ICLN_RAT
ID ICLN_RAT Reviewed; 236 AA.
AC Q04753;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 132.
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, Rcl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8391324; DOI=10.1016/0167-4781(93)90138-4;
RA Abe T., Takeuchi K., Ishii K., Abe K.;
RT "Molecular cloning and expression of a rat cDNA encoding MDCK-type chloride
RT channel.";
RL Biochim. Biophys. Acta 1173:353-356(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7683461; DOI=10.1006/bbrc.1993.1452;
RA Ishibashi K., Sasaki S., Uchida S., Imai T., Marumo F.;
RT "Tissue expression of mRNA of chloride channel from MDCK cells and its
RT regulation by protein kinases.";
RL Biochem. Biophys. Res. Commun. 192:561-567(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neonatal heart atrium;
RX PubMed=8313467; DOI=10.1016/0092-8674(94)90109-0;
RA Krapivinsky G.B., Ackerman M.J., Gordon E.A., Krapivinsky L.D.,
RA Clapham D.E.;
RT "Molecular characterization of a swelling-induced chloride conductance
RT regulatory protein, pICln.";
RL Cell 76:439-448(1994).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Expressed in most tissues.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC37642.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D17698; BAA04561.1; -; mRNA.
DR EMBL; D13985; BAA03092.1; -; mRNA.
DR EMBL; L26450; AAC37642.1; ALT_INIT; mRNA.
DR PIR; B53014; B53014.
DR RefSeq; NP_113907.1; NM_031719.1.
DR RefSeq; XP_006229854.1; XM_006229792.2.
DR AlphaFoldDB; Q04753; -.
DR SMR; Q04753; -.
DR STRING; 10116.ENSRNOP00000017702; -.
DR iPTMnet; Q04753; -.
DR PhosphoSitePlus; Q04753; -.
DR jPOST; Q04753; -.
DR PaxDb; Q04753; -.
DR GeneID; 65160; -.
DR KEGG; rno:65160; -.
DR UCSC; RGD:61884; rat.
DR CTD; 1207; -.
DR RGD; 61884; Clns1a.
DR eggNOG; KOG3238; Eukaryota.
DR InParanoid; Q04753; -.
DR OrthoDB; 1508796at2759; -.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR PRO; PR:Q04753; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
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:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0006884; P:cell volume homeostasis; IMP:RGD.
DR GO; GO:0006821; P:chloride transport; IDA:RGD.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045794; P:negative regulation of cell volume; ISO:RGD.
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 1: Evidence at protein 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..236
FT /note="Methylosome subunit pICln"
FT /id="PRO_0000185157"
FT REGION 134..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
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 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
SQ SEQUENCE 236 AA; 26092 MW; 7430F2B96B5212A7 CRC64;
MSFLKSFPPP GSADGLRLQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT
ISLHAVSRDP NAYPQEHLYV MVNARFGEES KEPFSDEDED DNDDVEPISE FRFVPSDKSA
LEAMFTAMCE CQALHPDPED EDSDDYDGEE YDVEAHEQGQ GDIPTFYTYE EGLSHLTAEG
QATLERLEGM LSQSVSSQYN MAGVRTEDSV RTYEDGMEVE TTPTVAGQFE DADVDH
