MIP
entrez
4284
canonical
uniprot
P30301
canonical
ensembl
ENSG00000135517
resolver
ensp
ENSP00000498622
resolver
enst
ENST00000652304
resolver
genesymbol
MIP
resolver
genesymbol_syn
AQP0
resolver
hgnc
HGNC:7103
resolver
uniprot
Q17R41
resolver
uniprot_entry
MIP_HUMAN
resolver
uniprot_sec
Q17R41
resolver
activity_regulation
ACTIVITY REGULATION: The water channel activity is inhibited by calcium through calmodulin/CALM. {ECO:0000269|PubMed:30790544}.
uniprot
proteins
amino_acid_sequence
MWELRSASFWRAIFAEFFATLFYVFFGLGSSLRWAPGPLHVLQVAMAFGLALATLVQSVGHISGAHVNPAVTFAFLVGSQMSLLRAFCYMAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHPAVSVGQATTVEIFLTLQFVLCIFATYDERRNGQLGSVALAVGFSLALGHLFGMYYTGAGMNPARSFAPAILTGNFTNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSISERLSVLKGAKPDVSNGQPEVTGEPVELNTQAL
uniprot
proteins
disease_involvement
DISEASE: Cataract 15, multiple types (CTRCT15) [MIM:615274]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT15 includes polymorphic, progressive punctate lamellar, cortical, anterior and posterior polar, nonprogressive lamellar with sutural opacities, embryonic nuclear, and pulverulent cortical, among others. {ECO:0000269|PubMed:10802646, ECO:0000269|PubMed:11001937, ECO:0000269|PubMed:16564824, ECO:0000269|PubMed:17893667, ECO:0000269|PubMed:17960133, ECO:0000269|PubMed:20361015, ECO:0000269|PubMed:21245956, ECO:0000269|PubMed:23116563, ECO:0000269|PubMed:24120416, ECO:0000269|PubMed:25946197, ECO:0000269|PubMed:28839118, ECO:0000269|PubMed:29914532}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Aquaporins form homotetrameric transmembrane channels, with each monomer independently mediating water transport across the plasma membrane along its osmotic gradient (PubMed:11001937, PubMed:24120416). 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 (PubMed:24120416). {ECO:0000269|PubMed:11001937, ECO:0000269|PubMed:24120416}.
uniprot
proteins
mass_dalton
28122
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:0000269|PubMed:27378310}.
uniprot
proteins
protein_family
MIP/aquaporin (TC 1.A.8) family
uniprot
proteins
pubmed
10634618
uniprot
proteins
pubmed
10802646
uniprot
proteins
pubmed
11001937
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16564824
uniprot
proteins
pubmed
17893667
uniprot
proteins
pubmed
17960133
uniprot
proteins
pubmed
1840563
uniprot
proteins
pubmed
20361015
uniprot
proteins
pubmed
21245956
uniprot
proteins
pubmed
23116563
uniprot
proteins
pubmed
24120416
uniprot
proteins
pubmed
25946197
uniprot
proteins
pubmed
27378310
uniprot
proteins
pubmed
28839118
uniprot
proteins
pubmed
29914532
uniprot
proteins
pubmed
30790544
uniprot
proteins
sequence_length
263
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11001937, ECO:0000269|PubMed:23116563, ECO:0000269|PubMed:24120416, ECO:0000269|PubMed:25946197, ECO:0000269|PubMed:30790544}; 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