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Q9SP32

- DCL1_ARATH

UniProt

Q9SP32 - DCL1_ARATH

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Protein
Endoribonuclease Dicer homolog 1
Gene
DCL1, ASU1, CAF SIN1, SUS1, At1g01040, T25K16.4
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Ribonuclease (RNase) III involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the microRNAs (miRNAs) biogenesis pathway by cleaving primary miRNAs (pri-miRNAs) and precursor miRNAs (pre-miRNAs). Functions with DRB1/HYL1 and SERRATE proteins for accurate pri-miRNAs to miRNAs processing. Indirectly involved in the production of trans-acting small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or TAS3 endogenous transcripts by participating in the production of their initiating miRNAs. Involved in the processing of natural siRNAs (nat-siRNAs, derived from cis-natural antisense transcripts) by cleaving 24 nucleotide nat-siRNAs into 21 nucleotide nat-siRNAs. Can produce RDR6-dependent endogenous ta-siRNAs derived from TAS1 and TAS2. Required for the production of 30-40 nucleotide bacterial-induced long siRNAs (lsiRNA). Acts redundantly with DICER-LIKE 3 (DCL3) to promote flowering via repression of FLOWERING LOCUS C (FLC). Represses antiviral RNA silencing through negative regulation of the expression of DCL4 and DCL3.7 Publications

Cofactori

Magnesium or manganese By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1597 – 15971Magnesium or manganese By similarity
Sitei1689 – 16891Important for activity By similarity
Metal bindingi1693 – 16931Magnesium or manganese By similarity
Metal bindingi1696 – 16961Magnesium or manganese By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi269 – 2768ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: InterPro
  3. RNA binding Source: UniProtKB-KW
  4. helicase activity Source: UniProtKB-KW
  5. metal ion binding Source: UniProtKB-KW
  6. protein binding Source: UniProtKB
  7. ribonuclease III activity Source: InterPro

GO - Biological processi

  1. RNA processing Source: InterPro
  2. gene silencing by RNA Source: UniProtKB-KW
  3. rRNA catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Helicase, Hydrolase, Nuclease

Keywords - Biological processi

RNA-mediated gene silencing

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciARA:AT1G01040-MONOMER.
ARA:GQT-1487-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoribonuclease Dicer homolog 1 (EC:3.1.26.-)
Alternative name(s):
Dicer-like protein 1
Short name:
AtDCL1
Protein ABNORMAL SUSPENSOR 1
Protein CARPEL FACTORY
Protein SHORT INTEGUMENTS 1
Protein SUSPENSOR 1
Gene namesi
Name:DCL1
Synonyms:ASU1, CAF SIN1, SUS1
Ordered Locus Names:At1g01040
ORF Names:T25K16.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G01040.

Subcellular locationi

Nucleus
Note: Localizes to nuclear dicing body (also named D body), a nuclear body distributed throughout the nucleoplasm and involved in miRNA processing.2 Publications

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality in sus-1 mutant. Weaker mutant (caf-1) also exists. Mutant caf-1 produces extra whorls of stamens, indefinite number of carpels and show an absence of axillary inflorescence meristems and abnormally shaped leaves and floral organs.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi395 – 3951E → K in dcl1-13; early-flowering and decreased number of leaves. Suppresses hyl1 mutant phenotype. 1 Publication
Mutagenesisi415 – 4151P → S in sin1-1; impaired reproductive development. 1 Publication
Mutagenesisi431 – 4311I → K in sin1-2; impaired reproductive development. 1 Publication
Mutagenesisi1837 – 18437NDICLRK → IAEIDPG in caf-1; converts the floral meristem to an indeterminate state. 1 Publication
Mutagenesisi1844 – 190966Missing in caf-1; converts the floral meristem to an indeterminate state. 1 Publication
Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19091909Endoribonuclease Dicer homolog 1UniRule annotation
PRO_0000180472Add
BLAST

Proteomic databases

PaxDbiQ9SP32.
PRIDEiQ9SP32.

Expressioni

Tissue specificityi

Highly expressed in flowers and seeds and detected in leaves and stems. Found in ovule integuments, inflorescence and floral meristems, stigma of flowers until just before pollination, vasculature of the funiculus, and embryo.2 Publications

Developmental stagei

Detected in the embryo, but not in the suspensor, up to the globular stage.1 Publication

Gene expression databases

GenevestigatoriQ9SP32.

Interactioni

Subunit structurei

Interacts (via N-terminus) with DDL. Interacts (via DRBM domains) with DRB1, DRB2 and DRB5. May interact with AGO1 or AGO10 through their common PAZ domains By similarity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDLQ8W4D82EBI-632627,EBI-2015534
DRB1O044923EBI-632627,EBI-632620

Protein-protein interaction databases

BioGridi24809. 8 interactions.
DIPiDIP-33454N.
IntActiQ9SP32. 5 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1838 – 18425
Beta strandi1849 – 18546
Beta strandi1864 – 18696
Turni1873 – 18753
Beta strandi1886 – 18883
Helixi1889 – 190315
Helixi1904 – 19063

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LRSNMR-A1837-1907[»]
ProteinModelPortaliQ9SP32.
SMRiQ9SP32. Positions 248-495, 647-803, 835-939, 1295-1440, 1559-1795.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini256 – 433178Helicase ATP-binding
Add
BLAST
Domaini651 – 812162Helicase C-terminal
Add
BLAST
Domaini840 – 93596Dicer dsRNA-binding fold
Add
BLAST
Domaini1180 – 1318139PAZ
Add
BLAST
Domaini1342 – 1518177RNase III 1
Add
BLAST
Domaini1559 – 1707149RNase III 2
Add
BLAST
Domaini1733 – 179664DRBM 1
Add
BLAST
Domaini1831 – 190676DRBM 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi378 – 3814DECH boxUniRule annotation

Sequence similaritiesi

Contains 1 PAZ domain.
Contains 2 RNase III domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1111.
HOGENOMiHOG000239675.
InParanoidiQ9SP32.
KOiK11592.
PhylomeDBiQ9SP32.

Family and domain databases

Gene3Di1.10.1520.10. 3 hits.
3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
HAMAPiMF_00104. RNase_III.
InterProiIPR005034. Dicer_dimerisation_dom.
IPR014720. dsRNA-bd_dom.
IPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR003100. PAZ_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PfamiPF03368. Dicer_dimer. 1 hit.
PF00035. dsrm. 1 hit.
PF00271. Helicase_C. 1 hit.
PF02170. PAZ. 1 hit.
PF04851. ResIII. 1 hit.
PF00636. Ribonuclease_3. 2 hits.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00490. HELICc. 1 hit.
SM00949. PAZ. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]
SUPFAMiSSF101690. SSF101690. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF69065. SSF69065. 4 hits.
PROSITEiPS51327. DICER_DSRBF. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50821. PAZ. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9SP32-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MVMEDEPREA TIKPSYWLDA CEDISCDLID DLVSEFDPSS VAVNESTDEN     50
GVINDFFGGI DHILDSIKNG GGLPNNGVSD TNSQINEVTV TPQVIAKETV 100
KENGLQKNGG KRDEFSKEEG DKDRKRARVC SYQSERSNLS GRGHVNNSRE 150
GDRFMNRKRT RNWDEAGNNK KKRECNNYRR DGRDREVRGY WERDKVGSNE 200
LVYRSGTWEA DHERDVKKVS GGNRECDVKA EENKSKPEER KEKVVEEQAR 250
RYQLDVLEQA KAKNTIAFLE TGAGKTLIAI LLIKSVHKDL MSQNRKMLSV 300
FLVPKVPLVY QQAEVIRNQT CFQVGHYCGE MGQDFWDSRR WQREFESKQV 350
LVMTAQILLN ILRHSIIRME TIDLLILDEC HHAVKKHPYS LVMSEFYHTT 400
PKDKRPAIFG MTASPVNLKG VSSQVDCAIK IRNLETKLDS TVCTIKDRKE 450
LEKHVPMPSE IVVEYDKAAT MWSLHETIKQ MIAAVEEAAQ ASSRKSKWQF 500
MGARDAGAKD ELRQVYGVSE RTESDGAANL IHKLRAINYT LAELGQWCAY 550
KVGQSFLSAL QSDERVNFQV DVKFQESYLS EVVSLLQCEL LEGAAAEKVA 600
AEVGKPENGN AHDEMEEGEL PDDPVVSGGE HVDEVIGAAV ADGKVTPKVQ 650
SLIKLLLKYQ HTADFRAIVF VERVVAALVL PKVFAELPSL SFIRCASMIG 700
HNNSQEMKSS QMQDTISKFR DGHVTLLVAT SVAEEGLDIR QCNVVMRFDL 750
AKTVLAYIQS RGRARKPGSD YILMVERGNV SHAAFLRNAR NSEETLRKEA 800
IERTDLSHLK DTSRLISIDA VPGTVYKVEA TGAMVSLNSA VGLVHFYCSQ 850
LPGDRYAILR PEFSMEKHEK PGGHTEYSCR LQLPCNAPFE ILEGPVCSSM 900
RLAQQAVCLA ACKKLHEMGA FTDMLLPDKG SGQDAEKADQ DDEGEPVPGT 950
ARHREFYPEG VADVLKGEWV SSGKEVCESS KLFHLYMYNV RCVDFGSSKD 1000
PFLSEVSEFA ILFGNELDAE VLSMSMDLYV ARAMITKASL AFKGSLDITE 1050
NQLSSLKKFH VRLMSIVLDV DVEPSTTPWD PAKAYLFVPV TDNTSMEPIK 1100
GINWELVEKI TKTTAWDNPL QRARPDVYLG TNERTLGGDR REYGFGKLRH 1150
NIVFGQKSHP TYGIRGAVAS FDVVRASGLL PVRDAFEKEV EEDLSKGKLM 1200
MADGCMVAED LIGKIVTAAH SGKRFYVDSI CYDMSAETSF PRKEGYLGPL 1250
EYNTYADYYK QKYGVDLNCK QQPLIKGRGV SYCKNLLSPR FEQSGESETV 1300
LDKTYYVFLP PELCVVHPLS GSLIRGAQRL PSIMRRVESM LLAVQLKNLI 1350
SYPIPTSKIL EALTAASCQE TFCYERAELL GDAYLKWVVS RFLFLKYPQK 1400
HEGQLTRMRQ QMVSNMVLYQ FALVKGLQSY IQADRFAPSR WSAPGVPPVF 1450
DEDTKDGGSS FFDEEQKPVS EENSDVFEDG EMEDGELEGD LSSYRVLSSK 1500
TLADVVEALI GVYYVEGGKI AANHLMKWIG IHVEDDPDEV DGTLKNVNVP 1550
ESVLKSIDFV GLERALKYEF KEKGLLVEAI THASRPSSGV SCYQRLEFVG 1600
DAVLDHLITR HLFFTYTSLP PGRLTDLRAA AVNNENFARV AVKHKLHLYL 1650
RHGSSALEKQ IREFVKEVQT ESSKPGFNSF GLGDCKAPKV LGDIVESIAG 1700
AIFLDSGKDT TAAWKVFQPL LQPMVTPETL PMHPVRELQE RCQQQAEGLE 1750
YKASRSGNTA TVEVFIDGVQ VGVAQNPQKK MAQKLAARNA LAALKEKEIA 1800
ESKEKHINNG NAGEDQGENE NGNKKNGHQP FTRQTLNDIC LRKNWPMPSY 1850
RCVKEGGPAH AKRFTFGVRV NTSDRGWTDE CIGEPMPSVK KAKDSAAVLL 1900
LELLNKTFS 1909
Length:1,909
Mass (Da):213,574
Last modified:September 19, 2003 - v2
Checksum:iEAA944F0C0C81D4C
GO

Sequence cautioni

The sequence AAF26461.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481S → F in AAF03534. 1 Publication
Sequence conflicti988 – 9881Y → H in AAF03534. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF187317 mRNA. Translation: AAF03534.1.
AF292940 mRNA. Translation: AAG38019.1.
AF292941 Genomic DNA. Translation: AAG38020.1.
AC007323 Genomic DNA. Translation: AAF26461.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE27220.1.
RefSeqiNP_171612.1. NM_099986.3. [Q9SP32-1]
UniGeneiAt.22088.
At.57123.

Genome annotation databases

EnsemblPlantsiAT1G01040.1; AT1G01040.1; AT1G01040. [Q9SP32-1]
GeneIDi839574.
KEGGiath:AT1G01040.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF187317 mRNA. Translation: AAF03534.1 .
AF292940 mRNA. Translation: AAG38019.1 .
AF292941 Genomic DNA. Translation: AAG38020.1 .
AC007323 Genomic DNA. Translation: AAF26461.1 . Sequence problems.
CP002684 Genomic DNA. Translation: AEE27220.1 .
RefSeqi NP_171612.1. NM_099986.3. [Q9SP32-1 ]
UniGenei At.22088.
At.57123.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LRS NMR - A 1837-1907 [» ]
ProteinModelPortali Q9SP32.
SMRi Q9SP32. Positions 248-495, 647-803, 835-939, 1295-1440, 1559-1795.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 24809. 8 interactions.
DIPi DIP-33454N.
IntActi Q9SP32. 5 interactions.

Proteomic databases

PaxDbi Q9SP32.
PRIDEi Q9SP32.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G01040.1 ; AT1G01040.1 ; AT1G01040 . [Q9SP32-1 ]
GeneIDi 839574.
KEGGi ath:AT1G01040.

Organism-specific databases

TAIRi AT1G01040.

Phylogenomic databases

eggNOGi COG1111.
HOGENOMi HOG000239675.
InParanoidi Q9SP32.
KOi K11592.
PhylomeDBi Q9SP32.

Enzyme and pathway databases

BioCyci ARA:AT1G01040-MONOMER.
ARA:GQT-1487-MONOMER.

Gene expression databases

Genevestigatori Q9SP32.

Family and domain databases

Gene3Di 1.10.1520.10. 3 hits.
3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
HAMAPi MF_00104. RNase_III.
InterProi IPR005034. Dicer_dimerisation_dom.
IPR014720. dsRNA-bd_dom.
IPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR003100. PAZ_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view ]
Pfami PF03368. Dicer_dimer. 1 hit.
PF00035. dsrm. 1 hit.
PF00271. Helicase_C. 1 hit.
PF02170. PAZ. 1 hit.
PF04851. ResIII. 1 hit.
PF00636. Ribonuclease_3. 2 hits.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00490. HELICc. 1 hit.
SM00949. PAZ. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view ]
SUPFAMi SSF101690. SSF101690. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF69065. SSF69065. 4 hits.
PROSITEi PS51327. DICER_DSRBF. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50821. PAZ. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Disruption of an RNA helicase/RNase III gene in Arabidopsis causes unregulated cell division in floral meristems."
    Jacobsen S.E., Running M.P., Meyerowitz E.M.
    Development 126:5231-5243(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF 1837-ASN--LYS-1843 AND 1844-ASN--SER-1909.
    Strain: cv. Wassilewskija.
  2. "SHORT INTEGUMENTS1/SUSPENSOR1/CARPEL FACTORY, a Dicer homolog, is a maternal effect gene required for embryo development in Arabidopsis."
    Golden T.A., Schauer S.E., Lang J.D., Pien S., Mushegian A.R., Grossniklaus U., Meinke D.W., Ray A.
    Plant Physiol. 130:808-822(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-415 AND ILE-431.
    Strain: cv. Landsberg erecta.
  3. "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.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Partially redundant functions of Arabidopsis DICER-like enzymes and a role for DCL4 in producing trans-acting siRNAs."
    Gasciolli V., Mallory A.C., Bartel D.P., Vaucheret H.
    Curr. Biol. 15:1494-1500(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Specific interactions between Dicer-like proteins and HYL1/DRB-family dsRNA-binding proteins in Arabidopsis thaliana."
    Hiraguri A., Itoh R., Kondo N., Nomura Y., Aizawa D., Murai Y., Koiwa H., Seki M., Shinozaki K., Fukuhara T.
    Plant Mol. Biol. 57:173-188(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DRB1; DRB2 AND DRB5.
  7. "The interaction between DCL1 and HYL1 is important for efficient and precise processing of pri-miRNA in plant microRNA biogenesis."
    Kurihara Y., Takashi Y., Watanabe Y.
    RNA 12:206-212(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DRB1.
  8. "Identification of nuclear dicing bodies containing proteins for microRNA biogenesis in living Arabidopsis plants."
    Fang Y., Spector D.L.
    Curr. Biol. 17:818-823(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "A novel class of bacteria-induced small RNAs in Arabidopsis."
    Katiyar-Agarwal S., Gao S., Vivian-Smith A., Jin H.
    Genes Dev. 21:3123-3134(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "DICER-LIKE 1 and DICER-LIKE 3 redundantly act to promote flowering via repression of FLOWERING LOCUS C in Arabidopsis thaliana."
    Schmitz R.J., Hong L., Fitzpatrick K.E., Amasino R.M.
    Genetics 176:1359-1362(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The RNA-binding proteins HYL1 and SE promote accurate in vitro processing of pri-miRNA by DCL1."
    Dong Z., Han M.-H., Fedoroff N.
    Proc. Natl. Acad. Sci. U.S.A. 105:9970-9975(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in small RNA biogenesis."
    Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., Ramachandran V., Li W., Lagrange T., Walker J.C., Chen X.
    Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDL.
  13. "Arabidopsis DRB4, AGO1, AGO7, and RDR6 participate in a DCL4-initiated antiviral RNA silencing pathway negatively regulated by DCL1."
    Qu F., Ye X., Morris T.J.
    Proc. Natl. Acad. Sci. U.S.A. 105:14732-14737(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "A dominant mutation in DCL1 suppresses the hyl1 mutant phenotype by promoting the processing of miRNA."
    Tagami Y., Motose H., Watanabe Y.
    RNA 15:450-458(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-395.

Entry informationi

Entry nameiDCL1_ARATH
AccessioniPrimary (citable) accession number: Q9SP32
Secondary accession number(s): Q9FDY6, Q9MAN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: September 19, 2003
Last modified: June 11, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Expression in the early embryo is from the maternally contributed genome.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi