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Conserved domains on  [gi|81882221|sp|P97287.3|MCL1_MOUSE]
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RecName: Full=Induced myeloid leukemia cell differentiation protein Mcl-1 homolog; AltName: Full=Bcl-2-related protein EAT/mcl1

Protein Classification

Bcl-2_like domain-containing protein (domain architecture ID 10160139)

Bcl-2_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Bcl-2_like cd06845
Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This ...
156-299 5.63e-42

Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This alignment model spans what have been described as Bcl-2 homology regions BH1, BH2, BH3, and BH4. Many members of this family have an additional C-terminal transmembrane segment. Some homologous proteins, which are not included in this model, may miss either the BH4 (Bax, Bak) or the BH2 (Bcl-X(S)) region, and some appear to only share the BH3 region (Bik, Bim, Bad, Bid, Egl-1). This family is involved in the regulation of the outer mitochondrial membrane's permeability and in promoting or preventing the release of apoptogenic factors, which in turn may trigger apoptosis by activating caspases. Bcl-2 and the closely related Bcl-X(L) are anti-apoptotic key regulators of programmed cell death. They are assumed to function via heterodimeric protein-protein interactions, binding pro-apoptotic proteins such as Bad (BCL2-antagonist of cell death), Bid, and Bim, by specifically interacting with their BH3 regions. Interfering with this heterodimeric interaction via small-molecule inhibitors may prove effective in targeting various cancers. This family also includes the Caenorhabditis elegans Bcl-2 homolog CED-9, which binds to CED-4, the C. Elegans homolog of mammalian Apaf-1. Apaf-1, however, does not seem to be inhibited by Bcl-2 directly.


:

Pssm-ID: 132900  Cd Length: 144  Bit Score: 145.17  E-value: 5.63e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221 156 YRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVF 235
Cdd:cd06845   1 DEITRRLARDYLRYRLGEPETPNSPLPSGSPPSEVAETLRRVGDELEEKHRRLFENMCRQLNISPDNAYEVFQEVARELF 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81882221 236 KDGVTNWGRIVTLISFGAFVAKHLKSVNQESFIEPLAETITDVLVRTKRDWLVKQRGWDGFVEF 299
Cdd:cd06845  81 EDGGINWGRIVALFAFGGRLAVKCVEQGLPELVRSIAEWTSDFLEENLADWIQENGGWDGFVEF 144
 
Name Accession Description Interval E-value
Bcl-2_like cd06845
Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This ...
156-299 5.63e-42

Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This alignment model spans what have been described as Bcl-2 homology regions BH1, BH2, BH3, and BH4. Many members of this family have an additional C-terminal transmembrane segment. Some homologous proteins, which are not included in this model, may miss either the BH4 (Bax, Bak) or the BH2 (Bcl-X(S)) region, and some appear to only share the BH3 region (Bik, Bim, Bad, Bid, Egl-1). This family is involved in the regulation of the outer mitochondrial membrane's permeability and in promoting or preventing the release of apoptogenic factors, which in turn may trigger apoptosis by activating caspases. Bcl-2 and the closely related Bcl-X(L) are anti-apoptotic key regulators of programmed cell death. They are assumed to function via heterodimeric protein-protein interactions, binding pro-apoptotic proteins such as Bad (BCL2-antagonist of cell death), Bid, and Bim, by specifically interacting with their BH3 regions. Interfering with this heterodimeric interaction via small-molecule inhibitors may prove effective in targeting various cancers. This family also includes the Caenorhabditis elegans Bcl-2 homolog CED-9, which binds to CED-4, the C. Elegans homolog of mammalian Apaf-1. Apaf-1, however, does not seem to be inhibited by Bcl-2 directly.


Pssm-ID: 132900  Cd Length: 144  Bit Score: 145.17  E-value: 5.63e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221 156 YRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVF 235
Cdd:cd06845   1 DEITRRLARDYLRYRLGEPETPNSPLPSGSPPSEVAETLRRVGDELEEKHRRLFENMCRQLNISPDNAYEVFQEVARELF 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81882221 236 KDGVTNWGRIVTLISFGAFVAKHLKSVNQESFIEPLAETITDVLVRTKRDWLVKQRGWDGFVEF 299
Cdd:cd06845  81 EDGGINWGRIVALFAFGGRLAVKCVEQGLPELVRSIAEWTSDFLEENLADWIQENGGWDGFVEF 144
BCL smart00337
BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not ...
194-293 3.99e-34

BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not BH4(one helix only)). Involved in apoptosis regulation


Pssm-ID: 214626  Cd Length: 100  Bit Score: 123.20  E-value: 3.99e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221    194 LRRVGDGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVNQESFIEPLAE 273
Cdd:smart00337   1 LRRVGDELNKRYERAFSSFSAQLHVTPGTAIELFGEVATELFSDGNINWGRVVALLSFGGALAVKLVQKEDPDLVSRLAS 80
                           90       100
                   ....*....|....*....|
gi 81882221    274 TITDVLVRTKRDWLVKQRGW 293
Cdd:smart00337  81 WLSEFLRETLRSWIRENGGW 100
Bcl-2 pfam00452
Apoptosis regulator proteins, Bcl-2 family;
199-293 9.35e-30

Apoptosis regulator proteins, Bcl-2 family;


Pssm-ID: 306867  Cd Length: 95  Bit Score: 111.21  E-value: 9.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221   199 DGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVNQESFIEPLAETITDV 278
Cdd:pfam00452   1 DELERKYPEEFNRMLQQLLLTPDTAYELFNEVADELFSDGVINWGRVVALFAFAGALAVKCVEQGMPELVRSLAEWLVDY 80
                          90
                  ....*....|....*
gi 81882221   279 LVRTKRDWLVKQRGW 293
Cdd:pfam00452  81 LEERLADWIIQQGGW 95
bcl-2 TIGR00865
apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the ...
191-331 8.72e-18

apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the apoptosis regulator, Bcl-X, and its homologues. Bcl-X is a dominant regulator of programmed cell death in mammalian cells. The long form (Bcl-X(L)) displays cell death repressor activity, but the short isoform (Bcl-X(S)) and the b-isoform (Bcl-Xb) promote cell death. Bcl-X(L), Bcl-X(S) and Bcl-Xb are three isoforms derived by alternative RNA splicing. Bcl-X(S) forms heterodimers with Bcl-2. Homologues of Bcl-X include the Bax (rat; 192 aas; spQ63690) and Bak (mouse; 208 aas; spO08734) proteins which also influence apoptosis. Using isolated mitochondria, recombinant Bax and Bak have been shown to induce Dy loss, swelling and cytochrome c release. All of these changes are dependent on Ca2+ and are prevented by cyclosporin A and bongkrekic acid, both of which are known to close permeability transition pores (megachannels). Coimmimoprecipitation studies revealed that Bax and Bak interact with VDAC to form permeability transition pores. Thus, even though they can form channels in artificial membranes at acidic pH, proapoptotic Bcl-2 family proteins (including Bax and Bak) probably induce the mitochondrial permeability transition and cytochrome c release by interacting with permeability transition pores, the most important component for pore fomation of which is VDAC. [Regulatory functions, Other]


Pssm-ID: 273308  Cd Length: 213  Bit Score: 80.63  E-value: 8.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221   191 LETLRRVGDGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVtNWGRIVTLISFGAFVAkhLKSVNQEsfIEP 270
Cdd:TIGR00865  68 HQALRRAGDEFERRYRRAFSDMTSQLHITPFTARQSFFQVAAELFRDGV-NWGRIVAFFSFGGALC--VESVNKE--MSE 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221   271 LAETI----TDVLVRTKRDWLVKQRGWDGFVEFF-----HVQDLEGGIRNVLLAFAGVAGVGAGLAYLIR 331
Cdd:TIGR00865 143 LVSRIagwmTEYLNEHLHPWIQENGGWDGFVELYgnnaaQLFDFSWESFNTLLTAGLVTAVLTLGAYMGR 212
 
Name Accession Description Interval E-value
Bcl-2_like cd06845
Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This ...
156-299 5.63e-42

Apoptosis regulator proteins of the Bcl-2 family, named after B-cell lymphoma 2. This alignment model spans what have been described as Bcl-2 homology regions BH1, BH2, BH3, and BH4. Many members of this family have an additional C-terminal transmembrane segment. Some homologous proteins, which are not included in this model, may miss either the BH4 (Bax, Bak) or the BH2 (Bcl-X(S)) region, and some appear to only share the BH3 region (Bik, Bim, Bad, Bid, Egl-1). This family is involved in the regulation of the outer mitochondrial membrane's permeability and in promoting or preventing the release of apoptogenic factors, which in turn may trigger apoptosis by activating caspases. Bcl-2 and the closely related Bcl-X(L) are anti-apoptotic key regulators of programmed cell death. They are assumed to function via heterodimeric protein-protein interactions, binding pro-apoptotic proteins such as Bad (BCL2-antagonist of cell death), Bid, and Bim, by specifically interacting with their BH3 regions. Interfering with this heterodimeric interaction via small-molecule inhibitors may prove effective in targeting various cancers. This family also includes the Caenorhabditis elegans Bcl-2 homolog CED-9, which binds to CED-4, the C. Elegans homolog of mammalian Apaf-1. Apaf-1, however, does not seem to be inhibited by Bcl-2 directly.


Pssm-ID: 132900  Cd Length: 144  Bit Score: 145.17  E-value: 5.63e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221 156 YRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVF 235
Cdd:cd06845   1 DEITRRLARDYLRYRLGEPETPNSPLPSGSPPSEVAETLRRVGDELEEKHRRLFENMCRQLNISPDNAYEVFQEVARELF 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81882221 236 KDGVTNWGRIVTLISFGAFVAKHLKSVNQESFIEPLAETITDVLVRTKRDWLVKQRGWDGFVEF 299
Cdd:cd06845  81 EDGGINWGRIVALFAFGGRLAVKCVEQGLPELVRSIAEWTSDFLEENLADWIQENGGWDGFVEF 144
BCL smart00337
BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not ...
194-293 3.99e-34

BCL (B-Cell lymphoma); contains BH1, BH2 regions; (BH1, BH2, (BH3 (one helix only)) and not BH4(one helix only)). Involved in apoptosis regulation


Pssm-ID: 214626  Cd Length: 100  Bit Score: 123.20  E-value: 3.99e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221    194 LRRVGDGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVNQESFIEPLAE 273
Cdd:smart00337   1 LRRVGDELNKRYERAFSSFSAQLHVTPGTAIELFGEVATELFSDGNINWGRVVALLSFGGALAVKLVQKEDPDLVSRLAS 80
                           90       100
                   ....*....|....*....|
gi 81882221    274 TITDVLVRTKRDWLVKQRGW 293
Cdd:smart00337  81 WLSEFLRETLRSWIRENGGW 100
Bcl-2 pfam00452
Apoptosis regulator proteins, Bcl-2 family;
199-293 9.35e-30

Apoptosis regulator proteins, Bcl-2 family;


Pssm-ID: 306867  Cd Length: 95  Bit Score: 111.21  E-value: 9.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221   199 DGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVNQESFIEPLAETITDV 278
Cdd:pfam00452   1 DELERKYPEEFNRMLQQLLLTPDTAYELFNEVADELFSDGVINWGRVVALFAFAGALAVKCVEQGMPELVRSLAEWLVDY 80
                          90
                  ....*....|....*
gi 81882221   279 LVRTKRDWLVKQRGW 293
Cdd:pfam00452  81 LEERLADWIIQQGGW 95
bcl-2 TIGR00865
apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the ...
191-331 8.72e-18

apoptosis regulator; The Bcl-2 (Bcl-2) Family (TC 1.A.21) The Bcl-2 family consists of the apoptosis regulator, Bcl-X, and its homologues. Bcl-X is a dominant regulator of programmed cell death in mammalian cells. The long form (Bcl-X(L)) displays cell death repressor activity, but the short isoform (Bcl-X(S)) and the b-isoform (Bcl-Xb) promote cell death. Bcl-X(L), Bcl-X(S) and Bcl-Xb are three isoforms derived by alternative RNA splicing. Bcl-X(S) forms heterodimers with Bcl-2. Homologues of Bcl-X include the Bax (rat; 192 aas; spQ63690) and Bak (mouse; 208 aas; spO08734) proteins which also influence apoptosis. Using isolated mitochondria, recombinant Bax and Bak have been shown to induce Dy loss, swelling and cytochrome c release. All of these changes are dependent on Ca2+ and are prevented by cyclosporin A and bongkrekic acid, both of which are known to close permeability transition pores (megachannels). Coimmimoprecipitation studies revealed that Bax and Bak interact with VDAC to form permeability transition pores. Thus, even though they can form channels in artificial membranes at acidic pH, proapoptotic Bcl-2 family proteins (including Bax and Bak) probably induce the mitochondrial permeability transition and cytochrome c release by interacting with permeability transition pores, the most important component for pore fomation of which is VDAC. [Regulatory functions, Other]


Pssm-ID: 273308  Cd Length: 213  Bit Score: 80.63  E-value: 8.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221   191 LETLRRVGDGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVtNWGRIVTLISFGAFVAkhLKSVNQEsfIEP 270
Cdd:TIGR00865  68 HQALRRAGDEFERRYRRAFSDMTSQLHITPFTARQSFFQVAAELFRDGV-NWGRIVAFFSFGGALC--VESVNKE--MSE 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81882221   271 LAETI----TDVLVRTKRDWLVKQRGWDGFVEFF-----HVQDLEGGIRNVLLAFAGVAGVGAGLAYLIR 331
Cdd:TIGR00865 143 LVSRIagwmTEYLNEHLHPWIQENGGWDGFVELYgnnaaQLFDFSWESFNTLLTAGLVTAVLTLGAYMGR 212
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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