| General information | | DisProt: | DP00717 | | Name: | Methylosome subunit pICln | | Synonym(s): | ICLN_CANFA
Chloride channel, nucleotide sensitive 1A
Chloride conductance regulatory protein ICln
I(Cln)
ICln
| | First appeared in release: | Release 5.9 (02/23/2012) | | UniProt: | P35521 | | UniGene: | | | SwissProt: | ICLN_CANFA | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Canis familiaris (Dog) (Canis lupus familiaris) | | Sequence length: | 235 | | Percent disordered: | 79% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MSFLKSFPPP GSAEGLRQQQ PETEAVLNGK GLGTGTLYIA ESRLSWLDGS GLGFSLEYPT - 60
ISLHAVSRDL NAYPREHLYV MVNAKFGEES KESVAEEEDS DDDVEPIAEF RFVPSDKSAL - 120
EAMFTAMCEC QALHPDPEDE DSDDYDGEEY DVEAHEQGQG DIPTFYTYEE GLSHLTAEGQ - 180
ATLERLEGML SQSVSSQYNM AGVRTEDSTR DYEDGMEVDT TPTVAGQFED ADVDH
|
| Functional narrative |
Function: The interaction with Sm proteins inhibits their assembly on U RNA and interferes with snRNP biogenesis. Inhibits the binding of survival motor neuron protein (SMN) to Sm proteins. May participate in cellular volume control by activation of a swelling-induced chloride conductance pathway (By similarity).
SUBUNIT: Homooligomer. Component of the methylosome, a 20S complex containing SKB1. Interacts with Sm proteins. Interacts with LSM10, LSM11 and SNRPB (By similarity).
Subcellular Location: Cytoplasm (By similarity). Nucleus (By similarity).
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity).
SIMILARITY: Belongs to the pICln family.
CAUTION: Was originally thought to be a chloride channel.
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|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | N-terminal region | | Location: | 1 - 23 | | Length: | 23 | | Region sequence: |
MSFLKSFPPPGSAEGLRQQQPET | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
Molecular recognition effectors
| | Functional subclasses: | Phosphorylation
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM; H2O/D2O (90%/10%))
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:Furst, et al (2005), using both full length ICln and N-terminal fragment (aa M1-Q159, Rgn 1-17), determined the following:
PH domain structure: ICln N-terminal domain (aa M1-L133, Regions 1-16) exhibits the canonical structure of a plekstrin-homology (PH) domain. This consists of a sandwich of seven beta-strands topped with an alpha-helix and containing three major loops. In ICln, one side of sandwich contains Beta-strands 2, 3, 4 (Rgns 4, 6, 8), the other side contains Beta-strands 1, 5, 6, 7 (Rgns 2, 10, 12, 14).
Loops B5-B6 and B6-B7 (Rgns 11 and 13) are described as highly mobile.
Charge:The ICln N-terminal domain exhibits a strong overall negative electrostatic charge. Loop B6-B7 (Rgn 13) may be important for formation of current in lipid bilayers.
Pore region: The putative transmembrane sections forming the pore region are aa K30-A40 (Rgn 3, 4), encompassing Beta-strand 2; aa G49-R68 (Rgns 7 through 11), encompassing Beta-strands 4 and 5; aa H77-E88 (Rgns 12, 13), encompassing Beta-strand 6.
Acidic domains (full-length ICln): Three acidic regions are present that vary slightly by author: Furst, et al describe AD1 at E69-E105 (Rgn 13), AD2 at D136-E149 (Rgn 17), AD3 E213-H235 (Rgns 20-21); Schedlbauer et al describe AR1 at E69-E105 (Rgn 13), AR2 at D136-E153 (Rgn 17), AR3 E229-H235 (Rgn 21).
PTM sites (full-length ICln): Nine putative phosporylation sites and their targeting kinases are:
1) S2 [Rgn 1], PKGII;
2) T34 [Rgn 3], PKC/PKA/PKGI or II;
3) S45 [Rgn 6], PKC/PKA/PKGI or II;
4) S93 [Rgn 13], PKGII;
5) S115 [Rgn 15], PKC/PKGI or II;
6) S142 [Rgn 17], unknown kinase;
7) T167 [Rgn 18], CKI/II;
8) S173 [Rgn 19], CKI/II;
9) S208 [Rgn 20], PKC/PKGI or II.
See overall Comments section near end of record for more details about structure.
Putative phosporylation site and targeting kinase: S2, PKGII.
|
| Region 2 | | Type: | Ordered | | Name: | Beta-strand 1 | | Location: | 24 - 27 | | Length: | 4 | | Region sequence: |
EAVL | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
Electron transfer
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 3 | | Type: | Disordered | | Name: | Loop B1-B2 | | Location: | 28 - 34 | | Length: | 7 | | Region sequence: |
NGKGLGT | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
Phosphorylation
Electron transfer
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
Putative phosporylation site and targeting kinases: T34, PKC/PKA/PKGI or II.
|
| Region 4 | | Type: | Ordered | | Name: | Beta-strand 2 | | Location: | 35 - 40 | | Length: | 6 | | Region sequence: |
GTLYIA | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 5 | | Type: | Disordered | | Name: | Loop B2-B3 | | Location: | 41 - 43 | | Length: | 3 | | Region sequence: |
ESR | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 6 | | Type: | Ordered | | Name: | Beta-strand 3 | | Location: | 44 - 47 | | Length: | 4 | | Region sequence: |
LSWL | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Modification site
Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Phosphorylation
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
Putative phosporylation site and targeting kinases: S45, PKC/PKA/PKGI or II.
|
| Region 7 | | Type: | Disordered | | Name: | Loop B3-B4 | | Location: | 48 - 52 | | Length: | 5 | | Region sequence: |
DGSGL | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 8 | | Type: | Ordered | | Name: | Beta-strand 4 | | Location: | 53 - 55 | | Length: | 3 | | Region sequence: |
GFS | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 9 | | Type: | Disordered | | Name: | Loop B4-B5 | | Location: | 56 - 62 | | Length: | 7 | | Region sequence: |
LEYPTIS | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 10 | | Type: | Ordered | | Name: | Beta-strand 5 | | Location: | 63 - 65 | | Length: | 3 | | Region sequence: |
LHA | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 11 | | Type: | Disordered | | Name: | Loop B5-B6 | | Location: | 66 - 76 | | Length: | 11 | | Region sequence: |
VSRDLNAYPRE | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 12 | | Type: | Ordered | | Name: | Beta-strand 6 | | Location: | 77 - 83 | | Length: | 7 | | Region sequence: |
HLYVMVN | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 13 | | Type: | Disordered | | Name: | Loop B6-B7 | | Location: | 84 - 106 | | Length: | 23 | | Region sequence: |
AKFGEESKESVAEEEDSDDDVEP | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
Molecular recognition effectors
| | Functional subclasses: | Protein-lipid interaction
Phosphorylation
Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
Putative phosporylation site and targeting kinase: S93, PKGII.
Furst et al discuss the possibility that Loop B6-B7 is important for formation of current in lipid bilayers.
|
| Region 14 | | Type: | Ordered | | Name: | Beta-strand 7 | | Location: | 107 - 113 | | Length: | 7 | | Region sequence: |
IAEFRFV | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 15 | | Type: | Disordered | | Name: | Loop B7-A1 | | Location: | 114 - 118 | | Length: | 5 | | Region sequence: |
PSDKS | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Phosphorylation
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
Putative phosporylation site and targeting kinases: S115, PKC/PKGI or II.
|
| Region 16 | | Type: | Ordered | | Name: | Alpha-helix 1 | | Location: | 119 - 133 | | Length: | 15 | | Region sequence: |
ALEAMFTAMCECQAL | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Electron transfer
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
| Comments:See overall Comments section near end of record for more details about structure.
|
| Region 17 | | Type: | Disordered | | Name: | Loop A1-B8 | | Location: | 134 - 160 | | Length: | 27 | | Region sequence: |
HPDPEDEDSDDYDGEEYDVEAHEQGQG | | Modification type: | Monomeric
Native
| | PDB: | 1ZYI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
Molecular recognition effectors
| | Functional subclasses: | Phosphorylation
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 1-159) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
- Nuclear magnetic resonance (NMR) (298 K; ICln (FL or aa 159-235))
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
- Schedlbauer A, Gandini R, Kontaxis G, Paulmichl M, Furst J, Konrat R. "The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation." Cell. Physiol. Biochem.. 2011; 28(6): 1203-10. PubMed: 22179008
| Comments:Furst, et al (2005), using both full length ICln and N-terminal fragment (aa M1-Q159, Rgn 1-17), determined the following:
PH domain structure: ICln N-terminal domain (aa M1-L133, Regions 1-16) exhibits the canonical structure of a plekstrin-homology (PH) domain. This consists of a sandwich of seven beta-strands topped with an alpha-helix and containing three major loops. In ICln, one side of sandwich contains Beta-strands 2, 3, 4 (Rgns 4, 6, 8), the other side contains Beta-strands 1, 5, 6, 7 (Rgns 2, 10, 12, 14).
Loops B5-B6 and B6-B7 (Rgns 11 and 13) are described as highly mobile.
Charge:The ICln N-terminal domain exhibits a strong overall negative electrostatic charge. Loop B6-B7 (Rgn 13) may be important for formation of current in lipid bilayers.
Pore region: The putative transmembrane sections forming the pore region are aa K30-A40 (Rgn 3, 4), encompassing Beta-strand 2; aa G49-R68 (Rgns 7 through 11), encompassing Beta-strands 4 and 5; aa H77-E88 (Rgns 12, 13), encompassing Beta-strand 6.
Acidic domains (full-length ICln): Three acidic regions are present that vary slightly by author: Furst, et al describe AD1 at E69-E105 (Rgn 13), AD2 at D136-E149 (Rgn 17), AD3 E213-H235 (Rgns 20-21); Schedlbauer et al describe AR1 at E69-E105 (Rgn 13), AR2 at D136-E153 (Rgn 17), AR3 E229-H235 (Rgn 21).
PTM sites (full-length ICln): Nine putative phosporylation sites and their targeting kinases are:
1) S2 [Rgn 1], PKGII;
2) T34 [Rgn 3], PKC/PKA/PKGI or II;
3) S45 [Rgn 6], PKC/PKA/PKGI or II;
4) S93 [Rgn 13], PKGII;
5) S115 [Rgn 15], PKC/PKGI or II;
6) S142 [Rgn 17], unknown kinase;
7) T167 [Rgn 18], CKI/II;
8) S173 [Rgn 19], CKI/II;
9) S208 [Rgn 20], PKC/PKGI or II.
Schedlbauer et al (2011), using both full-length ICln and C-terminal fragment (aa Q159-H235, Rgns 18-22), determined the following:
Intrinsically Disordered Structure: The full C-terminal segment (aa H134-H235, Rgns 17-22) of ICln is intrinsically disordered, with regions of transient structure at aa D161-Y168 (Beta-strand 8, Rgn 18), E170-E187 (Alpha-helix 2, Rgn 19), E218-T223 (Beta-strand 9, Rgn 21).
Acidic domains: Three acidic regions are present that vary slightly by author: Furst, et al describe AD1 at E69-E105 (Rgn 13), AD2 at D136-E149 (Rgn 17), AD3 E213-H235 (Rgns 20-21); Schedlbauer et al describe AR1 at E69-E105 (Rgn 13), AR2 at D136-E153 (Rgn 17), AR3 E229-H235 (Rgn 21).
Conservation: The C-terminal domain is highly conserved in vertebrates and likely very involved in multiple protein-protein interactions.
Putative phosporylation site and targeting kinase: S142, unknown kinase.
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| Region 18 | | Type: | Disordered w/ Residual Structure | | Name: | Beta-strand 8 | | Location: | 161 - 168 | | Length: | 8 | | Region sequence: |
DIPTFYTY | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Modification site
Molecular recognition effectors
| | Functional subclasses: | Phosphorylation
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 159-235) 25 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
- Schedlbauer A, Gandini R, Kontaxis G, Paulmichl M, Furst J, Konrat R. "The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation." Cell. Physiol. Biochem.. 2011; 28(6): 1203-10. PubMed: 22179008
| Comments:See overall Comments section near end of record for more details about structure.
Putative phosporylation site and targeting kinases: T167, CKI/II.
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| Region 19 | | Type: | Disordered w/ Residual Structure | | Name: | Alpha-helix 2 | | Location: | 170 - 187 | | Length: | 18 | | Region sequence: |
EGLSHLTAEGQATLERLE | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Modification site
Molecular recognition effectors
| | Functional subclasses: | Phosphorylation
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 159-235) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- Schedlbauer A, Gandini R, Kontaxis G, Paulmichl M, Furst J, Konrat R. "The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation." Cell. Physiol. Biochem.. 2011; 28(6): 1203-10. PubMed: 22179008
| Comments:See overall Comments section near end of record for more details about structure.
Putative phosporylation site and targeting kinases: S173, CKI/II.
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| Region 20 | | Type: | Disordered | | Name: | Loop A2-B9 | | Location: | 188 - 216 | | Length: | 29 | | Region sequence: |
GMLSQSVSSQYNMAGVRTEDSTRDYEDGM | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
Molecular recognition effectors
| | Functional subclasses: | Phosphorylation
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 159-235) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- Schedlbauer A, Gandini R, Kontaxis G, Paulmichl M, Furst J, Konrat R. "The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation." Cell. Physiol. Biochem.. 2011; 28(6): 1203-10. PubMed: 22179008
| Comments:See overall Comments section near end of record for more details about structure.
Putative phosporylation site and targeting kinases: S208, PKC/PKGI or II.
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| Region 21 | | Type: | Disordered w/ Residual Structure | | Name: | Beta-strand 9 | | Location: | 217 - 223 | | Length: | 7 | | Region sequence: |
EVDTTPT | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 159-235) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- Schedlbauer A, Gandini R, Kontaxis G, Paulmichl M, Furst J, Konrat R. "The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation." Cell. Physiol. Biochem.. 2011; 28(6): 1203-10. PubMed: 22179008
| Comments:See overall Comments section near end of record for more details about structure.
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| Region 22 | | Type: | Disordered | | Name: | C-terminal region | | Location: | 224 - 235 | | Length: | 12 | | Region sequence: |
VAGQFEDADVDH | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; H2O/D2O (90%/10%); ICln (FL or aa 159-235) 1 mM; NaCl 150 mM; potassium phosphate buffer 25 mM)
| References:
- Schedlbauer A, Gandini R, Kontaxis G, Paulmichl M, Furst J, Konrat R. "The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation." Cell. Physiol. Biochem.. 2011; 28(6): 1203-10. PubMed: 22179008
| Comments:See overall Comments section near end of record for more details about structure.
|
| References |
- 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. "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4." J. Biol. Chem.. 2005; 280(35): 31276-82. PubMed: 15905169
- Schedlbauer A, Gandini R, Kontaxis G, Paulmichl M, Furst J, Konrat R. "The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation." Cell. Physiol. Biochem.. 2011; 28(6): 1203-10. PubMed: 22179008
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| Comments |
Furst, et al (2005), using both full length ICln and N-terminal fragment (aa M1-Q159, Rgn 1-17), determined the following:
PH domain structure: ICln N-terminal domain (aa M1-L133, Regions 1-16) exhibits the canonical structure of a plekstrin-homology (PH) domain. This consists of a sandwich of seven beta-strands topped with an alpha-helix and containing three major loops. In ICln, one side of sandwich contains Beta-strands 2, 3, 4 (Rgns 4, 6, 8), the other side contains Beta-strands 1, 5, 6, 7 (Rgns 2, 10, 12, 14).
Loops B5-B6 and B6-B7 (Rgns 11 and 13) are described as highly mobile.
Charge:The ICln N-terminal domain exhibits a strong overall negative electrostatic charge. Loop B6-B7 (Rgn 13) may be important for formation of current in lipid bilayers.
Pore region: The putative transmembrane sections forming the pore region are aa K30-A40 (Rgn 3, 4), encompassing Beta-strand 2; aa G49-R68 (Rgns 7 through 11), encompassing Beta-strands 4 and 5; aa H77-E88 (Rgns 12, 13), encompassing Beta-strand 6.
Acidic domains (full-length ICln): Three acidic regions are present that vary slightly by author: Furst, et al describe AD1 at E69-E105 (Rgn 13), AD2 at D136-E149 (Rgn 17), AD3 E213-H235 (Rgns 20-21); Schedlbauer et al describe AR1 at E69-E105 (Rgn 13), AR2 at D136-E153 (Rgn 17), AR3 E229-H235 (Rgn 21).
PTM sites (full-length ICln): Nine putative phosporylation sites and their targeting kinases are:
1) S2 [Rgn 1], PKGII;
2) T34 [Rgn 3], PKC/PKA/PKGI or II;
3) S45 [Rgn 6], PKC/PKA/PKGI or II;
4) S93 [Rgn 13], PKGII;
5) S115 [Rgn 15], PKC/PKGI or II;
6) S142 [Rgn 17], unknown kinase;
7) T167 [Rgn 18], CKI/II;
8) S173 [Rgn 19], CKI/II;
9) S208 [Rgn 20], PKC/PKGI or II.
Schedlbauer et al (2011), using both full-length ICln and C-terminal fragment (aa Q159-H235, Rgns 18-22), determined the following:
Intrinsically Disordered Structure: The full C-terminal segment (aa H134-H235, Rgns 17-22) of ICln is intrinsically disordered, with regions of transient structure at aa D161-Y168 (Beta-strand 8, Rgn 18), E170-E187 (Alpha-helix 2, Rgn 19), E218-T223 (Beta-strand 9, Rgn 21).
Acidic domains: Three acidic regions are present that vary slightly by author: Furst, et al describe AD1 at E69-E105 (Rgn 13), AD2 at D136-E149 (Rgn 17), AD3 E213-H235 (Rgns 20-21); Schedlbauer et al describe AR1 at E69-E105 (Rgn 13), AR2 at D136-E153 (Rgn 17), AR3 E229-H235 (Rgn 21).
Conservation: The C-terminal domain is highly conserved in vertebrates and likely very involved in multiple protein-protein interactions.
Verification Request sent 2-21-2012 (PMID:15905169)
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