ICLN_DROME
ID ICLN_DROME Reviewed; 215 AA.
AC A1ZAW5; Q9U3W1;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Methylosome subunit pICln;
GN Name=icln; ORFNames=CG4924;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Laurencon A., Hawley S.;
RT "Molecular cloning of ICLn.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-180 IN 6S PICLN-SM COMPLEX,
RP IDENTIFICATION IN 6S PICLN-SM COMPLEX, AND FUNCTION IN SNRNP BIOGENESIS.
RX PubMed=23333303; DOI=10.1016/j.molcel.2012.12.009;
RA Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K.,
RA Stark H., Schindelin H., Fischer U.;
RT "Structural basis of assembly chaperone-mediated snRNP formation.";
RL Mol. Cell 49:692-703(2013).
CC -!- FUNCTION: Involved in both the assembly of spliceosomal snRNPs and the
CC methylation of Sm proteins. Chaperone that regulates the assembly of
CC spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC (snRNPs), the building blocks of the spliceosome, and thereby plays an
CC important role in the splicing of cellular pre-mRNAs. Most spliceosomal
CC snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein
CC ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm
CC core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and
CC SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone
CC CLNS1A that controls the assembly of the core snRNP. Dissociation by
CC the SMN complex of CLNS1A from the trapped Sm proteins and their
CC transfer to an SMN-Sm complex triggers the assembly of core snRNPs and
CC their transport to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:P54105, ECO:0000269|PubMed:23333303}.
CC -!- SUBUNIT: Component of the methylosome, a 20S complex containing at
CC least CLNS1A/pICln, PRMT5/SKB1 and WDR77/MEP50; may mediate SNRPD1 and
CC SNRPD3 methylation. Forms a 6S pICln-Sm complex composed of
CC CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like
CC structure where CLNS1A/pICln mimics additional Sm proteins and which is
CC unable to assemble into the core snRNP. {ECO:0000269|PubMed:23333303}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pICln (TC 1.A.47) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF216522; AAF21126.1; -; mRNA.
DR EMBL; AE013599; AAF57826.1; -; Genomic_DNA.
DR EMBL; AY084214; AAL89952.1; -; mRNA.
DR RefSeq; NP_611237.2; NM_137393.4.
DR PDB; 4F7U; X-ray; 1.90 A; P/Q=1-160.
DR PDB; 4V98; X-ray; 3.10 A; A3/AG/AO/AW/Ae/Am/Au/B3/BG/BO/BW/Be/Bm/Bu/CG/CO/CW/Ce/Cm/Cu=1-180.
DR PDBsum; 4F7U; -.
DR PDBsum; 4V98; -.
DR AlphaFoldDB; A1ZAW5; -.
DR SMR; A1ZAW5; -.
DR BioGRID; 62685; 14.
DR IntAct; A1ZAW5; 3.
DR STRING; 7227.FBpp0086010; -.
DR PaxDb; A1ZAW5; -.
DR PRIDE; A1ZAW5; -.
DR DNASU; 36997; -.
DR EnsemblMetazoa; FBtr0086832; FBpp0086010; FBgn0029079.
DR GeneID; 36997; -.
DR KEGG; dme:Dmel_CG4924; -.
DR UCSC; CG4924-RA; d. melanogaster.
DR CTD; 36997; -.
DR FlyBase; FBgn0029079; icln.
DR VEuPathDB; VectorBase:FBgn0029079; -.
DR eggNOG; KOG3238; Eukaryota.
DR HOGENOM; CLU_077804_4_0_1; -.
DR InParanoid; A1ZAW5; -.
DR OMA; CIYFMLD; -.
DR OrthoDB; 1508796at2759; -.
DR PhylomeDB; A1ZAW5; -.
DR SignaLink; A1ZAW5; -.
DR BioGRID-ORCS; 36997; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36997; -.
DR PRO; PR:A1ZAW5; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0029079; Expressed in eye disc (Drosophila) and 23 other tissues.
DR ExpressionAtlas; A1ZAW5; baseline and differential.
DR Genevisible; A1ZAW5; DM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0034709; C:methylosome; IEA:InterPro.
DR GO; GO:0034715; C:pICln-Sm protein complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0006884; P:cell volume homeostasis; IEA:InterPro.
DR GO; GO:0006821; P:chloride transport; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR003521; ICln.
DR InterPro; IPR039924; ICln/Lot5/Saf5.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR21399; PTHR21399; 1.
DR Pfam; PF03517; Voldacs; 1.
DR PRINTS; PR01348; ICLNCHANNEL.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Cytoskeleton; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome.
FT CHAIN 1..215
FT /note="Methylosome subunit pICln"
FT /id="PRO_0000425412"
FT REGION 88..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 6
FT /note="R -> H (in Ref. 1; AAF21126 and 4; AAL89952)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4F7U"
FT STRAND 14..27
FT /evidence="ECO:0007829|PDB:4F7U"
FT STRAND 29..50
FT /evidence="ECO:0007829|PDB:4F7U"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:4F7U"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:4F7U"
FT STRAND 60..79
FT /evidence="ECO:0007829|PDB:4F7U"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4F7U"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:4F7U"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:4F7U"
SQ SEQUENCE 215 AA; 23743 MW; AD92706F7891D800 CRC64;
MVLIMRVSPP EHGLLYTANN IKLKLGDKVV GEGTVYIAQN TLSWQPTELA EGISIEWKQV
SLHGISSNPR KCIYFMLDHK VEWNGVYGDP PQQAVNGRNG GGSEAEVDEG NGSDEHDEDD
NFEDAVDEQF GEVTECWLMP EDIHTVDTMY SAMTTCQALH PDSANSDSED SDPMQDAGGL
EDEAMEEDDA LTLGRNGVQN LSLDDDEERF EDADE
