CLNS1A

Protein-coding gene in humans
CLNS1A
Identifiers
AliasesCLNS1A, CLCI, CLNS1B, ICln, chloride nucleotide-sensitive channel 1A
External IDsOMIM: 602158; MGI: 109638; HomoloGene: 990; GeneCards: CLNS1A; OMA:CLNS1A - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for CLNS1A
Genomic location for CLNS1A
Band11q14.1Start77,514,936 bp[1]
End77,637,794 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for CLNS1A
Genomic location for CLNS1A
Band7 E1|7 53.57 cMStart97,345,841 bp[2]
End97,370,003 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • ganglionic eminence

  • body of pancreas

  • right adrenal gland

  • left adrenal gland

  • monocyte

  • rectum

  • corpus callosum

  • lymph node

  • thymus
Top expressed in
  • motor neuron

  • primitive streak

  • medial ganglionic eminence

  • condyle

  • fossa

  • hair follicle

  • renal corpuscle

  • internal carotid artery

  • facial motor nucleus

  • external carotid artery
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein heterodimerization activity
  • protein binding
  • RNA binding
Cellular component
  • plasma membrane
  • cytoskeleton
  • nucleoplasm
  • nucleus
  • methylosome
  • pICln-Sm protein complex
  • cytosol
  • cytoplasm
Biological process
  • cell volume homeostasis
  • chloride transport
  • spliceosomal snRNP assembly
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1207

12729

Ensembl

ENSG00000074201

ENSMUSG00000025439

UniProt

P54105

Q61189
Q923F1

RefSeq (mRNA)

NM_001311202
NM_001293
NM_001311199
NM_001311200
NM_001311201

NM_023671

RefSeq (protein)

NP_001284
NP_001298128
NP_001298129
NP_001298130
NP_001298131

NP_076160

Location (UCSC)Chr 11: 77.51 – 77.64 MbChr 7: 97.35 – 97.37 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Methylosome subunit pICln is a protein that in humans is encoded by the CLNS1A gene.[5][6][7]

Interactions

CLNS1A has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000074201 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025439 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Anguita J, Chalfant ML, Civan MM, Coca-Prados M (Apr 1995). "Molecular cloning of the human volume-sensitive chloride conductance regulatory protein, pICln, from ocular ciliary epithelium". Biochem Biophys Res Commun. 208 (1): 89–95. doi:10.1006/bbrc.1995.1309. PMID 7887970.
  6. ^ Nagl UO, Erdel M, Schmarda A, Seri M, Pinggera GM, Gschwentner M, Duba C, Galietta LJ, Deetjen P, Utermann G, Paulmichl M (Mar 1997). "Chromosomal localization of the genes (CLNS1A and CLNS1B) coding for the swelling-dependent chloride channel ICln". Genomics. 38 (3): 438–41. doi:10.1006/geno.1996.0651. PMID 8975725.
  7. ^ "Entrez Gene: CLNS1A chloride channel, nucleotide-sensitive, 1A".
  8. ^ Larkin D, Murphy D, Reilly DF, Cahill M, Sattler E, Harriott P, Cahill DJ, Moran N (Jun 2004). "ICln, a novel integrin alphaIIbbeta3-associated protein, functionally regulates platelet activation". J. Biol. Chem. 279 (26): 27286–93. doi:10.1074/jbc.M402159200. PMID 15075326.
  9. ^ a b c Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G, Rappsilber J, Mann M, Dreyfuss G (Dec 2001). "The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins". Mol. Cell. Biol. 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. PMC 99994. PMID 11713266.
  10. ^ Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE (May 1998). "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology". J. Biol. Chem. 273 (18): 10811–4. doi:10.1074/jbc.273.18.10811. PMID 9556550.
  11. ^ Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, Dreyfuss G (Mar 2002). "A novel WD repeat protein component of the methylosome binds Sm proteins". J. Biol. Chem. 277 (10): 8243–7. doi:10.1074/jbc.M109984200. PMID 11756452.
  12. ^ Krzyzanowski A, Gasper R, Adihou H, 't Hart P, Waldmann H (Feb 2021). "Biochemical Investigation of the Interaction of pICln, RioK1 and COPR5 with the PRMT5-MEP50 Complex". ChemBioChem. 22 (11): 1908–1914. doi:10.1002/cbic.202100079. PMC 8252068. PMID 33624332.

Further reading

  • Calinisan V, Gravem D, Chen RP, Brittin S, Mohandas N, Lecomte MC, Gascard P (2006). "New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium". Front. Biosci. 11: 1646–66. doi:10.2741/1911. PMID 16368544. S2CID 26325962.
  • Buyse G, de Greef C, Raeymaekers L, Droogmans G, Nilius B, Eggermont J (1996). "The ubiquitously expressed pICln protein forms homomeric complexes in vitro". Biochem. Biophys. Res. Commun. 218 (3): 822–7. doi:10.1006/bbrc.1996.0146. PMID 8579598.
  • Schwartz RS, Rybicki AC, Nagel RL (1997). "Molecular cloning and expression of a chloride channel-associated protein pICln in human young red blood cells: association with actin". Biochem. J. 327 (2): 609–16. doi:10.1042/bj3270609. PMC 1218836. PMID 9359436.
  • Bekri S, Adélaïde J, Merscher S, Grosgeorge J, Caroli-Bosc F, Perucca-Lostanlen D, Kelley PM, Pébusque MJ, Theillet C, Birnbaum D, Gaudray P (1998). "Detailed map of a region commonly amplified at 11q13→q14 in human breast carcinoma". Cytogenet. Cell Genet. 79 (1–2): 125–31. doi:10.1159/000134699. PMID 9533029.
  • Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE (1998). "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology". J. Biol. Chem. 273 (18): 10811–4. doi:10.1074/jbc.273.18.10811. PMID 9556550.
  • Tang CJ, Tang TK (1998). "The 30-kD domain of protein 4.1 mediates its binding to the carboxyl terminus of pICln, a protein involved in cellular volume regulation". Blood. 92 (4): 1442–7. doi:10.1182/blood.V92.4.1442. PMID 9694734.
  • Pu WT, Krapivinsky GB, Krapivinsky L, Clapham DE (1999). "pICln inhibits snRNP biogenesis by binding core spliceosomal proteins". Mol. Cell. Biol. 19 (6): 4113–20. doi:10.1128/MCB.19.6.4113. PMC 104370. PMID 10330151.
  • Hubert MD, Levitan I, Hoffman MM, Zraggen M, Hofreiter ME, Garber SS (2000). "Modulation of volume regulated anion current by I(Cln)". Biochim. Biophys. Acta. 1466 (1–2): 105–14. doi:10.1016/S0005-2736(00)00177-2. PMID 10825435.
  • Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G, Rappsilber J, Mann M, Dreyfuss G (2001). "The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins". Mol. Cell. Biol. 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. PMC 99994. PMID 11713266.
  • Meister G, Eggert C, Bühler D, Brahms H, Kambach C, Fischer U (2002). "Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln". Curr. Biol. 11 (24): 1990–4. doi:10.1016/S0960-9822(01)00592-9. hdl:11858/00-001M-0000-0012-F501-7. PMID 11747828. S2CID 14742376.
  • Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, Dreyfuss G (2002). "A novel WD repeat protein component of the methylosome binds Sm proteins". J. Biol. Chem. 277 (10): 8243–7. doi:10.1074/jbc.M109984200. PMID 11756452.
  • Meyer G, Rodighiero S, Guizzardi F, Bazzini C, Bottà G, Bertocchi C, Garavaglia L, Dossena S, Manfredi R, Sironi C, Catania A, Paulmichl M (2004). "Volume-regulated Cl− channels in human pleural mesothelioma cells". FEBS Lett. 559 (1–3): 45–50. doi:10.1016/S0014-5793(04)00020-1. PMID 14960305. S2CID 24747269.
  • Larkin D, Murphy D, Reilly DF, Cahill M, Sattler E, Harriott P, Cahill DJ, Moran N (2004). "ICln, a novel integrin alphaIIbbeta3-associated protein, functionally regulates platelet activation". J. Biol. Chem. 279 (26): 27286–93. doi:10.1074/jbc.M402159200. PMID 15075326.
  • Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M (2005). "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4". J. Biol. Chem. 280 (35): 31276–82. doi:10.1074/jbc.M500541200. PMID 15905169.
  • Azzouz TN, Pillai RS, Däpp C, Chari A, Meister G, Kambach C, Fischer U, Schümperli D (2005). "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes". J. Biol. Chem. 280 (41): 34435–40. doi:10.1074/jbc.M505077200. hdl:21.11116/0000-0007-E5F1-6. PMID 16087681.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

  • v
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  • e
  • 1zyi: Solution structure of ICLN, a multifunctional protein involved in regulatory mechanisms as different as cell volume regulation and rna splicing
    1zyi: Solution structure of ICLN, a multifunctional protein involved in regulatory mechanisms as different as cell volume regulation and rna splicing
  • v
  • t
  • e
Ligand-gated
Voltage-gated
Constitutively active
Proton-gated
Voltage-gated
Calcium-activated
Inward-rectifier
Tandem pore domain
Voltage-gated
Miscellaneous
Cl−: Chloride channel
H+: Proton channel
M+: CNG cation channel
M+: TRP cation channel
H2O (+ solutes): Porin
Cytoplasm: Gap junction
By gating mechanism
Ion channel class
see also disorders


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