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Conserved domains on  [gi|30039716|ref|NP_780314|]
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aquaporin-11 [Mus musculus]

Protein Classification

MIP/aquaporin family protein( domain architecture ID 239)

MIP (Major Intrinsic Protein)/aquaporin family protein similar to aquaporin that permits osmotically driven movement of water in both directions, and glycerol uptake facilitator protein that mediates glycerol diffusion across the cytoplasmic membrane via a pore-type mechanism

CATH:  1.20.1080.10
Gene Ontology:  GO:0055085|GO:0015267
PubMed:  8849412|11473620|11964478
SCOP:  3000508
TCDB:  1.A.8

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MIP super family cl00200
Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane ...
 46-257 1.23e-03

Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane channels that selectively transport water, small neutral molecules, and ions out of and between cells. The channel proteins share a common fold: the N-terminal cytosolic portion followed by six transmembrane helices, which might have arisen through gene duplication. On the basis of sequence similarity and functional characteristics, the superfamily can be subdivided into two major groups: water-selective channels called aquaporins (AQPs) and glycerol uptake facilitators (GlpFs). AQPs are found in all three kingdoms of life, while GlpFs have been characterized only within microorganisms.


The actual alignment was detected with superfamily member cd00333:

Pssm-ID: 444743  Cd Length: 228  Bit Score: 39.16  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039716  46 AFVLEFLATFQL----CCCTHELQVLSEQDSAHptWTLTLIYFFSLVHGLTLVGTAS----NPCGVMMQMILGGMSPEMG 117
Cdd:cd00333   2 KYLAEFLGTFLLvffgCGSVLAVKLAGGASGGL--LGIALAWGFAIFVLVYAVGHISgghiNPAVTLALAVGGRFPLIRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039716 118 AVRLLAQLVSALCSRYCISALWSLSLTKYHYDERILACRN----PIHTDMSKAIIIEAICSFIFHSALLHFQEVRTKLRI 193
Cdd:cd00333  80 IPYIIAQLLGAILGAALLYGLYYGLYLEFLGANNIVAGIFgtypSPGVSNGNAFFVEFIGTFILVLVVFATTDDPNGPPP 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30039716 194 HLLAALITFLAY-----AGGSLTGALFNPALALSLHFPCFDELFYKFFVVYWLAPSVGVLMMILMFSFF 257
Cdd:cd00333 160 GGLAPLAIGLLVaaiglAGGPITGASMNPARSLGPALFTGLARHWHYFWVYWVGPLIGAIAGALVYDYV 228
 
Name Accession Description Interval E-value
MIP cd00333
Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane ...
 46-257 1.23e-03

Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane channels that selectively transport water, small neutral molecules, and ions out of and between cells. The channel proteins share a common fold: the N-terminal cytosolic portion followed by six transmembrane helices, which might have arisen through gene duplication. On the basis of sequence similarity and functional characteristics, the superfamily can be subdivided into two major groups: water-selective channels called aquaporins (AQPs) and glycerol uptake facilitators (GlpFs). AQPs are found in all three kingdoms of life, while GlpFs have been characterized only within microorganisms.


Pssm-ID: 238204  Cd Length: 228  Bit Score: 39.16  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039716  46 AFVLEFLATFQL----CCCTHELQVLSEQDSAHptWTLTLIYFFSLVHGLTLVGTAS----NPCGVMMQMILGGMSPEMG 117
Cdd:cd00333   2 KYLAEFLGTFLLvffgCGSVLAVKLAGGASGGL--LGIALAWGFAIFVLVYAVGHISgghiNPAVTLALAVGGRFPLIRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039716 118 AVRLLAQLVSALCSRYCISALWSLSLTKYHYDERILACRN----PIHTDMSKAIIIEAICSFIFHSALLHFQEVRTKLRI 193
Cdd:cd00333  80 IPYIIAQLLGAILGAALLYGLYYGLYLEFLGANNIVAGIFgtypSPGVSNGNAFFVEFIGTFILVLVVFATTDDPNGPPP 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30039716 194 HLLAALITFLAY-----AGGSLTGALFNPALALSLHFPCFDELFYKFFVVYWLAPSVGVLMMILMFSFF 257
Cdd:cd00333 160 GGLAPLAIGLLVaaiglAGGPITGASMNPARSLGPALFTGLARHWHYFWVYWVGPLIGAIAGALVYDYV 228
 
Name Accession Description Interval E-value
MIP cd00333
Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane ...
 46-257 1.23e-03

Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane channels that selectively transport water, small neutral molecules, and ions out of and between cells. The channel proteins share a common fold: the N-terminal cytosolic portion followed by six transmembrane helices, which might have arisen through gene duplication. On the basis of sequence similarity and functional characteristics, the superfamily can be subdivided into two major groups: water-selective channels called aquaporins (AQPs) and glycerol uptake facilitators (GlpFs). AQPs are found in all three kingdoms of life, while GlpFs have been characterized only within microorganisms.


Pssm-ID: 238204  Cd Length: 228  Bit Score: 39.16  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039716  46 AFVLEFLATFQL----CCCTHELQVLSEQDSAHptWTLTLIYFFSLVHGLTLVGTAS----NPCGVMMQMILGGMSPEMG 117
Cdd:cd00333   2 KYLAEFLGTFLLvffgCGSVLAVKLAGGASGGL--LGIALAWGFAIFVLVYAVGHISgghiNPAVTLALAVGGRFPLIRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30039716 118 AVRLLAQLVSALCSRYCISALWSLSLTKYHYDERILACRN----PIHTDMSKAIIIEAICSFIFHSALLHFQEVRTKLRI 193
Cdd:cd00333  80 IPYIIAQLLGAILGAALLYGLYYGLYLEFLGANNIVAGIFgtypSPGVSNGNAFFVEFIGTFILVLVVFATTDDPNGPPP 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30039716 194 HLLAALITFLAY-----AGGSLTGALFNPALALSLHFPCFDELFYKFFVVYWLAPSVGVLMMILMFSFF 257
Cdd:cd00333 160 GGLAPLAIGLLVaaiglAGGPITGASMNPARSLGPALFTGLARHWHYFWVYWVGPLIGAIAGALVYDYV 228
 
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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