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A1ZAW5 (ICLN_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylosome subunit pICln
Gene names
Name:icln
ORF Names:CG4924
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus By similarity. Ref.5

Subunit structure

Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1 and WDR77/MEP50; may mediate SNRPD1 and SNRPD3 methylation. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. Ref.5

Subcellular location

Cytoplasmcytosol By similarity. Nucleus By similarity. Cytoplasmcytoskeleton By similarity.

Sequence similarities

Belongs to the pICln (TC 1.A.47) family. [View classification]

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Molecular functionChaperone
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processspliceosomal snRNP assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Methylosome subunit pICln
PRO_0000425412

Experimental info

Sequence conflict61R → H in AAF21126. Ref.1
Sequence conflict61R → H in AAL89952. Ref.4

Secondary structure

................. 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A1ZAW5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: AD92706F7891D800

FASTA21523,743
        10         20         30         40         50         60 
MVLIMRVSPP EHGLLYTANN IKLKLGDKVV GEGTVYIAQN TLSWQPTELA EGISIEWKQV 

        70         80         90        100        110        120 
SLHGISSNPR KCIYFMLDHK VEWNGVYGDP PQQAVNGRNG GGSEAEVDEG NGSDEHDEDD 

       130        140        150        160        170        180 
NFEDAVDEQF GEVTECWLMP EDIHTVDTMY SAMTTCQALH PDSANSDSED SDPMQDAGGL 

       190        200        210 
EDEAMEEDDA LTLGRNGVQN LSLDDDEERF EDADE 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of ICLn."
Laurencon A., Hawley S.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Structural basis of assembly chaperone-mediated snRNP formation."
Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K., Stark H., Schindelin H., Fischer U.
Mol. Cell 49:692-703(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-180 IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN 6S PICLN-SM COMPLEX, FUNCTION IN SNRNP BIOGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF216522 mRNA. Translation: AAF21126.1.
AE013599 Genomic DNA. Translation: AAF57826.1.
AY084214 mRNA. Translation: AAL89952.1.
RefSeqNP_611237.2. NM_137393.4.
UniGeneDm.6477.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VU2X-ray3.103/G/O/W/e/m/u1-180[»]
1VU3X-ray3.10G/O/W/e/m/u1-180[»]
4F77X-ray3.103/G/O/W/e/m/u1-180[»]
4F7UX-ray1.90P/Q1-160[»]
ProteinModelPortalA1ZAW5.
SMRA1ZAW5. Positions 1-168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActA1ZAW5. 1 interaction.
STRING7227.FBpp0086010.

Proteomic databases

PaxDbA1ZAW5.
PRIDEA1ZAW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0086832; FBpp0086010; FBgn0029079.
GeneID36997.
KEGGdme:Dmel_CG4924.
UCSCCG4924-RA. d. melanogaster.

Organism-specific databases

CTD30699.
FlyBaseFBgn0029079. icln.

Phylogenomic databases

eggNOGNOG290633.
GeneTreeENSGT00390000010063.
InParanoidA1ZAW5.
KOK05019.
OMAYTANNIK.
OrthoDBEOG7H1JMG.
PhylomeDBA1ZAW5.

Gene expression databases

BgeeA1ZAW5.

Family and domain databases

InterProIPR003521. ICln.
[Graphical view]
PANTHERPTHR21399. PTHR21399. 1 hit.
PRINTSPR01348. ICLNCHANNEL.
ProtoNetSearch...

Other

GenomeRNAi36997.
NextBio801424.
PROA1ZAW5.

Entry information

Entry nameICLN_DROME
AccessionPrimary (citable) accession number: A1ZAW5
Secondary accession number(s): Q9U3W1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase