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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)DescriptionActionsGraphical viewLength
Sitei147Important for water channel gatingBy similarity1

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)DescriptionActionsGraphical viewLength
Topological domaini‹1 – 6CytoplasmicBy similarity›6
Transmembranei7 – 30HelicalBy similarityAdd BLAST24
Topological domaini31 – 36ExtracellularBy similarity6
Transmembranei37 – 59HelicalBy similarityAdd BLAST23
Intramembranei60 – 65By similarity6
Intramembranei66 – 76HelicalBy similarityAdd BLAST11
Topological domaini77 – 82CytoplasmicBy similarity6
Transmembranei83 – 105HelicalBy similarityAdd BLAST23
Topological domaini106 – 124ExtracellularBy similarityAdd BLAST19
Transmembranei125 – 145HelicalBy similarityAdd BLAST21
Topological domaini146 – 157CytoplasmicBy similarityAdd BLAST12
Transmembranei158 – 174HelicalBy similarityAdd BLAST17
Intramembranei175 – 181By similarity7
Intramembranei182 – 192HelicalBy similarityAdd BLAST11
Topological domaini193 – 198ExtracellularBy similarity6
Transmembranei199 – 217HelicalBy similarityAdd BLAST19
Topological domaini218 – 261CytoplasmicBy similarityAdd BLAST44

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)DescriptionActionsGraphical viewLength
Mutagenesisi244N → D: No effects. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000063914‹1 – 261Lens fiber major intrinsic proteinAdd BLAST›261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei233Phosphoserine1 Publication1
Modified residuei241PhosphoserineBy similarity1
Modified residuei243PhosphoserineBy 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

PaxDbiP09011.

PTM databases

iPTMnetiP09011.
PhosphoSitePlusiP09011.

Expressioni

Tissue specificityi

Major component of lens fiber gap junctions.

Gene expression databases

BgeeiENSRNOG00000003132.

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni225 – 235Interaction with CALMBy similarityAdd BLAST11

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi66 – 68NPA 13
Motifi182 – 184NPA 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.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP09011.
PhylomeDBiP09011.

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: 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)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti132 – 133EI → RF in CAA31035 (PubMed:7848273).Curated2

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004223.

PTM databases

iPTMnetiP09011.
PhosphoSitePlusiP09011.

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.

Gene expression databases

BgeeiENSRNOG00000003132.

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_RAT
AccessioniPrimary (citable) accession number: P09011
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 143 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.