Mip
entrez
17339
canonical
uniprot
P51180
canonical
ensembl
ENSMUSG00000025389
resolver
ensp
ENSMUSP00000026455
resolver
enst
ENSMUST00000026455
resolver
genesymbol
Mip
resolver
genesymbol_syn
Palm
resolver
uniprot
O00285
resolver
uniprot
Q3UWJ9
resolver
uniprot
Q8BHA2
resolver
uniprot_entry
MIP_MOUSE
resolver
uniprot_sec
O00285
resolver
uniprot_sec
Q3UWJ9
resolver
uniprot_sec
Q8BHA2
resolver
activity_regulation
ACTIVITY REGULATION: The water channel activity is inhibited by calcium through calmodulin/CALM. {ECO:0000250|UniProtKB:P30301}.
uniprot
proteins
amino_acid_sequence
MWELRSASFWRAIFAEFFATLFYVFFGLGASLRWAPGPLHVLQVALAFGLALATLVQTVGHISGAHVNPAVTFAFLVGSQMSLLRAFCYIAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHAGVSVGQATTVEIFLTLQFVLCIFATYDERRNGRMGSVALAVGFSLTLGHLFGMYYTGAGMNPARSFAPAILTRNFSNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSVSERLSILKGARPSDSNGQPEGTGEPVELKTQAL
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Mip are a cause of autosomal dominant cataract. The cataract Fraser mutation (Cat-Fr or Shrivelled) is a transposon-induced splicing error that substitutes a long terminal repeat sequence for the C-terminus of Mip. The lens opacity mutation (LOP) is an AA substitution that inhibits targeting of Mip to the cell-membrane. {ECO:0000269|PubMed:8563764}.
uniprot
proteins
function
FUNCTION: Aquaporins form homotetrameric transmembrane channels, with each monomer independently mediating water transport across the plasma membrane along its osmotic gradient. Specifically expressed in lens fiber cells, this aquaporin is crucial for maintaining lens water homeostasis and transparency. Beyond water permeability, it also acts as a cell-to-cell adhesion molecule, forming thin junctions between lens fiber cells that are essential for maintaining the ordered structure and transparency of the lens. {ECO:0000250|UniProtKB:P30301}.
uniprot
proteins
mass_dalton
28193
uniprot
proteins
post_translational_modification
PTM: Subject to partial proteolytic cleavage in the eye lens core. Partial proteolysis promotes interactions between tetramers from adjoining membranes. {ECO:0000250|UniProtKB:Q6J8I9}.; PTM: Fatty acylated at Met-1 and Lys-238. The acyl modifications, in decreasing order of ion abundance, are: oleoyl (C18:1) > palmitoyl (C16:0) > stearoyl (C18:0) > eicosenoyl (C20:1) > dihomo-gamma-linolenoyl (C20:3) > palmitoleoyl (C16:1) > eicosadienoyl (C20:2). {ECO:0000250|UniProtKB:P30301}.
uniprot
proteins
protein_family
MIP/aquaporin (TC 1.A.8) family
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
8563764
uniprot
proteins
sequence_length
263
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30301}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell junction {ECO:0000250|UniProtKB:Q6J8I9}. Note=Localizes to thin cell-cell junctions in lens fiber cells. {ECO:0000250|UniProtKB:Q6J8I9}.
uniprot
proteins
transmembrane_region
TRANSMEM 10..29; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P06624"; TRANSMEM 42..59; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P06624"; TRANSMEM 83..106; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P06624"; TRANSMEM 128..148; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P06624"; TRANSMEM 157..175; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P06624"; TRANSMEM 201..222; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P06624
uniprot
proteins