Major intrinsic proteins
| Major intrinsic protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Structure of a glycerol-conducting channel. | |||||||||
| Identifiers | |||||||||
| Symbol | MIP | ||||||||
| Pfam | PF00230 | ||||||||
| InterPro | IPR000425 | ||||||||
| PROSITE | PDOC00193 | ||||||||
| SCOP2 | 1fx8 / SCOPe / SUPFAM | ||||||||
| TCDB | 1.A.8 | ||||||||
| OPM superfamily | 7 | ||||||||
| OPM protein | 1z98 | ||||||||
| CDD | cd00333 | ||||||||
| 
 | |||||||||
Major intrinsic proteins comprise a large superfamily of transmembrane protein channels that are grouped together on the basis of homology. The MIP superfamily includes three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins.
- The aquaporins (AQPs) are water selective.
- The aquaglyceroporins are permeable to water, but also to other small uncharged molecules such as glycerol.
- The third subfamily, with little conserved amino acid sequences around the NPA boxes, include 'superaquaporins' (S-aquaporins).
The phylogeny of insect MIP family channels has been published.