Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005212 | molecular_function | structural constituent of eye lens |
| A | 0005516 | molecular_function | calmodulin binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006833 | biological_process | water transport |
| A | 0015250 | molecular_function | water channel activity |
| A | 0015267 | molecular_function | channel activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0034109 | biological_process | homotypic cell-cell adhesion |
| A | 0036438 | biological_process | maintenance of lens transparency |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0070161 | cellular_component | anchoring junction |
| A | 0098631 | molecular_function | cell adhesion mediator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MC3 A 264 |
| Chain | Residue |
| A | ARG196 |
| A | MC3269 |
| A | MC3270 |
| A | MC3272 |
| A | HOH273 |
| A | HOH304 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MC3 A 265 |
| Chain | Residue |
| A | SER106 |
| A | MC3270 |
| A | HOH291 |
| A | HOH301 |
| A | HOH327 |
| A | ALA102 |
| A | VAL103 |
| A | TYR105 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MC3 A 266 |
| Chain | Residue |
| A | LEU83 |
| A | LEU84 |
| A | ILE87 |
| A | VAL90 |
| A | VAL91 |
| A | LEU94 |
| A | LYS238 |
| A | MC3267 |
| A | MC3271 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MC3 A 267 |
| Chain | Residue |
| A | ARG5 |
| A | SER6 |
| A | PHE9 |
| A | TRP10 |
| A | LEU84 |
| A | CYS88 |
| A | MC3266 |
| A | MC3272 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MC3 A 268 |
| Chain | Residue |
| A | ALA7 |
| A | TRP10 |
| A | ARG11 |
| A | PHE14 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MC3 A 269 |
| Chain | Residue |
| A | MC3264 |
| A | MC3272 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MC3 A 270 |
| Chain | Residue |
| A | LEU95 |
| A | TYR105 |
| A | ILE193 |
| A | LEU194 |
| A | ARG196 |
| A | MC3264 |
| A | MC3265 |
| A | HOH326 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MC3 A 271 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MC3 A 272 |
| Chain | Residue |
| A | MC3264 |
| A | MC3267 |
| A | MC3269 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 29 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGLGSLLYdFllfprlksvserl.....SILK |
| Chain | Residue | Details |
| A | ILE210-LYS238 | |
| site_id | PS00221 |
| Number of Residues | 9 |
| Details | MIP MIP family signature. HVNPAVTFA |
| Chain | Residue | Details |
| A | HIS66-ALA74 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 35 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 27 |
| Details | Intramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 10 |
| Details | Region: {"description":"Interaction with CALM","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Motif: {"description":"NPA 1","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Motif: {"description":"NPA 2","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for water channel gating","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; promotes interactions between tetramers from adjoining membranes","evidences":[{"source":"PubMed","id":"15351655","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]} |