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Conserved domains on  [gi|6755965|ref|NP_035825|]
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voltage-dependent anion-selective channel protein 2 [Mus musculus]

Protein Classification

porin( domain architecture ID 10163986)

porin forms an aqueous channel for the diffusion of small hydrophilic molecules across the outer membrane, similar to mammalian voltage-dependent anion-selective channel proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
16-294 2.19e-134

Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent anion channel (VDAC) regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane, which is highly permeable to small molecules. VDAC is the most abundant protein in the outer membrane, and membrane potentials can toggle VDAC between open or high-conducting and closed or low-conducting forms. VDAC binds to and is regulated in part by hexokinase, an interaction that renders mitochondria less susceptible to pro-apoptotic signals, most likely by intefering with VDAC's capability to respond to Bcl-2 family proteins. While VDAC appears to play a key role in mitochondrially induced cell death, a proposed involvement in forming the mitochondrial permeability transition pore, which is characteristic for damaged mitochondria and apoptosis, has been challenged by more recent studies.


:

Pssm-ID: 132767 [Multi-domain]  Cd Length: 276  Bit Score: 381.56  E-value: 2.19e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965   16 PPPYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVSGTLETKYKWCeyGLTFTEKWNTDNTLGT 95
Cdd:cd07306   1 PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIK--GLTLTQKWNTDNVLLT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965   96 EIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSAYKRECINLGCDVDFDFaGPAIHGSAVFGYEGWLAGYQMTFDSAKSK 175
Cdd:cd07306  79 EITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLNK-GPLVGASAVLGYKGFLLGAEVVYDTAKSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965  176 LTRSNFAVGYRTGDFQLHTNVNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLI 255
Cdd:cd07306 158 FTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNETTFAVGGQYALDPDALVKAKVNNDGQL 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6755965  256 GVGYTQTLRPGVKLTLSALVDGKSFNAGGHKLGLALELE 294
Cdd:cd07306 238 GLSYQHKLRPGVTLTLSAGFDAKNLNQGGHKFGLSLSLK 276
 
Name Accession Description Interval E-value
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
16-294 2.19e-134

Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent anion channel (VDAC) regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane, which is highly permeable to small molecules. VDAC is the most abundant protein in the outer membrane, and membrane potentials can toggle VDAC between open or high-conducting and closed or low-conducting forms. VDAC binds to and is regulated in part by hexokinase, an interaction that renders mitochondria less susceptible to pro-apoptotic signals, most likely by intefering with VDAC's capability to respond to Bcl-2 family proteins. While VDAC appears to play a key role in mitochondrially induced cell death, a proposed involvement in forming the mitochondrial permeability transition pore, which is characteristic for damaged mitochondria and apoptosis, has been challenged by more recent studies.


Pssm-ID: 132767 [Multi-domain]  Cd Length: 276  Bit Score: 381.56  E-value: 2.19e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965   16 PPPYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVSGTLETKYKWCeyGLTFTEKWNTDNTLGT 95
Cdd:cd07306   1 PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIK--GLTLTQKWNTDNVLLT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965   96 EIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSAYKRECINLGCDVDFDFaGPAIHGSAVFGYEGWLAGYQMTFDSAKSK 175
Cdd:cd07306  79 EITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLNK-GPLVGASAVLGYKGFLLGAEVVYDTAKSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965  176 LTRSNFAVGYRTGDFQLHTNVNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLI 255
Cdd:cd07306 158 FTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNETTFAVGGQYALDPDALVKAKVNNDGQL 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6755965  256 GVGYTQTLRPGVKLTLSALVDGKSFNAGGHKLGLALELE 294
Cdd:cd07306 238 GLSYQHKLRPGVTLTLSAGFDAKNLNQGGHKFGLSLSLK 276
Porin_3 pfam01459
Eukaryotic porin;
15-288 1.01e-110

Eukaryotic porin;


Pssm-ID: 460220 [Multi-domain]  Cd Length: 269  Bit Score: 321.08  E-value: 1.01e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965     15 IPPPYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVSGTLETKYKWceYGLTFTEKWNTDNTLG 94
Cdd:pfam01459   1 NPGTYEDIGKEAKDLLNKDYHFDGAKLDVTTKSGLGVAFQVSGSFSLGSGLSSGDFEAKYKD--KGLTLTLKGDTDNDLS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965     95 TEIAIEDQICQGLKLTFDTTFSPNtgKKSGKIKSAYKRECINLGCDVDFdFAGPAIHGSAVFGYEGWLAGYQMTFDSAKS 174
Cdd:pfam01459  79 TTATVNEQLTPGLKTKLSTQFVPG--KKSGKLELDYKGDDFTASLKVGL-LAGPVVVGSYLQGVTGLALGAEASYDTASG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965    175 KLTRSNFAVGYRTGDFQLHTN-VNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSS 253
Cdd:pfam01459 156 KLTKYNAALGYTARDYIASLTlVNNGGVLTASYYHKVSEKLEVGAELTLNFSSNENTVTIGYKYDLDKSTTVKAKVNSNG 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 6755965    254 LIGVGYTQTLRPGVKLTLSALVDGKSFNaGGHKLG 288
Cdd:pfam01459 236 KVGLLYEQKLRPGVTLTLSAEVDHKKLN-GAHKFG 269
 
Name Accession Description Interval E-value
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
16-294 2.19e-134

Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent anion channel (VDAC) regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane, which is highly permeable to small molecules. VDAC is the most abundant protein in the outer membrane, and membrane potentials can toggle VDAC between open or high-conducting and closed or low-conducting forms. VDAC binds to and is regulated in part by hexokinase, an interaction that renders mitochondria less susceptible to pro-apoptotic signals, most likely by intefering with VDAC's capability to respond to Bcl-2 family proteins. While VDAC appears to play a key role in mitochondrially induced cell death, a proposed involvement in forming the mitochondrial permeability transition pore, which is characteristic for damaged mitochondria and apoptosis, has been challenged by more recent studies.


Pssm-ID: 132767 [Multi-domain]  Cd Length: 276  Bit Score: 381.56  E-value: 2.19e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965   16 PPPYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVSGTLETKYKWCeyGLTFTEKWNTDNTLGT 95
Cdd:cd07306   1 PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIK--GLTLTQKWNTDNVLLT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965   96 EIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSAYKRECINLGCDVDFDFaGPAIHGSAVFGYEGWLAGYQMTFDSAKSK 175
Cdd:cd07306  79 EITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLNK-GPLVGASAVLGYKGFLLGAEVVYDTAKSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965  176 LTRSNFAVGYRTGDFQLHTNVNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLI 255
Cdd:cd07306 158 FTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNETTFAVGGQYALDPDALVKAKVNNDGQL 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6755965  256 GVGYTQTLRPGVKLTLSALVDGKSFNAGGHKLGLALELE 294
Cdd:cd07306 238 GLSYQHKLRPGVTLTLSAGFDAKNLNQGGHKFGLSLSLK 276
Porin_3 pfam01459
Eukaryotic porin;
15-288 1.01e-110

Eukaryotic porin;


Pssm-ID: 460220 [Multi-domain]  Cd Length: 269  Bit Score: 321.08  E-value: 1.01e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965     15 IPPPYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVSGTLETKYKWceYGLTFTEKWNTDNTLG 94
Cdd:pfam01459   1 NPGTYEDIGKEAKDLLNKDYHFDGAKLDVTTKSGLGVAFQVSGSFSLGSGLSSGDFEAKYKD--KGLTLTLKGDTDNDLS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965     95 TEIAIEDQICQGLKLTFDTTFSPNtgKKSGKIKSAYKRECINLGCDVDFdFAGPAIHGSAVFGYEGWLAGYQMTFDSAKS 174
Cdd:pfam01459  79 TTATVNEQLTPGLKTKLSTQFVPG--KKSGKLELDYKGDDFTASLKVGL-LAGPVVVGSYLQGVTGLALGAEASYDTASG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965    175 KLTRSNFAVGYRTGDFQLHTN-VNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSS 253
Cdd:pfam01459 156 KLTKYNAALGYTARDYIASLTlVNNGGVLTASYYHKVSEKLEVGAELTLNFSSNENTVTIGYKYDLDKSTTVKAKVNSNG 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 6755965    254 LIGVGYTQTLRPGVKLTLSALVDGKSFNaGGHKLG 288
Cdd:pfam01459 236 KVGLLYEQKLRPGVTLTLSAEVDHKKLN-GAHKFG 269
Porin3 cd07303
Eukaryotic porin family that forms channels in the mitochondrial outer membrane; The porin ...
19-292 1.87e-90

Eukaryotic porin family that forms channels in the mitochondrial outer membrane; The porin family 3 contains two sub-families that play vital roles in the mitochondrial outer membrane, a translocase for unfolded pre-proteins (Tom40) and the voltage-dependent anion channel (VDAC) that regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane.


Pssm-ID: 132765 [Multi-domain]  Cd Length: 274  Bit Score: 269.91  E-value: 1.87e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965   19 YADLGKAARDIFNKGFgFGLVKLDVKTKSCSgvEFSTSGSSNTDTG----KVSGTLETKYKWCEYGLTFTEKWNTDNTLG 94
Cdd:cd07303   2 YAELGKSARDLFTKGY-GGGIKLDVKTKSEL--EFTSSGSANTETIesttKVGGSLETKYRWSPYGLTFTEKWNTDNTLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965   95 TEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSAYKRecINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKs 174
Cdd:cd07303  79 LEITVEDQLSRGLKSTFDSSFSPNTGKKNAKIKTGYKR--INLGCDVDFDIAGPLIRGALVLGYEGWLAGYQMVFETVS- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965  175 KLTRSNFAVGYRTG--DFQLHTNVNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNS 252
Cdd:cd07303 156 RVTQSNFAVGYKTDynEFQAHTNVNDGTEFGGSIYHKVNDKLEVGVNLAATAGNSNTRFGIAAKYQVDPDACFSASVNNS 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 6755965  253 SLIGVGYTQTLRPGVKLTLSALVDGKsfnAGGHKLGLALE 292
Cdd:cd07303 236 SLVGLGYTQTLKPGIKLTLSALLDHK---AGGHKLGLGLE 272
Porin3_Tom40 cd07305
Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the ...
180-294 2.37e-03

Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the mitochondrial outer membrane with a pore about 1.5 to 2.5 nanometers wide. It functions as a transport channel for unfolded protein chains and forms a complex with Tom5, Tom6, Tom7, and Tom22. The primary receptors Tom20 and Tom70 recruit the unfolded precursor protein from the mitochondrial-import stimulating factor (MSF) or cytosolic Hsc70. The precursor passes through the Tom40 channel and through another channel in the inner membrane, formed by Tim23, to be finally translocated into the mitochondrial matrix. The process depends on a proton motive force across the inner membrane and requires a contact site where the outer and inner membranes come close. Tom40 is also involved in inserting outer membrane proteins into the membrane, most likely not via a lateral opening in the pore, but by transfering precursor proteins to an outer membrane sorting and assembly machinery.


Pssm-ID: 132766 [Multi-domain]  Cd Length: 279  Bit Score: 38.73  E-value: 2.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755965  180 NFAVGYRTGDFQLHTNVNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLdPTASISAKVNNSSLIGVGY 259
Cdd:cd07305 169 SYAARYTAGNWIASGQLGAQGGLHLSYYRKLSDKLQLGVELELNLRTRESTATLGYQYDF-RQSRFRGSIDSNGKVSAVL 247
                        90       100       110
                ....*....|....*....|....*....|....*
gi 6755965  260 TQTLRPGVKLTLSALVDgksFNAGGHKLGLALELE 294
Cdd:cd07305 248 EKRLPLPLSLLLSGELN---HVKNDYKFGFGLTIG 279
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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