Mip
entrez
25480
canonical
uniprot
P09011
canonical
ensembl
ENSRNOG00000003132
resolver
ensp
ENSRNOP00000004223
resolver
enst
ENSRNOT00000004223
resolver
genesymbol
Mip
resolver
uniprot
G3V6E0
resolver
uniprot_entry
MIP_RAT
resolver
uniprot_sec
G3V6E0
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
MWELRSASFWRAIFAEFFATLFYVFFGLGSSLRWAPGPLHVLQVALAFGLALATLVQTVGHISGAHVNPAVTFAFLVGSQMSLLRAFCYIAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHAGVSVGQATTVEIFLTLQFVLCIFATYDERRNGRMGSVALAVGFSLTLGHLFGMYYTGAGMNPARSFAPAILTRNFSNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSVSERLSILKGARPSDSNGQPEGTGEPVELKTQAL
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
28209
uniprot
proteins
mutagenesis
MUTAGEN 246; /note="N->D: No effects."; /evidence="ECO:0000269|PubMed:7848273
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
10067969
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
2377471
uniprot
proteins
pubmed
3174458
uniprot
proteins
pubmed
7848273
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