeast dcp1 gene.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, INTERACTION WITH DCP2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=17158604; DOI=10.1105/tpc.106.047605;
RA Xu J., Yang J.-Y., Niu Q.-W., Chua N.-H.;
RT "Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for
RT postembryonic development.";
RL Plant Cell 18:3386-3398(2006).
RN [5]
RP FUNCTION, HOMODIMER, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=17485080; DOI=10.1016/j.febslet.2007.04.051;
RA Iwasaki S., Takeda A., Motose H., Watanabe Y.;
RT "Characterization of Arabidopsis decapping proteins AtDCP1 and AtDCP2,
RT which are essential for post-embryonic development.";
RL FEBS Lett. 581:2455-2459(2007).
RN [6]
RP INTERACTION WITH DCP5, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19855049; DOI=10.1105/tpc.109.070078;
RA Xu J., Chua N.-H.;
RT "Arabidopsis decapping 5 is required for mRNA decapping, P-body formation,
RT and translational repression during postembryonic development.";
RL Plant Cell 21:3270-3279(2009).
RN [7]
RP INTERACTION WITH BCHA1, AND SUBCELLULAR LOCATION.
RX PubMed=26133670; DOI=10.1371/journal.pbio.1002188;
RA Steffens A., Braeutigam A., Jakoby M., Huelskamp M.;
RT "The BEACH domain protein SPIRRIG is essential for Arabidopsis salt stress
RT tolerance and functions as a regulator of transcript stabilization and
RT localization.";
RL PLoS Biol. 13:E1002188-E1002188(2015).
CC -!- FUNCTION: As a component of the decapping complex, involved in the
CC degradation of mRNAs. Essential for postembryonic development.
CC {ECO:0000269|PubMed:17158604, ECO:0000269|PubMed:17485080}.
CC -!- SUBUNIT: Homodimer. Component of the decapping complex. Interacts with
CC DCP2 and DCP5 (PubMed:17158604, PubMed:19855049). Interacts with BCHA1
CC (PubMed:26133670). {ECO:0000269|PubMed:17158604,
CC ECO:0000269|PubMed:19855049, ECO:0000269|PubMed:26133670}.
CC -!- INTERACTION:
CC Q9SJF3; Q8GW31: DCP2; NbExp=2; IntAct=EBI-7786643, EBI-4425465;
CC Q9SJF3; Q9C658: DCP5; NbExp=2; IntAct=EBI-7786643, EBI-4440994;
CC Q9SJF3; F4HZB2: SPI; NbExp=5; IntAct=EBI-7786643, EBI-3386960;
CC Q9SJF3; Q92636: NSMAF; Xeno; NbExp=2; IntAct=EBI-7786643, EBI-2947053;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:17158604,
CC ECO:0000269|PubMed:17485080, ECO:0000269|PubMed:19855049,
CC ECO:0000269|PubMed:26133670}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, mostly in root tips, root
CC hairs, and the vascular system. Also present in roots, leaves, stems,
CC and flowers. {ECO:0000269|PubMed:17158604}.
CC -!- DEVELOPMENTAL STAGE: Gradually accumulates during seed maturation to
CC reached maximum levels in dry seeds. Fades progressively upon
CC germination. {ECO:0000269|PubMed:19855049}.
CC -!- DISRUPTION PHENOTYPE: Lethal phenotype at the seedling cotyledon stage,
CC with disorganized veins, swollen root hairs, and altered epidermal cell
CC morphology. {ECO:0000269|PubMed:17158604}.
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF22887.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF007109; AAC17938.1; -; mRNA.
DR EMBL; AC006932; AAF22887.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28282.1; -; Genomic_DNA.
DR PIR; T52141; T52141.
DR RefSeq; NP_563814.1; NM_100710.4.
DR AlphaFoldDB; Q9SJF3; -.
DR SMR; Q9SJF3; -.
DR BioGRID; 22598; 12.
DR DIP; DIP-61572N; -.
DR IntAct; Q9SJF3; 5.
DR MINT; Q9SJF3; -.
DR STRING; 3702.Q9SJF3; -.
DR iPTMnet; Q9SJF3; -.
DR PaxDb; 3702-AT1G08370-1; -.
DR ProteomicsDB; 224218; -.
DR EnsemblPlants; AT1G08370.1; AT1G08370.1; AT1G08370.
DR GeneID; 837357; -.
DR Gramene; AT1G08370.1; AT1G08370.1; AT1G08370.
DR KEGG; ath:AT1G08370; -.
DR Araport; AT1G08370; -.
DR TAIR; AT1G08370; DCP1.
DR eggNOG; KOG2868; Eukaryota.
DR HOGENOM; CLU_058542_1_0_1; -.
DR InParanoid; Q9SJF3; -.
DR OMA; RCCFNAL; -.
DR OrthoDB; 385293at2759; -.
DR PhylomeDB; Q9SJF3; -.
DR PRO; PR:Q9SJF3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SJF3; baseline and differential.
DR Genevisible; Q9SJF3; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IDA:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd13182; EVH1-like_Dcp1; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290:SF39; MRNA-DECAPPING ENZYME-LIKE PROTEIN; 1.
DR PANTHER; PTHR16290; TRANSCRIPTION FACTOR SMIF DECAPPING ENZYME DCP1; 1.
DR Pfam; PF06058; DCP1; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; mRNA processing; Reference proteome.
FT CHAIN 1..367
FT /note="mRNA-decapping enzyme-like protein"
FT /id="PRO_0000189636"
FT REGION 144..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..330
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 212
FT /note="P -> PHQP (in Ref. 1; AAC17938)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="T -> S (in Ref. 1; AAC17938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40611 MW; 1820226F02FEE28D CRC64;
MSQNGKIIPN LDQNSTRLLN LTVLQRIDPY IEEILITAAH VTFYEFNIEL SQWSRKDVEG
SLFVVKRSTQ PRFQFIVMNR RNTDNLVENL LGDFEYEVQG PYLLYRNASQ EVNGIWFYNK
RECEEVATLF NRILSAYSKV NQKPKASSSK SEFEELEAKP TMAVMDGPLE PSSTARDAPD
DPAFVNFFSS TMNLGNTASG SASGPYQSSA IPHQPHQPHQ PTIAPPVAAA APPQIQSPPP
LQSSSPLMTL FDNNPEVISS NSNIHTDLVT PSFFGPPRMM AQPHLIPGVS MPTAPPLNPN
NASHQQRSYG TPVLQPFPPP TPPPSLAPAP TGPVISRDKV KEALLSLLQE DEFIDKITRT
LQNALQQ
//
