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
Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane ...
13-223
1.45e-24
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: 96.94 E-value: 1.45e-24
Major intrinsic protein; MIP (Major Intrinsic Protein) family proteins exhibit essentially two ...
14-221
1.14e-23
Major intrinsic protein; MIP (Major Intrinsic Protein) family proteins exhibit essentially two distinct types of channel properties: (1) specific water transport by the aquaporins, and (2) small neutral solutes transport, such as glycerol by the glycerol facilitators.
Pssm-ID: 395174 [Multi-domain] Cd Length: 223 Bit Score: 94.69 E-value: 1.14e-23
MIP family channel proteins; 1.A.8 The Major Intrinsic Protein (MIP) FamilyThe MIP family is ...
14-221
1.14e-21
MIP family channel proteins; 1.A.8 The Major Intrinsic Protein (MIP) FamilyThe MIP family is large and diverse, possessing over 100 members that all form transmembrane channels. These channel proteins function in water, smallcarbohydrate (e.g., glycerol), urea, NH3, CO2 and possibly ion transport by an energy independent mechanism. They are found ubiquitously in bacteria, archaeaand eukaryotes. The MIP family contains two major groups of channels: aquaporins and glycerol facilitators.The known aquaporins cluster loosely together as do the known glycerol facilitators. MIP family proteins are believed to form aqueous pores that selectively allow passive transport of their solute(s) across the membrane with minimal apparent recognition. Aquaporins selectively transport water (but not glycerol) while glycerol facilitators selectively transport glycerol but not water. Some aquaporins can transport NH3 and CO2. Glycerol facilitators function as solute nonspecific channels, and may transport glycerol, dihydroxyacetone, propanediol, urea and other small neutral molecules in physiologically importantprocesses. Some members of the family, including the yeast FPS protein (TC #1.A.8.5.1) and tobacco NtTIPA may transport both water and small solutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273306 [Multi-domain] Cd Length: 216 Bit Score: 89.28 E-value: 1.14e-21
Major intrinsic protein (MIP) superfamily. Members of the MIP superfamily function as membrane ...
13-223
1.45e-24
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: 96.94 E-value: 1.45e-24
Major intrinsic protein; MIP (Major Intrinsic Protein) family proteins exhibit essentially two ...
14-221
1.14e-23
Major intrinsic protein; MIP (Major Intrinsic Protein) family proteins exhibit essentially two distinct types of channel properties: (1) specific water transport by the aquaporins, and (2) small neutral solutes transport, such as glycerol by the glycerol facilitators.
Pssm-ID: 395174 [Multi-domain] Cd Length: 223 Bit Score: 94.69 E-value: 1.14e-23
MIP family channel proteins; 1.A.8 The Major Intrinsic Protein (MIP) FamilyThe MIP family is ...
14-221
1.14e-21
MIP family channel proteins; 1.A.8 The Major Intrinsic Protein (MIP) FamilyThe MIP family is large and diverse, possessing over 100 members that all form transmembrane channels. These channel proteins function in water, smallcarbohydrate (e.g., glycerol), urea, NH3, CO2 and possibly ion transport by an energy independent mechanism. They are found ubiquitously in bacteria, archaeaand eukaryotes. The MIP family contains two major groups of channels: aquaporins and glycerol facilitators.The known aquaporins cluster loosely together as do the known glycerol facilitators. MIP family proteins are believed to form aqueous pores that selectively allow passive transport of their solute(s) across the membrane with minimal apparent recognition. Aquaporins selectively transport water (but not glycerol) while glycerol facilitators selectively transport glycerol but not water. Some aquaporins can transport NH3 and CO2. Glycerol facilitators function as solute nonspecific channels, and may transport glycerol, dihydroxyacetone, propanediol, urea and other small neutral molecules in physiologically importantprocesses. Some members of the family, including the yeast FPS protein (TC #1.A.8.5.1) and tobacco NtTIPA may transport both water and small solutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273306 [Multi-domain] Cd Length: 216 Bit Score: 89.28 E-value: 1.14e-21
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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