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Protein

mRNA-decapping enzyme-like protein

Gene

At1g08370

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

As a component of the decapping complex, involved in the degradation of mRNAs. Essential for postembryonic development.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing

Enzyme and pathway databases

ReactomeiR-ATH-430039. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-decapping enzyme-like protein (EC:3.-.-.-)
Alternative name(s):
DCP1 homolog
Gene namesi
Ordered Locus Names:At1g08370
ORF Names:T27G7.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G08370.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • cytoplasmic mRNA processing body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Lethal phenotype at the seedling cotyledon stage, with disorganized veins, swollen root hairs, and altered epidermal cell morphology.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367mRNA-decapping enzyme-like proteinPRO_0000189636Add
BLAST

Proteomic databases

PaxDbiQ9SJF3.
PRIDEiQ9SJF3.

PTM databases

iPTMnetiQ9SJF3.

Expressioni

Tissue specificityi

Expressed in seedlings, mostly in root tips, root hairs, and the vascular system. Also present in roots, leaves, stems, and flowers.1 Publication

Developmental stagei

Gradually accumulates during seed maturation to reached maximum levels in dry seeds. Fades progressively upon germination.1 Publication

Gene expression databases

GenevisibleiQ9SJF3. AT.

Interactioni

Subunit structurei

Homodimer. Component of the decapping complex. Interacts with DCP2 and DCP5 (PubMed:17158604, PubMed:19855049). Interacts with BCHA1 (PubMed:26133670).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DCP2Q8GW312EBI-7786643,EBI-4425465
DCP5Q9C6582EBI-7786643,EBI-4440994

Protein-protein interaction databases

BioGridi22598. 10 interactions.
DIPiDIP-61572N.
IntActiQ9SJF3. 3 interactions.
MINTiMINT-8393469.
STRINGi3702.AT1G08370.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SJF3.
SMRiQ9SJF3. Positions 19-134, 334-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi212 – 333122Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the DCP1 family.Curated

Phylogenomic databases

eggNOGiKOG2868. Eukaryota.
ENOG410XRY6. LUCA.
HOGENOMiHOG000242228.
InParanoidiQ9SJF3.
KOiK12611.
OMAiARIATNE.
PhylomeDBiQ9SJF3.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR010334. Dcp1.
IPR011993. PH_dom-like.
[Graphical view]
PANTHERiPTHR16290. PTHR16290. 1 hit.
PfamiPF06058. DCP1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9SJF3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQNGKIIPN LDQNSTRLLN LTVLQRIDPY IEEILITAAH VTFYEFNIEL
60 70 80 90 100
SQWSRKDVEG SLFVVKRSTQ PRFQFIVMNR RNTDNLVENL LGDFEYEVQG
110 120 130 140 150
PYLLYRNASQ EVNGIWFYNK RECEEVATLF NRILSAYSKV NQKPKASSSK
160 170 180 190 200
SEFEELEAKP TMAVMDGPLE PSSTARDAPD DPAFVNFFSS TMNLGNTASG
210 220 230 240 250
SASGPYQSSA IPHQPHQPHQ PTIAPPVAAA APPQIQSPPP LQSSSPLMTL
260 270 280 290 300
FDNNPEVISS NSNIHTDLVT PSFFGPPRMM AQPHLIPGVS MPTAPPLNPN
310 320 330 340 350
NASHQQRSYG TPVLQPFPPP TPPPSLAPAP TGPVISRDKV KEALLSLLQE
360
DEFIDKITRT LQNALQQ
Length:367
Mass (Da):40,611
Last modified:June 7, 2005 - v2
Checksum:i1820226F02FEE28D
GO

Sequence cautioni

The sequence AAF22887.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121P → PHQP in AAC17938 (Ref. 1) Curated
Sequence conflicti293 – 2931T → S in AAC17938 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007109 mRNA. Translation: AAC17938.1.
AC006932 Genomic DNA. Translation: AAF22887.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28282.1.
PIRiT52141.
RefSeqiNP_563814.1. NM_100710.3.
UniGeneiAt.24949.

Genome annotation databases

EnsemblPlantsiAT1G08370.1; AT1G08370.1; AT1G08370.
GeneIDi837357.
GrameneiAT1G08370.1; AT1G08370.1; AT1G08370.
KEGGiath:AT1G08370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007109 mRNA. Translation: AAC17938.1.
AC006932 Genomic DNA. Translation: AAF22887.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28282.1.
PIRiT52141.
RefSeqiNP_563814.1. NM_100710.3.
UniGeneiAt.24949.

3D structure databases

ProteinModelPortaliQ9SJF3.
SMRiQ9SJF3. Positions 19-134, 334-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi22598. 10 interactions.
DIPiDIP-61572N.
IntActiQ9SJF3. 3 interactions.
MINTiMINT-8393469.
STRINGi3702.AT1G08370.1.

PTM databases

iPTMnetiQ9SJF3.

Proteomic databases

PaxDbiQ9SJF3.
PRIDEiQ9SJF3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G08370.1; AT1G08370.1; AT1G08370.
GeneIDi837357.
GrameneiAT1G08370.1; AT1G08370.1; AT1G08370.
KEGGiath:AT1G08370.

Organism-specific databases

TAIRiAT1G08370.

Phylogenomic databases

eggNOGiKOG2868. Eukaryota.
ENOG410XRY6. LUCA.
HOGENOMiHOG000242228.
InParanoidiQ9SJF3.
KOiK12611.
OMAiARIATNE.
PhylomeDBiQ9SJF3.

Enzyme and pathway databases

ReactomeiR-ATH-430039. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

PROiQ9SJF3.

Gene expression databases

GenevisibleiQ9SJF3. AT.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR010334. Dcp1.
IPR011993. PH_dom-like.
[Graphical view]
PANTHERiPTHR16290. PTHR16290. 1 hit.
PfamiPF06058. DCP1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Putative homolog of yeast dcp1 gene."
    van Hoof A., Green P.J.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for postembryonic development."
    Xu J., Yang J.-Y., Niu Q.-W., Chua N.-H.
    Plant Cell 18:3386-3398(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DCP2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  5. "Characterization of Arabidopsis decapping proteins AtDCP1 and AtDCP2, which are essential for post-embryonic development."
    Iwasaki S., Takeda A., Motose H., Watanabe Y.
    FEBS Lett. 581:2455-2459(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMER, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  6. "Arabidopsis decapping 5 is required for mRNA decapping, P-body formation, and translational repression during postembryonic development."
    Xu J., Chua N.-H.
    Plant Cell 21:3270-3279(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCP5, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  7. "The BEACH domain protein SPIRRIG is essential for Arabidopsis salt stress tolerance and functions as a regulator of transcript stabilization and localization."
    Steffens A., Braeutigam A., Jakoby M., Huelskamp M.
    PLoS Biol. 13:E1002188-E1002188(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCHA1, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDCP1_ARATH
AccessioniPrimary (citable) accession number: Q9SJF3
Secondary accession number(s): O64895
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: February 17, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.