ICLN_CANLF
ID ICLN_CANLF Reviewed; 235 AA.
AC P35521;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 121.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
RC TISSUE=Kidney;
RX PubMed=1313151; DOI=10.1038/356238a0;
RA Paulmichl M., Li Y., Wickman K., Ackerman M., Peralta E.G., Clapham D.E.;
RT "New mammalian chloride channel identified by expression cloning.";
RL Nature 356:238-241(1992).
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}.
CC -!- CAUTION: Was originally thought to be a chloride channel.
CC {ECO:0000305|PubMed:1313151}.
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DR EMBL; X65450; CAA46447.1; -; mRNA.
DR PIR; S23401; S23401.
DR RefSeq; NP_001003288.1; NM_001003288.1.
DR PDB; 1ZYI; NMR; -; A=18-133.
DR PDBsum; 1ZYI; -.
DR AlphaFoldDB; P35521; -.
DR BMRB; P35521; -.
DR SMR; P35521; -.
DR STRING; 9612.ENSCAFP00000007306; -.
DR iPTMnet; P35521; -.
DR PaxDb; P35521; -.
DR GeneID; 403971; -.
DR KEGG; cfa:403971; -.
DR CTD; 1207; -.
DR eggNOG; KOG3238; Eukaryota.
DR InParanoid; P35521; -.
DR OrthoDB; 1508796at2759; -.
DR EvolutionaryTrace; P35521; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0016020; C:membrane; IDA:CAFA.
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:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IMP:CAFA.
DR GO; GO:0005267; F:potassium channel activity; IMP:CAFA.
DR GO; GO:1990935; F:splicing factor binding; IPI:CAFA.
DR GO; GO:0006884; P:cell volume homeostasis; IEA:InterPro.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:CAFA.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:CAFA.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR DisProt; DP00717; -.
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; Acetylation; Cytoplasm; Cytoskeleton; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT CHAIN 2..235
FT /note="Methylosome subunit pICln"
FT /id="PRO_0000185154"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 191
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 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MUTAGEN 49
FT /note="G->A: Removes cAMP sensitivity."
FT /evidence="ECO:0000269|PubMed:1313151"
FT MUTAGEN 51
FT /note="G->A: Removes cAMP sensitivity."
FT /evidence="ECO:0000269|PubMed:1313151"
FT MUTAGEN 53
FT /note="G->A: Removes cAMP sensitivity."
FT /evidence="ECO:0000269|PubMed:1313151"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:1ZYI"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1ZYI"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1ZYI"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1ZYI"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1ZYI"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1ZYI"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1ZYI"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1ZYI"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:1ZYI"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:1ZYI"
SQ SEQUENCE 235 AA; 25935 MW; 8360BA9E6C6955D1 CRC64;
MSFLKSFPPP GSAEGLRQQQ PETEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT
ISLHAVSRDL NAYPREHLYV MVNAKFGEES KESVAEEEDS DDDVEPIAEF RFVPSDKSAL
EAMFTAMCEC QALHPDPEDE DSDDYDGEEY DVEAHEQGQG DIPTFYTYEE GLSHLTAEGQ
ATLERLEGML SQSVSSQYNM AGVRTEDSTR DYEDGMEVDT TPTVAGQFED ADVDH
