DCP5_ARATH
ID DCP5_ARATH Reviewed; 611 AA.
AC Q9C658; B9DHI7; F4IE33; Q8RWC4; Q9ASU0; Q9C604;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Protein decapping 5;
GN Name=DCP5; OrderedLocusNames=At1g26110; ORFNames=F14G11.8, F28B23.21;
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 MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-552.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, HOMODIMER, INTERACTION WITH DCP1 AND DCP2, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, 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).
CC -!- FUNCTION: As a component of the decapping complex, involved in the
CC degradation of mRNAs. Promotes P-body formation. Translational
CC repressor. {ECO:0000269|PubMed:19855049}.
CC -!- SUBUNIT: Homodimer. Component of the decapping complex. Interacts with
CC DCP1 and DCP2. {ECO:0000269|PubMed:19855049}.
CC -!- INTERACTION:
CC Q9C658; Q9SJF3: At1g08370; NbExp=2; IntAct=EBI-4440994, EBI-7786643;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:19855049}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C658-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C658-2; Sequence=VSP_044028;
CC -!- DEVELOPMENTAL STAGE: Gradually accumulates during seed maturation and
CC reaches maximum levels in dry seeds. Fades progressively upon
CC germination. {ECO:0000269|PubMed:19855049}.
CC -!- DISRUPTION PHENOTYPE: Seedlings with pale and weak cotyledons,
CC characterized by disorganized veins. Impaired mRNA decapping and
CC reduced P-bodies size. Altered transient seed storage proteins (SSPs)
CC translational repression and degradation during seed germination.
CC {ECO:0000269|PubMed:19855049}.
CC -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50526.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079829; AAG50671.1; -; Genomic_DNA.
DR EMBL; AC084221; AAG50526.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30649.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30650.1; -; Genomic_DNA.
DR EMBL; AF361833; AAK32845.1; -; mRNA.
DR EMBL; AY078047; AAL77748.1; -; mRNA.
DR EMBL; AY093191; AAM13190.1; -; mRNA.
DR EMBL; AK317540; BAH20204.1; -; mRNA.
DR PIR; B86387; B86387.
DR RefSeq; NP_001154367.1; NM_001160895.1. [Q9C658-2]
DR RefSeq; NP_564239.1; NM_102376.4. [Q9C658-1]
DR AlphaFoldDB; Q9C658; -.
DR SMR; Q9C658; -.
DR BioGRID; 24389; 7.
DR IntAct; Q9C658; 6.
DR MINT; Q9C658; -.
DR STRING; 3702.AT1G26110.1; -.
DR iPTMnet; Q9C658; -.
DR PaxDb; Q9C658; -.
DR PRIDE; Q9C658; -.
DR ProteomicsDB; 224684; -. [Q9C658-1]
DR EnsemblPlants; AT1G26110.1; AT1G26110.1; AT1G26110. [Q9C658-1]
DR EnsemblPlants; AT1G26110.2; AT1G26110.2; AT1G26110. [Q9C658-2]
DR GeneID; 839152; -.
DR Gramene; AT1G26110.1; AT1G26110.1; AT1G26110. [Q9C658-1]
DR Gramene; AT1G26110.2; AT1G26110.2; AT1G26110. [Q9C658-2]
DR KEGG; ath:AT1G26110; -.
DR Araport; AT1G26110; -.
DR TAIR; locus:2011410; AT1G26110.
DR eggNOG; KOG1073; Eukaryota.
DR HOGENOM; CLU_028438_0_0_1; -.
DR InParanoid; Q9C658; -.
DR OMA; GIAMPMY; -.
DR OrthoDB; 1569369at2759; -.
DR PhylomeDB; Q9C658; -.
DR PRO; PR:Q9C658; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C658; baseline and differential.
DR Genevisible; Q9C658; AT.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IMP:TAIR.
DR GO; GO:0033962; P:P-body assembly; IMP:TAIR.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IMP:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR CDD; cd01736; LSm14_N; 1.
DR InterPro; IPR025762; DFDF.
DR InterPro; IPR019050; FDF_dom.
DR InterPro; IPR025761; FFD_box.
DR InterPro; IPR025609; Lsm14-like_N.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR025768; TFG_box.
DR Pfam; PF09532; FDF; 1.
DR Pfam; PF12701; LSM14; 1.
DR SMART; SM01199; FDF; 1.
DR SMART; SM01271; LSM14; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR PROSITE; PS51512; DFDF; 1.
DR PROSITE; PS51513; FFD; 1.
DR PROSITE; PS51536; TFG; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; mRNA processing; Reference proteome;
KW Repressor; Translation regulation.
FT CHAIN 1..611
FT /note="Protein decapping 5"
FT /id="PRO_0000418339"
FT DOMAIN 453..489
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 111..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 512..527
FT /note="FFD box"
FT MOTIF 534..554
FT /note="TFG box"
FT COMPBIAS 111..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 429..442
FT /note="KPNGHSFPNHNGYR -> KMHENLSG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044028"
FT CONFLICT 412
FT /note="E -> K (in Ref. 3; AAK32845/AAL77748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 64370 MW; 2BB81ABEFAB33E12 CRC64;
MAADNTGSKS SSAADSYVGS LISLTSKSEI RYEGILYNIN TDESSIGLQN VRSFGTEGRK
KDGPQVPPSD KVYEYILFRG TDIKDLQVKA SPPVQPPAST INNDPAIIQS HYPSPMPTSG
SLPSTASGSL PDISSHNGQP GQHGMGFQNA MPLYQPGGNL GSWGASPQPP MYWQGFYTPP
PNGLPQLHQQ SLIRPPHGLP MPNSLQQPLQ YPNFNTPPPP TGSSSLQGSS LPEAPSSLFP
FSTSSQMLAP SSLPFPGLPP VTLSSSLQST LQSAPSPSLA SEMAPPLLSN KAPITAPPTL
PQDTNLLSFS LSTTRATEAS TGLPLSNKPS VVTGPISPPQ TTPLTSAPVA GVSSSISQDK
PKPLLVTPGQ LLQSGSSAVS LSPPSTNADK DVEVVQVSSS AGLEQSVPVT SEAQPPILPL
PSSARPTQKP NGHSFPNHNG YRGRGRGRGR GAGRSHQVMK FTEDFDFTAM NEKFNKDEVW
GHLGKSTTLD GDEDDDSPTV DEAELPKIEA KPVYNKDDFF DSLSSNTIDR ESQNSRPRFS
EQRKLDTETF GEFSRFRGGR GGRGGYGRNN GYSRGGYGGR GYGGYGGRGG GGGGYGYGGR
GQGRGVSNRT T
