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Protein

Lens fiber major intrinsic protein

Gene

MIP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Water channel (PubMed:23893133). 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).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei149Important for water channel gating1

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiR-BTA-432047. Passive transport by Aquaporins.

Protein family/group databases

TCDBi1.A.8.8.2. the major intrinsic protein (mip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Lens fiber major intrinsic protein
Alternative name(s):
Aquaporin-0
MIP26
Short name:
MP26
Gene namesi
Name:MIP
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

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 – 8Cytoplasmic8
Transmembranei9 – 32HelicalAdd BLAST24
Topological domaini33 – 38Extracellular6
Transmembranei39 – 61HelicalAdd BLAST23
Intramembranei62 – 676
Intramembranei68 – 78HelicalAdd BLAST11
Topological domaini79 – 84Cytoplasmic6
Transmembranei85 – 107HelicalAdd BLAST23
Topological domaini108 – 126ExtracellularAdd BLAST19
Transmembranei127 – 147HelicalAdd BLAST21
Topological domaini148 – 159CytoplasmicAdd BLAST12
Transmembranei160 – 176HelicalAdd BLAST17
Intramembranei177 – 1837
Intramembranei184 – 194HelicalAdd BLAST11
Topological domaini195 – 200Extracellular6
Transmembranei201 – 219HelicalAdd BLAST19
Topological domaini220 – 263CytoplasmicAdd BLAST44

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell junction, Cell membrane, Gap junction, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi149Y → G: Increases constitutive water permeability. Abolishes regulation by cytoplasmic calcium levels. 1 Publication1
Mutagenesisi149Y → L: Strongly decreases water permeability. Abolishes regulation by cytoplasmic calcium levels. 1 Publication1
Mutagenesisi149Y → S: Slightly decreases water permeability, but has a minor effect on the regulation by cytoplasmic calcium levels. 1 Publication1
Mutagenesisi227L → A: Strongly reduced CALM binding. 1 Publication1
Mutagenesisi230V → A: Strongly reduced CALM binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000639101 – 263Lens fiber major intrinsic proteinAdd BLAST263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei235Phosphoserine1 Publication1
Modified residuei243Phosphoserine; by PKA1 Publication1
Modified residuei245Phosphoserine1 Publication1
Modified residuei246Deamidated asparagine1 Publication1

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

PaxDbiP06624.

PTM databases

iPTMnetiP06624.

Expressioni

Tissue specificityi

Major component of lens fiber gap junctions.

Developmental stagei

Higher expression in pre-natal (1-5 months gestation) than in postnatal (4-6 months) calf lens.

Gene expression databases

BgeeiENSBTAG00000010127.

Interactioni

Subunit structurei

Homotetramer (PubMed:15377788, PubMed:16309700). Homooctamer formed by head-to-head interaction between homotetramers from adjoining membranes (PubMed:15377788, PubMed:16309700). Interacts with CALM; one CALM molecule interacts with the cytoplasmic domains of two aquaporins, leading to channel closure (PubMed:23893133).3 Publications

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-60546N.
STRINGi9913.ENSBTAP00000013360.

Structurei

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 31Combined sources22
Helixi38 – 59Combined sources22
Turni60 – 63Combined sources4
Helixi69 – 77Combined sources9
Helixi83 – 107Combined sources25
Turni110 – 112Combined sources3
Turni114 – 117Combined sources4
Helixi127 – 149Combined sources23
Helixi160 – 179Combined sources20
Helixi185 – 195Combined sources11
Turni199 – 202Combined sources4
Helixi203 – 220Combined sources18
Turni221 – 223Combined sources3
Helixi230 – 238Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YMGX-ray2.24A1-263[»]
2C32X-ray7.01A1-263[»]
ProteinModelPortaliP06624.
SMRiP06624.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06624.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni227 – 237Interaction with CALM1 PublicationAdd BLAST11

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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.

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP06624.
KOiK09863.
OMAiCELVFVI.
OrthoDBiEOG091G166T.
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.

P06624-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWELRSASFW RAICAEFFAS LFYVFFGLGA SLRWAPGPLH VLQVALAFGL
60 70 80 90 100
ALATLVQAVG HISGAHVNPA VTFAFLVGSQ MSLLRAICYM VAQLLGAVAG
110 120 130 140 150
AAVLYSVTPP AVRGNLALNT LHPGVSVGQA TIVEIFLTLQ FVLCIFATYD
160 170 180 190 200
ERRNGRLGSV ALAVGFSLTL GHLFGMYYTG AGMNPARSFA PAILTRNFTN
210 220 230 240 250
HWVYWVGPVI GAGLGSLLYD FLLFPRLKSV SERLSILKGS RPSESNGQPE
260
VTGEPVELKT QAL
Length:263
Mass (Da):28,223
Last modified:January 1, 1988 - v1
Checksum:iE08C2C4F33398D4E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14C → L AA sequence (PubMed:3882455).Curated1
Sequence conflicti29 – 33GASLR → RAFLL AA sequence (PubMed:3882455).Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02818 mRNA. Translation: AAA30622.1.
PIRiA23251. MMBOLM.
RefSeqiNP_776362.1. NM_173937.2.
UniGeneiBt.4516.

Genome annotation databases

EnsembliENSBTAT00000013360; ENSBTAP00000013360; ENSBTAG00000010127.
GeneIDi280859.
KEGGibta:280859.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02818 mRNA. Translation: AAA30622.1.
PIRiA23251. MMBOLM.
RefSeqiNP_776362.1. NM_173937.2.
UniGeneiBt.4516.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YMGX-ray2.24A1-263[»]
2C32X-ray7.01A1-263[»]
ProteinModelPortaliP06624.
SMRiP06624.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60546N.
STRINGi9913.ENSBTAP00000013360.

Protein family/group databases

TCDBi1.A.8.8.2. the major intrinsic protein (mip) family.

PTM databases

iPTMnetiP06624.

Proteomic databases

PaxDbiP06624.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000013360; ENSBTAP00000013360; ENSBTAG00000010127.
GeneIDi280859.
KEGGibta:280859.

Organism-specific databases

CTDi4284.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP06624.
KOiK09863.
OMAiCELVFVI.
OrthoDBiEOG091G166T.
TreeFamiTF312940.

Enzyme and pathway databases

ReactomeiR-BTA-432047. Passive transport by Aquaporins.

Miscellaneous databases

EvolutionaryTraceiP06624.

Gene expression databases

BgeeiENSBTAG00000010127.

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_BOVIN
AccessioniPrimary (citable) accession number: P06624
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 2, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.