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Conserved domains on  [gi|1959493770|ref|NP_001378892|]
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voltage-dependent anion-selective channel protein 2 isoform 2 [Homo sapiens]

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 ...
15-293 7.65e-133

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: 377.70  E-value: 7.65e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  15 PPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCeyGLTFTEKWNTDNTLGT 94
Cdd:cd07306     1 PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIK--GLTLTQKWNTDNVLLT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  95 EIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFaGPAIHGSAVFGYEGWLAGYQMTFDSAKSK 174
Cdd:cd07306    79 EITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLNK-GPLVGASAVLGYKGFLLGAEVVYDTAKSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770 175 LTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLI 254
Cdd:cd07306   158 FTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNETTFAVGGQYALDPDALVKAKVNNDGQL 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1959493770 255 GVGYTQTLRPGVKLTLSALVDGKSINAGGHKVGLALELE 293
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 ...
15-293 7.65e-133

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: 377.70  E-value: 7.65e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  15 PPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCeyGLTFTEKWNTDNTLGT 94
Cdd:cd07306     1 PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIK--GLTLTQKWNTDNVLLT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  95 EIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFaGPAIHGSAVFGYEGWLAGYQMTFDSAKSK 174
Cdd:cd07306    79 EITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLNK-GPLVGASAVLGYKGFLLGAEVVYDTAKSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770 175 LTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLI 254
Cdd:cd07306   158 FTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNETTFAVGGQYALDPDALVKAKVNNDGQL 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1959493770 255 GVGYTQTLRPGVKLTLSALVDGKSINAGGHKVGLALELE 293
Cdd:cd07306   238 GLSYQHKLRPGVTLTLSAGFDAKNLNQGGHKFGLSLSLK 276
Porin_3 pfam01459
Eukaryotic porin;
14-287 2.60e-109

Eukaryotic porin;


Pssm-ID: 460220 [Multi-domain]  Cd Length: 269  Bit Score: 317.62  E-value: 2.60e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  14 IPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWceYGLTFTEKWNTDNTLG 93
Cdd:pfam01459   1 NPGTYEDIGKEAKDLLNKDYHFDGAKLDVTTKSGLGVAFQVSGSFSLGSGLSSGDFEAKYKD--KGLTLTLKGDTDNDLS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  94 TEIAIEDQICQGLKLTFDTTFSPNtgKKSGKIKSSYKRECINLGCDVDFdFAGPAIHGSAVFGYEGWLAGYQMTFDSAKS 173
Cdd:pfam01459  79 TTATVNEQLTPGLKTKLSTQFVPG--KKSGKLELDYKGDDFTASLKVGL-LAGPVVVGSYLQGVTGLALGAEASYDTASG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770 174 KLTRNNFAVGYRTGDFQLHTN-VNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSS 252
Cdd:pfam01459 156 KLTKYNAALGYTARDYIASLTlVNNGGVLTASYYHKVSEKLEVGAELTLNFSSNENTVTIGYKYDLDKSTTVKAKVNSNG 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1959493770 253 LIGVGYTQTLRPGVKLTLSALVDGKSiNAGGHKVG 287
Cdd:pfam01459 236 KVGLLYEQKLRPGVTLTLSAEVDHKK-LNGAHKFG 269
 
Name Accession Description Interval E-value
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
15-293 7.65e-133

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: 377.70  E-value: 7.65e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  15 PPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCeyGLTFTEKWNTDNTLGT 94
Cdd:cd07306     1 PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIK--GLTLTQKWNTDNVLLT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  95 EIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFaGPAIHGSAVFGYEGWLAGYQMTFDSAKSK 174
Cdd:cd07306    79 EITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLNK-GPLVGASAVLGYKGFLLGAEVVYDTAKSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770 175 LTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLI 254
Cdd:cd07306   158 FTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNETTFAVGGQYALDPDALVKAKVNNDGQL 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1959493770 255 GVGYTQTLRPGVKLTLSALVDGKSINAGGHKVGLALELE 293
Cdd:cd07306   238 GLSYQHKLRPGVTLTLSAGFDAKNLNQGGHKFGLSLSLK 276
Porin_3 pfam01459
Eukaryotic porin;
14-287 2.60e-109

Eukaryotic porin;


Pssm-ID: 460220 [Multi-domain]  Cd Length: 269  Bit Score: 317.62  E-value: 2.60e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  14 IPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWceYGLTFTEKWNTDNTLG 93
Cdd:pfam01459   1 NPGTYEDIGKEAKDLLNKDYHFDGAKLDVTTKSGLGVAFQVSGSFSLGSGLSSGDFEAKYKD--KGLTLTLKGDTDNDLS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  94 TEIAIEDQICQGLKLTFDTTFSPNtgKKSGKIKSSYKRECINLGCDVDFdFAGPAIHGSAVFGYEGWLAGYQMTFDSAKS 173
Cdd:pfam01459  79 TTATVNEQLTPGLKTKLSTQFVPG--KKSGKLELDYKGDDFTASLKVGL-LAGPVVVGSYLQGVTGLALGAEASYDTASG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770 174 KLTRNNFAVGYRTGDFQLHTN-VNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSS 252
Cdd:pfam01459 156 KLTKYNAALGYTARDYIASLTlVNNGGVLTASYYHKVSEKLEVGAELTLNFSSNENTVTIGYKYDLDKSTTVKAKVNSNG 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1959493770 253 LIGVGYTQTLRPGVKLTLSALVDGKSiNAGGHKVG 287
Cdd:pfam01459 236 KVGLLYEQKLRPGVTLTLSAEVDHKK-LNGAHKFG 269
Porin3 cd07303
Eukaryotic porin family that forms channels in the mitochondrial outer membrane; The porin ...
17-291 1.79e-88

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: 264.91  E-value: 1.79e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  17 SYADLGKAARDIFNKGFgFGLVKLDVKTKSCSgvEFSTSGSSNTDTG----KVTGTLETKYKWCEYGLTFTEKWNTDNTL 92
Cdd:cd07303     1 TYAELGKSARDLFTKGY-GGGIKLDVKTKSEL--EFTSSGSANTETIesttKVGGSLETKYRWSPYGLTFTEKWNTDNTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770  93 GTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRecINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAK 172
Cdd:cd07303    78 GLEITVEDQLSRGLKSTFDSSFSPNTGKKNAKIKTGYKR--INLGCDVDFDIAGPLIRGALVLGYEGWLAGYQMVFETVS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770 173 sKLTRNNFAVGYRTG--DFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNN 250
Cdd:cd07303   156 -RVTQSNFAVGYKTDynEFQAHTNVNDGTEFGGSIYHKVNDKLEVGVNLAATAGNSNTRFGIAAKYQVDPDACFSASVNN 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1959493770 251 SSLIGVGYTQTLRPGVKLTLSALVDGKsinAGGHKVGLALE 291
Cdd:cd07303   235 SSLVGLGYTQTLKPGIKLTLSALLDHK---AGGHKLGLGLE 272
Porin3_Tom40 cd07305
Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the ...
179-293 1.05e-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: 39.88  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959493770 179 NFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLdPTASISAKVNNSSLIGVGY 258
Cdd:cd07305   169 SYAARYTAGNWIASGQLGAQGGLHLSYYRKLSDKLQLGVELELNLRTRESTATLGYQYDF-RQSRFRGSIDSNGKVSAVL 247
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1959493770 259 TQTLRPGVKLTLSALVDGKSINAgghKVGLALELE 293
Cdd:cd07305   248 EKRLPLPLSLLLSGELNHVKNDY---KFGFGLTIG 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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