ID   ICLN_PONAB              Reviewed;         237 AA.
AC   Q5R719;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Methylosome subunit pICln;
DE   AltName: Full=Chloride channel, nucleotide sensitive 1A;
DE   AltName: Full=Chloride conductance regulatory protein ICln;
DE            Short=I(Cln);
GN   Name=CLNS1A; Synonyms=ICLN;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in both the assembly of spliceosomal snRNPs and the
CC       methylation of Sm proteins (By similarity). Chaperone that regulates
CC       the assembly of spliceosomal U1, U2, U4 and U5 small nuclear
CC       ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC       and thereby plays an important role in the splicing of cellular pre-
CC       mRNAs (By similarity). Most spliceosomal snRNPs contain a common set of
CC       Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that
CC       assemble in a heptameric protein ring on the Sm site of the small
CC       nuclear RNA to form the core snRNP (Sm core) (By similarity). In the
CC       cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are
CC       trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that
CC       controls the assembly of the core snRNP (By similarity). Dissociation
CC       by 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}.
CC   -!- SUBUNIT: Component of the methylosome, a 20S complex containing at
CC       least PRMT5/SKB1, WDR77/MEP50 and CLNS1A/pICln. 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. Interacts with LSM10 and LSM11
CC       (By similarity). {ECO:0000250|UniProtKB:P54105}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P54105}. Nucleus {ECO:0000250|UniProtKB:P54105}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P54105}. Note=A small
CC       fraction is also associated with the cytoskeleton.
CC       {ECO:0000250|UniProtKB:P54105}.
CC   -!- SIMILARITY: Belongs to the pICln (TC 1.A.47) family. {ECO:0000305}.
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DR   EMBL; CR860304; CAH92441.1; -; mRNA.
DR   RefSeq; NP_001126440.1; NM_001132968.1.
DR   AlphaFoldDB; Q5R719; -.
DR   SMR; Q5R719; -.
DR   STRING; 9601.ENSPPYP00000004240; -.
DR   GeneID; 100173424; -.
DR   KEGG; pon:100173424; -.
DR   CTD; 1207; -.
DR   eggNOG; KOG3238; Eukaryota.
DR   InParanoid; Q5R719; -.
DR   OrthoDB; 1508796at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0034715; C:pICln-Sm protein complex; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0006884; P:cell volume homeostasis; IEA:InterPro.
DR   GO; GO:0006821; P:chloride transport; IEA:InterPro.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Cytoskeleton; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P54105"
FT   CHAIN           2..237
FT                   /note="Methylosome subunit pICln"
FT                   /id="PRO_0000224182"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54105"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54105"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54105"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54105"
FT   MOD_RES         195
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54105"
FT   MOD_RES         223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P54105"
SQ   SEQUENCE   237 AA;  26272 MW;  77CD5996AF062A3B CRC64;
     MSFLKSFPPP GPAEGLLRQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT
     ISLHALSRDR SDCLGEHLYV MVNAKFEEES KEPVADEEEE DSDDDVEPIT EFRFVPSDKS
     ALEAMFTAMC ECQALHPDPE DEDSDDYDGE EYDVEAHEQG QGDIPTFYTY EEGLSHLTAE
     GQATQERLEG MLSQSVSCQY NMAGVRTEDL IRDYEDGMEV DTTPTVAGQF EDADVDH