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A1ZAW5

- ICLN_DROME

UniProt

A1ZAW5 - ICLN_DROME

Protein

Methylosome subunit pICln

Gene

icln

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Biological processi

    1. cell volume homeostasis Source: InterPro
    2. chloride transport Source: InterPro
    3. spliceosomal snRNP assembly Source: InterPro

    Keywords - Molecular functioni

    Chaperone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylosome subunit pICln
    Gene namesi
    Name:icln
    ORF Names:CG4924
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0029079. icln.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Nucleus By similarity. Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. cytosol Source: UniProtKB-SubCell
    3. methylosome Source: InterPro
    4. nucleus Source: UniProtKB-SubCell
    5. pICln-Sm protein complex Source: InterPro
    6. plasma membrane Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 215215Methylosome subunit pIClnPRO_0000425412Add
    BLAST

    Proteomic databases

    PaxDbiA1ZAW5.
    PRIDEiA1ZAW5.

    Expressioni

    Gene expression databases

    BgeeiA1ZAW5.

    Interactioni

    Subunit structurei

    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.1 Publication

    Protein-protein interaction databases

    IntActiA1ZAW5. 1 interaction.
    STRINGi7227.FBpp0086010.

    Structurei

    Secondary structure

    1
    215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Beta strandi14 – 2714
    Beta strandi29 – 5022
    Beta strandi52 – 565
    Helixi57 – 593
    Beta strandi60 – 7920
    Turni84 – 863
    Beta strandi133 – 1419
    Helixi145 – 15915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliA1ZAW5.
    SMRiA1ZAW5. Positions 1-168.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG290633.
    GeneTreeiENSGT00390000010063.
    InParanoidiA1ZAW5.
    KOiK05019.
    OMAiYTANNIK.
    OrthoDBiEOG7H1JMG.
    PhylomeDBiA1ZAW5.

    Family and domain databases

    InterProiIPR003521. ICln.
    [Graphical view]
    PANTHERiPTHR21399. PTHR21399. 1 hit.
    PRINTSiPR01348. ICLNCHANNEL.

    Sequencei

    Sequence statusi: Complete.

    A1ZAW5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLIMRVSPP EHGLLYTANN IKLKLGDKVV GEGTVYIAQN TLSWQPTELA    50
    EGISIEWKQV SLHGISSNPR KCIYFMLDHK VEWNGVYGDP PQQAVNGRNG 100
    GGSEAEVDEG NGSDEHDEDD NFEDAVDEQF GEVTECWLMP EDIHTVDTMY 150
    SAMTTCQALH PDSANSDSED SDPMQDAGGL EDEAMEEDDA LTLGRNGVQN 200
    LSLDDDEERF EDADE 215
    Length:215
    Mass (Da):23,743
    Last modified:February 6, 2007 - v1
    Checksum:iAD92706F7891D800
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61R → H in AAF21126. 1 PublicationCurated
    Sequence conflicti6 – 61R → H in AAL89952. (PubMed:12537569)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF216522 mRNA. Translation: AAF21126.1.
    AE013599 Genomic DNA. Translation: AAF57826.1.
    AY084214 mRNA. Translation: AAL89952.1.
    RefSeqiNP_611237.2. NM_137393.4.
    UniGeneiDm.6477.

    Genome annotation databases

    EnsemblMetazoaiFBtr0086832; FBpp0086010; FBgn0029079.
    GeneIDi36997.
    KEGGidme:Dmel_CG4924.
    UCSCiCG4924-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF216522 mRNA. Translation: AAF21126.1 .
    AE013599 Genomic DNA. Translation: AAF57826.1 .
    AY084214 mRNA. Translation: AAL89952.1 .
    RefSeqi NP_611237.2. NM_137393.4.
    UniGenei Dm.6477.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VU2 X-ray 3.10 3/G/O/W/e/m/u 1-180 [» ]
    1VU3 X-ray 3.10 G/O/W/e/m/u 1-180 [» ]
    4F77 X-ray 3.10 3/G/O/W/e/m/u 1-180 [» ]
    4F7U X-ray 1.90 P/Q 1-160 [» ]
    ProteinModelPortali A1ZAW5.
    SMRi A1ZAW5. Positions 1-168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi A1ZAW5. 1 interaction.
    STRINGi 7227.FBpp0086010.

    Proteomic databases

    PaxDbi A1ZAW5.
    PRIDEi A1ZAW5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0086832 ; FBpp0086010 ; FBgn0029079 .
    GeneIDi 36997.
    KEGGi dme:Dmel_CG4924.
    UCSCi CG4924-RA. d. melanogaster.

    Organism-specific databases

    CTDi 36997.
    FlyBasei FBgn0029079. icln.

    Phylogenomic databases

    eggNOGi NOG290633.
    GeneTreei ENSGT00390000010063.
    InParanoidi A1ZAW5.
    KOi K05019.
    OMAi YTANNIK.
    OrthoDBi EOG7H1JMG.
    PhylomeDBi A1ZAW5.

    Miscellaneous databases

    GenomeRNAii 36997.
    NextBioi 801424.
    PROi A1ZAW5.

    Gene expression databases

    Bgeei A1ZAW5.

    Family and domain databases

    InterProi IPR003521. ICln.
    [Graphical view ]
    PANTHERi PTHR21399. PTHR21399. 1 hit.
    PRINTSi PR01348. ICLNCHANNEL.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. 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.

    Entry informationi

    Entry nameiICLN_DROME
    AccessioniPrimary (citable) accession number: A1ZAW5
    Secondary accession number(s): Q9U3W1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 19, 2014
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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