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Protein

Lens fiber major intrinsic protein

Gene

Mip

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca2+ levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei149Important for water channel gatingBy similarity1

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • channel activity Source: UniProtKB
  • gap junction channel activity Source: UniProtKB
  • glycerol channel activity Source: GO_Central
  • structural constituent of eye lens Source: MGI
  • water channel activity Source: UniProtKB

GO - Biological processi

  • cell communication Source: UniProtKB
  • cellular water homeostasis Source: GO_Central
  • gap junction-mediated intercellular transport Source: UniProtKB
  • ion transmembrane transport Source: GO_Central
  • lens development in camera-type eye Source: MGI
  • positive regulation of cell adhesion Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • response to stimulus Source: UniProtKB-KW
  • visual perception Source: MGI
  • water transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Keywords - Biological processi

Sensory transduction, Transport, Vision

Enzyme and pathway databases

ReactomeiR-MMU-432047. Passive transport by Aquaporins.

Names & Taxonomyi

Protein namesi
Recommended name:
Lens fiber major intrinsic protein
Alternative name(s):
Aquaporin-0
MIP26
Short name:
MP26
Gene namesi
Name:Mip
Synonyms:Palm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:96990. Mip.

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity
  • Cell junctiongap junction By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 8CytoplasmicBy similarity8
Transmembranei9 – 32HelicalBy similarityAdd BLAST24
Topological domaini33 – 38ExtracellularBy similarity6
Transmembranei39 – 61HelicalBy similarityAdd BLAST23
Intramembranei62 – 67By similarity6
Intramembranei68 – 78HelicalBy similarityAdd BLAST11
Topological domaini79 – 84CytoplasmicBy similarity6
Transmembranei85 – 107HelicalBy similarityAdd BLAST23
Topological domaini108 – 126ExtracellularBy similarityAdd BLAST19
Transmembranei127 – 147HelicalBy similarityAdd BLAST21
Topological domaini148 – 159CytoplasmicBy similarityAdd BLAST12
Transmembranei160 – 176HelicalBy similarityAdd BLAST17
Intramembranei177 – 183By similarity7
Intramembranei184 – 194HelicalBy similarityAdd BLAST11
Topological domaini195 – 200ExtracellularBy similarity6
Transmembranei201 – 219HelicalBy similarityAdd BLAST19
Topological domaini220 – 263CytoplasmicBy similarityAdd BLAST44

GO - Cellular componenti

  • apical plasma membrane Source: GO_Central
  • endoplasmic reticulum Source: UniProtKB
  • gap junction Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Gap junction, Membrane

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000639131 – 263Lens fiber major intrinsic proteinAdd BLAST263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei235PhosphoserineBy similarity1
Modified residuei243PhosphoserineBy similarity1
Modified residuei245PhosphoserineBy similarity1

Post-translational modificationi

Subject to partial proteolytic cleavage in the eye lens core. Partial proteolysis promotes interactions between tetramers from adjoining membranes (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP51180.
PaxDbiP51180.
PRIDEiP51180.

PTM databases

iPTMnetiP51180.
PhosphoSitePlusiP51180.
SwissPalmiP51180.

Expressioni

Tissue specificityi

Major component of lens fiber gap junctions.

Gene expression databases

BgeeiENSMUSG00000025389.
CleanExiMM_MIP.
MM_PALM.
GenevisibleiP51180. MM.

Interactioni

Subunit structurei

Homotetramer. Homooctamer formed by head-to-head interaction between homotetramers from adjoining membranes. Interacts with CALM; one CALM molecule interacts with the cytoplasmic domains of two aquaporins, leading to channel closure.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026455.

Structurei

3D structure databases

ProteinModelPortaliP51180.
SMRiP51180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni227 – 237Interaction with CALMBy similarityAdd BLAST11

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi34 – 38Important for formation of cell junctionBy similarity5
Motifi68 – 70NPA 13
Motifi184 – 186NPA 23

Domaini

Aquaporins contain two tandem repeats each containing two membrane-spanning helices and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Each tandem repeat contains a loop and a short helix that enter and leave the lipid bilayer on the same side (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP51180.
KOiK09863.
OMAiCELVFVI.
OrthoDBiEOG091G166T.
PhylomeDBiP51180.
TreeFamiTF312940.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51180-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWELRSASFW RAIFAEFFAT LFYVFFGLGA SLRWAPGPLH VLQVALAFGL
60 70 80 90 100
ALATLVQTVG HISGAHVNPA VTFAFLVGSQ MSLLRAFCYI AAQLLGAVAG
110 120 130 140 150
AAVLYSVTPP AVRGNLALNT LHAGVSVGQA TTVEIFLTLQ FVLCIFATYD
160 170 180 190 200
ERRNGRMGSV ALAVGFSLTL GHLFGMYYTG AGMNPARSFA PAILTRNFSN
210 220 230 240 250
HWVYWVGPII GGGLGSLLYD FLLFPRLKSV SERLSILKGA RPSDSNGQPE
260
GTGEPVELKT QAL
Length:263
Mass (Da):28,193
Last modified:May 10, 2004 - v2
Checksum:i3D141F7986A7ED16
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30A → S in AAC03168 (Ref. 2) Curated1
Sequence conflicti123A → T in AAC52416 (PubMed:8563764).Curated1
Sequence conflicti259K → N in AAC03168 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti51A → P in LOP. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27502 mRNA. Translation: AAC52416.1.
AF000143 mRNA. Translation: AAC03168.1.
AK053490 mRNA. Translation: BAC35401.1.
AK053494 mRNA. Translation: BAC35402.1.
AK136287 mRNA. Translation: BAE22916.1.
CCDSiCCDS24265.1.
RefSeqiNP_032626.2. NM_008600.5.
UniGeneiMm.31625.
Mm.396469.

Genome annotation databases

EnsembliENSMUST00000026455; ENSMUSP00000026455; ENSMUSG00000025389.
GeneIDi17339.
KEGGimmu:17339.
UCSCiuc007hlr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27502 mRNA. Translation: AAC52416.1.
AF000143 mRNA. Translation: AAC03168.1.
AK053490 mRNA. Translation: BAC35401.1.
AK053494 mRNA. Translation: BAC35402.1.
AK136287 mRNA. Translation: BAE22916.1.
CCDSiCCDS24265.1.
RefSeqiNP_032626.2. NM_008600.5.
UniGeneiMm.31625.
Mm.396469.

3D structure databases

ProteinModelPortaliP51180.
SMRiP51180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026455.

PTM databases

iPTMnetiP51180.
PhosphoSitePlusiP51180.
SwissPalmiP51180.

Proteomic databases

MaxQBiP51180.
PaxDbiP51180.
PRIDEiP51180.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026455; ENSMUSP00000026455; ENSMUSG00000025389.
GeneIDi17339.
KEGGimmu:17339.
UCSCiuc007hlr.1. mouse.

Organism-specific databases

CTDi4284.
MGIiMGI:96990. Mip.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP51180.
KOiK09863.
OMAiCELVFVI.
OrthoDBiEOG091G166T.
PhylomeDBiP51180.
TreeFamiTF312940.

Enzyme and pathway databases

ReactomeiR-MMU-432047. Passive transport by Aquaporins.

Miscellaneous databases

PROiP51180.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025389.
CleanExiMM_MIP.
MM_PALM.
GenevisibleiP51180. MM.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMIP_MOUSE
AccessioniPrimary (citable) accession number: P51180
Secondary accession number(s): O00285, Q3UWJ9, Q8BHA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2004
Last modified: November 2, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Ref. 2 sequence was originally thought to originate from Human.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.