General information | DisProt: | DP00565 | Name: | Calcineurin subunit B type 1 | Synonym(s): | CANB1_HUMAN
Calcineurin B
CaNB
Protein phosphatase 2B regulatory subunit 1
Protein phosphatase 3 regulatory subunit B alpha isoform 1
PPP3R1
| First appeared in release: | Release 6.01 (10/15/2012) | UniProt: | P63098 | UniGene: | Hs.280604 | SwissProt: | CANB1_HUMAN | TrEMBL: | | NCBI (GI): | 52000904 | Source organism: | Homo sapiens (Human) | Sequence length: | 170 | Percent disordered: | 31% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MGNEASYPLE MCSHFDADEI KRLGKRFKKL DLDNSGSLSV EEFMSLPELQ QNPLVQRVID - 60 IFDTDGNGEV DFKEFIEGVS QFSVKGDKEQ KLRFAFRIYD MDKDGYISNG ELFQVLKMMV - 120 GNNLKDTQLQ QIVDKTIINA DKDGDGRISF EEFCAVVGGL DIHKKMVVDV
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Functional narrative |
Function: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
Subunit structure: Composed of a catalytic subunit (A) [DP00092] and a regulatory subunit (B) [DP00565].
Miscellaneous: This protein has four functional calcium-binding sites.
Sequence similarities: Belongs to the calcineurin regulatory subunit family. Contains 4 EF-hand domains.
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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.
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Region 1 | Type: | Disordered | Name: | N-terminal region | Location: | 1 - 16 | Length: | 16 | Region sequence: |
MGNEASYPLEMCSHFD | Modification type: | Complex
Native
| PDB: | 1AUI:B | Structural/functional type: | Function arises from the disordered state | Functional classes: | Modification site
| Functional subclasses: | Fatty acylation (myristolation and palmitoylation)
| Detection methods:
- Nuclear magnetic resonance (NMR) (310 K; pH: 4.95; Calcineurin B 2.3 mM; CHAPS 25 mM; Ca2+ 20 mM; 95%H2O/5%D2O)
- Hydrogen-deuterium exchange (303 K; pH: 7.8; CaCl2 4 mM; Calcineurin B 0.4 mM; CHAPS 5 mM; D2O 0.7 mL; NaN3 0.01 %)
- Nuclear magnetic resonance (NMR) (320 K; pH: 5.9; CnB protein/CnA peptide(P2465) 1.5 mM; KCl 200 mM)
- X-ray crystallography (pH: 7.5; CaCl2 0.1 M; CaN A and B subunits (PDB 1AUI); DTT 1 mM; PEG 6000 8 %; TES 0.1 M)
- High relative B-factor
- Sensitivity to proteolysis
| References:
- Anglister J, Grzesiek S, Wang AC, Ren H, Klee CB, Bax A. "1H, 13C, 15N nuclear magnetic resonance backbone assignments and secondary structure of human calcineurin B." Biochemistry. 1994; 33(12): 3540-7. PubMed: 8142351
- Anglister J, Ren H, Klee CB, Bax A. "NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide." FEBS Lett.. 1995; 375(1-2): 108-12. PubMed: 7498455
- Jin L, Harrison SC. "Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin." Proc Natl Acad Sci U S A. 2002; 99(21): 13522-6. PubMed: 12357034
- Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al. "Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex." Nature. 1995; 378(6557): 641-4. PubMed: 8524402
- Li H, Zhang L, Rao A, Harrison SC, Hogan PG. "Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction." J. Mol. Biol.. 2007; 369(5): 1296-306. PubMed: 17498738
| Comments:
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Region 2 | Type: | Disordered | Name: | Loop 2-3 | Location: | 44 - 53 | Length: | 10 | Region sequence: |
MSLPELQQNP | Modification type: | Complex
Native
| PDB: | | Structural/functional type: | Function arises from the disordered state | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- Nuclear magnetic resonance (NMR) (320 K; pH: 5.9; CnB protein/CnA peptide(P2465) 1.5 mM; KCl 200 mM)
| References:
- Anglister J, Ren H, Klee CB, Bax A. "NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide." FEBS Lett.. 1995; 375(1-2): 108-12. PubMed: 7498455
| Comments:
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Region 3 | Type: | Disordered | Name: | domain linker (Loop 4-5) | Location: | 82 - 87 | Length: | 6 | Region sequence: |
FSVKGD | Modification type: | Complex
Native
| PDB: | 2P6B:B | Structural/functional type: | Function arises from the disordered state | Functional classes: | Molecular recognition effectors
Molecular assembly
| Functional subclasses: | Flexible linkers/spacers
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (310 K; pH: 4.95; 95%H2O/5%D2O; Ca2+ 20 mM; Calcineurin B 2.3 mM; CHAPS 25 mM)
- Hydrogen-deuterium exchange (303 K; pH: 7.8; CaCl2 4 mM; Calcineurin B 0.4 mM; CHAPS 5 mM; D2O 0.7 mL; NaN3 0.01 %)
- Nuclear magnetic resonance (NMR) (320 K; pH: 5.9; CnB protein/CnA peptide(P2465) 1.5 mM; KCl 200 mM)
- X-ray crystallography (295 K; pH: 8; CaCl2 0.1 M; CNA (1-380)-CNB (16-170)-PVIVIT complex (PDB 2P6B) 7 mg/mL; DTT 0.001 M; PEG 4000 12 %; TES 0.1 M)
| References:
- Anglister J, Grzesiek S, Wang AC, Ren H, Klee CB, Bax A. "1H, 13C, 15N nuclear magnetic resonance backbone assignments and secondary structure of human calcineurin B." Biochemistry. 1994; 33(12): 3540-7. PubMed: 8142351
- Anglister J, Ren H, Klee CB, Bax A. "NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide." FEBS Lett.. 1995; 375(1-2): 108-12. PubMed: 7498455
- Li H, Zhang L, Rao A, Harrison SC, Hogan PG. "Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction." J. Mol. Biol.. 2007; 369(5): 1296-306. PubMed: 17498738
| Comments:
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Region 4 | Type: | Disordered | Name: | Loop 6-7 (Loop F-G) | Location: | 120 - 128 | Length: | 9 | Region sequence: |
VGNNLKDTQ | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular assembly
| Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- Nuclear magnetic resonance (NMR) (310 K; pH: 4.95; 95%H2O/5%D2O; Ca2+ 20 mM; Calcineurin B 2.3 mM; CHAPS 25 mM)
- Hydrogen-deuterium exchange (303 K; pH: 7.8; CaCl2 4 mM; Calcineurin B 0.4 mM; CHAPS 5 mM; D2O 0.7 mL; NaN3 0.01 %)
| References:
- Anglister J, Grzesiek S, Wang AC, Ren H, Klee CB, Bax A. "1H, 13C, 15N nuclear magnetic resonance backbone assignments and secondary structure of human calcineurin B." Biochemistry. 1994; 33(12): 3540-7. PubMed: 8142351
| Comments:Anglister et al (1994) describe fast H/D exchange for this region (loop V120-K125 plus the first 3 residues of helix 7, D126-Q128), and this region is visible in crystal structures, suggesting a disorder-to-order transition.
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Region 5 | Type: | Disordered | Name: | C-terminal region | Location: | 159 - 170 | Length: | 12 | Region sequence: |
GLDIHKKMVVDV | Modification type: | Complex
Native
| PDB: | 1AUI:B, 1MF8:B, 2P6B:B | Structural/functional type: | Function arises from the disordered state | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (303 K; pH: 4.95; 95%H2O/5%D2O; Ca2+ 20 mM; Calcineurin B 2.3 mM; CHAPS 25 mM)
- Hydrogen-deuterium exchange (303 K; pH: 7.8; CaCl2 4 mM; Calcineurin B 0.4 mM; CHAPS 5 mM; D2O 0.7 mL; NaN3 0.01 %)
- Nuclear magnetic resonance (NMR) (320 K; pH: 5.9; CnB protein/CnA peptide(P2465) 1.5 mM; KCl 200 mM)
- X-ray crystallography (pH: 7.5; CaCl2 0.1 M; CaN A and B subunits (PDB 1AUI); DTT 1 mM; PEG 6000 8 %; TES 0.1 M)
- X-ray crystallography (292 K; pH: 4.6; Cyp/CsA/Cn complex (PDB 1MF8); glycerol 15 %; potassoium phosphate 5 mM; sodium citrate 75 mM; Tris 5 mM)
- X-ray crystallography (295 K; pH: 8; CaCl2 0.1 M; CNA (1-380)-CNB (16-170)-PVIVIT complex (PDB 2P6B) 7 mg/mL; DTT 0.001 M; PEG 4000 12 %; TES 0.1 M)
- High relative B-factor
- Sensitivity to proteolysis
| References:
- Anglister J, Grzesiek S, Wang AC, Ren H, Klee CB, Bax A. "1H, 13C, 15N nuclear magnetic resonance backbone assignments and secondary structure of human calcineurin B." Biochemistry. 1994; 33(12): 3540-7. PubMed: 8142351
- Anglister J, Ren H, Klee CB, Bax A. "NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide." FEBS Lett.. 1995; 375(1-2): 108-12. PubMed: 7498455
- Jin L, Harrison SC. "Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin." Proc Natl Acad Sci U S A. 2002; 99(21): 13522-6. PubMed: 12357034
- Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al. "Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex." Nature. 1995; 378(6557): 641-4. PubMed: 8524402
- Li H, Zhang L, Rao A, Harrison SC, Hogan PG. "Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction." J. Mol. Biol.. 2007; 369(5): 1296-306. PubMed: 17498738
| Comments:
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References |
- Manalan AS, Klee CB. "Activation of calcineurin by limited proteolysis." Proc. Natl. Acad. Sci. U.S.A.. 1983; 80(14): 4291-5. PubMed: 6576338
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Comments |
The entry DP00092_A001 has been replaced by DP00565. The protein Calcineurin subunit B type 1 is not an alternatively-spliced version of DP00092:Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform, and therefore receives its own DisProt record, DP00565. The two proteins are interacting subunits of calcineurin.
Manalan and Klee (1983) conducted proteolysis experiments on bovine calcineurin.
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