ICLN_RABIT
ID ICLN_RABIT Reviewed; 236 AA.
AC Q28678; O02820;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 25-MAY-2022, entry version 90.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white; TISSUE=Ocular ciliary epithelium;
RX PubMed=9367830; DOI=10.1006/bbrc.1997.7523;
RA Wan X.L., Chen S., Sears M.;
RT "Cloning and functional expression of a swelling-induced chloride
RT conductance regulatory protein, plCln, from rabbit ocular ciliary
RT epithelium.";
RL Biochem. Biophys. Res. Commun. 239:692-696(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Heart;
RA Okada H., Ishii K., Nunoki K., Taira N.;
RT "Molecular cloning and expression of rabbit heart chloride channel.";
RL Submitted (DEC-1993) 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 {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: Widely distributed but expressed more abundantly in
CC nonpigmented ciliary epithelial cells than in pigmented ones.
CC {ECO:0000269|PubMed:9367830}.
CC -!- SIMILARITY: Belongs to the pICln (TC 1.A.47) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF003907; AAC48778.1; -; mRNA.
DR EMBL; D26076; BAA05069.1; ALT_INIT; mRNA.
DR PIR; JC5790; JC5790.
DR AlphaFoldDB; Q28678; -.
DR SMR; Q28678; -.
DR STRING; 9986.ENSOCUP00000016544; -.
DR PRIDE; Q28678; -.
DR eggNOG; KOG3238; Eukaryota.
DR InParanoid; Q28678; -.
DR Proteomes; UP000001811; 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..236
FT /note="Methylosome subunit pICln"
FT /id="PRO_0000224183"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54105"
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"
FT CONFLICT 5
FT /note="K -> R (in Ref. 2; BAA05069)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="P -> L (in Ref. 2; BAA05069)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="L -> W (in Ref. 1; AAC48778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 26065 MW; 76342DF2A474D7DA CRC64;
MSFLKSFPPP GPTEGLRHQQ PDTEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT
ISLHAVSRDP NAYPQEHLYV MVNAKFGEES KELVADEEED SDDDVEPISE FRFVPGDKSA
LEAMFTAMCE CQALHPDPED EDSDDYDGEE YDVEAHEQGQ GDIPTFYTYE EGLSHLTAEG
QATLERLEGM LSQSVSSQYN MAGVRTEDSI RDYEDGMEVD TTPTVAGQFE DADVDH
