ICLN_XENLA
ID ICLN_XENLA Reviewed; 241 AA.
AC P54106;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Methylosome subunit pICln;
DE AltName: Full=Chloride conductance regulatory protein ICln;
DE Short=I(Cln);
GN Name=clns1a; Synonyms=icln;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
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).
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 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: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}.
CC -!- SIMILARITY: Belongs to the pICln (TC 1.A.47) family. {ECO:0000305}.
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DR EMBL; L26449; AAC38009.1; -; mRNA.
DR PIR; A53014; A53014.
DR RefSeq; NP_001081766.1; NM_001088297.1.
DR AlphaFoldDB; P54106; -.
DR SMR; P54106; -.
DR MaxQB; P54106; -.
DR DNASU; 398038; -.
DR GeneID; 398038; -.
DR KEGG; xla:398038; -.
DR CTD; 398038; -.
DR Xenbase; XB-GENE-17346342; clns1a.S.
DR OrthoDB; 1508796at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 398038; Expressed in blastula and 19 other tissues.
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 Cytoplasm; Cytoskeleton; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome.
FT CHAIN 1..241
FT /note="Methylosome subunit pICln"
FT /id="PRO_0000185158"
FT REGION 88..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 26446 MW; 4E62C01EDE0E224E CRC64;
MNLLSSFPPP ADGVRRLQPG TEAVVGGRGL GPGTLYIAES RLSWLNGSGL GFSLEYPSIS
LHAISRDTAA YPEEHLYVMV NSKLADKEDK EAHMADQEEE ESEDDDDDEE PITEIRFVPG
EKSDLGEMFS AMCDCQALHP DPEDADSDDD YEGDEYDVEA HEQGQVDVPT FYTYEEGLSH
LTTEGQATLE RLENMLSNSI GNQHTMAGVR TEGPALEPED GMDVENTQTV AGQFEDADVD
H