| General information | | DisProt: | DP00449 | | Name: | Bcl-2-like protein 1 [Isoform Bcl-X(L)] | | Synonym(s): | B2CL1_RAT
Bcl2-L-1
Apoptosis regulator Bcl-X
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P53563-1 | | UniGene: | Rn.10323 | | SwissProt: | B2CL1_RAT | | TrEMBL: | | | NCBI (GI): | 2506218 | | Source organism: | Rattus norvegicus (Rat) | | Sequence length: | 233 | | Percent disordered: | 24% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEPERETPSA INGNPSWHLA - 60
DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY - 120
QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP - 180
WIQENGGWDT FVDLYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK
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| Functional narrative |
Potent inhibitor of cell death. Isoform Bcl-X(L) anti-apoptotic activity is inhibited by association with SIVA isoform 1. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channnel (VDAC) by binding to it and preventing the release of the caspase activator, cytochrome c, from the mitochondrial membrane. The Bcl-X(S) and Bcl-X(beta) isoforms promote apoptosis.
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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: | | | Location: | 31 - 80 | | Length: | 50 | | Region sequence: |
EENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREV | | Modification type: | Fragment
Isoform
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Modification site
| | Functional subclasses: | Autoregulatory
| Detection methods:
- X-ray crystallography (293 K; pH: 5.6; dithiothreitol 1 mM; glycerol (v/v) 5 %; MES 50 mM; Na2SO4 0.7 M; NaCl 100 mM)
| References:
- Aritomi M, Kunishima N, Inohara N, Ishibashi Y, Ohta S, Morikawa K. "Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family." J Biol Chem. 1997; 272(44): 27886-92. PubMed: 9346936
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | Loop | | Location: | 101 - 105 | | Length: | 5 | | Region sequence: |
YRRAF | | Modification type: | Fragment
Isoform
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography (293 K; pH: 5.6; dithiothreitol 1 mM; glycerol 5 %v/v; MES 50 mM; Na2SO4 0.7 M; NaCl 100 mM)
| References:
- Aritomi M, Kunishima N, Inohara N, Ishibashi Y, Ohta S, Morikawa K. "Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family." J Biol Chem. 1997; 272(44): 27886-92. PubMed: 9346936
| Comments:
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| References |
- Shiraiwa N, Inohara N, Okada S, Yuzaki M, Shoji S, Ohta S. "An additional form of rat Bcl-x, Bcl-xbeta, generated by an unspliced RNA, promotes apoptosis in promyeloid cells." J Biol Chem. 1996; 271(22): 13258-65. PubMed: 8662675
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