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Protein

Lens fiber major intrinsic protein

Gene

Mip

Organism
Rattus norvegicus (Rat)
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei147 – 1471Important for water channel gatingBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Lens fiber major intrinsic protein
Alternative name(s):
Aquaporin-0
MIP26
Short name:
MP26
Gene namesi
Name:Mip
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3090. Mip.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini‹1 – 6›6CytoplasmicBy similarity
Transmembranei7 – 3024HelicalBy similarityAdd
BLAST
Topological domaini31 – 366ExtracellularBy similarity
Transmembranei37 – 5923HelicalBy similarityAdd
BLAST
Intramembranei60 – 656By similarity
Intramembranei66 – 7611HelicalBy similarityAdd
BLAST
Topological domaini77 – 826CytoplasmicBy similarity
Transmembranei83 – 10523HelicalBy similarityAdd
BLAST
Topological domaini106 – 12419ExtracellularBy similarityAdd
BLAST
Transmembranei125 – 14521HelicalBy similarityAdd
BLAST
Topological domaini146 – 15712CytoplasmicBy similarityAdd
BLAST
Transmembranei158 – 17417HelicalBy similarityAdd
BLAST
Intramembranei175 – 1817By similarity
Intramembranei182 – 19211HelicalBy similarityAdd
BLAST
Topological domaini193 – 1986ExtracellularBy similarity
Transmembranei199 – 21719HelicalBy similarityAdd
BLAST
Topological domaini218 – 26144CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • gap junction Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: UniProtKB
  • intracellular canaliculus Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Gap junction, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi244 – 2441N → D: No effects. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 261›261Lens fiber major intrinsic proteinPRO_0000063914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei233 – 2331Phosphoserine1 Publication
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei243 – 2431PhosphoserineBy similarity

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

PaxDbiP09011.

PTM databases

iPTMnetiP09011.
PhosphoSiteiP09011.

Expressioni

Tissue specificityi

Major component of lens fiber gap junctions.

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

STRINGi10116.ENSRNOP00000004223.

Structurei

3D structure databases

ProteinModelPortaliP09011.
SMRiP09011. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni225 – 23511Interaction with CALMBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi66 – 683NPA 1
Motifi182 – 1843NPA 2

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.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP09011.
PhylomeDBiP09011.

Family and domain databases

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: Fragment.

P09011-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ELRSASFWRA IFAEFFATLF YVFFGLGSSL RWAPGPLHVL QVALAFGLAL
60 70 80 90 100
ATLVQTVGHI SGAHVNPAVT FAFLVGSQMS LLRAFCYIAA QLLGAVAGAA
110 120 130 140 150
VLYSVTPPAV RGNLALNTLH AGVSVGQATT VEIFLTLQFV LCIFATYDER
160 170 180 190 200
RNGRMGSVAL AVGFSLTLGH LFGMYYTGAG MNPARSFAPA ILTRNFSNHW
210 220 230 240 250
VYWVGPIIGG GLGSLLYDFL LFPRLKSVSE RLSILKGARP SDSNGQPEGT
260
GEPVELKTQA L
Length:261
Mass (Da):27,891
Last modified:February 1, 1991 - v2
Checksum:i703C3FDBA113AA95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti132 – 1332EI → RF in CAA31035 (PubMed:7848273).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12514 mRNA. Translation: CAA31035.1.
X53052 mRNA. Translation: CAA37219.1.
PIRiS01439.
S53423.
UniGeneiRn.23532.

Genome annotation databases

UCSCiRGD:3090. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12514 mRNA. Translation: CAA31035.1.
X53052 mRNA. Translation: CAA37219.1.
PIRiS01439.
S53423.
UniGeneiRn.23532.

3D structure databases

ProteinModelPortaliP09011.
SMRiP09011. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004223.

PTM databases

iPTMnetiP09011.
PhosphoSiteiP09011.

Proteomic databases

PaxDbiP09011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3090. rat.

Organism-specific databases

RGDi3090. Mip.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP09011.
PhylomeDBiP09011.

Family and domain databases

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...

Publicationsi

  1. "Nucleotide and derived amino-acid sequence of the major intrinsic protein of rat eye-lens."
    Kent N.A., Shiels A.
    Nucleic Acids Res. 18:4256-4256(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Eye.
  2. "Heterologous expression in Escherichia coli of native and mutant forms of the major intrinsic protein of rat eye lens (MIP26)."
    Dilsiz N., Crabbe M.J.C.
    Biochem. J. 305:753-759(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASN-244.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-261.
    Strain: Sprague-Dawley.
  4. "Modifications to rat lens major intrinsic protein in selenite-induced cataract."
    Schey K.L., Fowler J.G., Shearer T.R., David L.
    Invest. Ophthalmol. Vis. Sci. 40:657-667(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-233.

Entry informationi

Entry nameiMIP_RAT
AccessioniPrimary (citable) accession number: P09011
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1991
Last modified: July 6, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.