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Protein

Lens fiber major intrinsic protein

Gene

MIP

Organism
Ovis aries (Sheep)
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.5 Publications

Sites

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionEye lens protein
Biological processSensory transduction, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Lens fiber major intrinsic protein
Alternative name(s):
Aquaporin-0
Gene namesi
Name:MIP
Synonyms:AQP0
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Chromosome 3

Subcellular locationi

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

Keywords - Cellular componenti

Cell junction, Cell membrane, Gap junction, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000639151 – 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.1 Publication
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).By similarity

Keywords - PTMi

Lipoprotein, Phosphoprotein

Expressioni

Tissue specificityi

Detected in eye lens (at protein level).3 Publications

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.4 Publications

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-46234N.

Structurei

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 31Combined sources26
Beta strandi36 – 38Combined sources3
Helixi40 – 58Combined sources19
Helixi59 – 61Combined sources3
Helixi69 – 77Combined sources9
Helixi83 – 107Combined sources25
Turni110 – 112Combined sources3
Beta strandi114 – 117Combined sources4
Helixi127 – 148Combined sources22
Helixi160 – 175Combined sources16
Turni176 – 178Combined sources3
Helixi185 – 195Combined sources11
Turni199 – 202Combined sources4
Helixi203 – 220Combined sources18
Turni221 – 223Combined sources3
Helixi230 – 233Combined sources4
Helixi234 – 236Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SORX-ray3.00A5-239[»]
2B6OX-ray1.90A1-263[»]
2B6PX-ray2.40A1-263[»]
3J41electron microscopy25.0A/B/C/D1-263[»]
3M9Ielectron microscopy2.50A7-226[»]
ProteinModelPortaliQ6J8I9.
SMRiQ6J8I9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6J8I9.

Family & Domainsi

Region

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

GeneTreeiENSGT00760000119223.
HOVERGENiHBG000312.
KOiK09863.
OMAiMWELRST.
OrthoDBiEOG091G166T.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
InterProiView protein in InterPro
IPR023271. Aquaporin-like.
IPR034294. Aquaporin_transptr.
IPR000425. MIP.
IPR022357. MIP_CS.
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiView protein in Pfam
PF00230. MIP. 1 hit.
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiView protein in PROSITE
PS00221. MIP. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6J8I9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWELRSASFW RAIFAEFFAT LFYVFFGLGA SLRWAPGPLH VLQVALAFGL
60 70 80 90 100
ALATLVQAVG HISGAHVNPA VTFAFLVGSQ MSLLRAICYV 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 SERLSILKGT RPSESNGQPE
260
VTGEPVELKT QAL
Length:263
Mass (Da):28,263
Last modified:July 5, 2004 - v1
Checksum:i1BF16D4E6662C5A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY573927 Genomic DNA. Translation: AAT09161.1.
RefSeqiNP_001153230.1. NM_001159758.1.
UniGeneiOar.19891.

Genome annotation databases

EnsembliENSOART00000009579; ENSOARP00000009442; ENSOARG00000008796.
GeneIDi100294602.
KEGGioas:100294602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY573927 Genomic DNA. Translation: AAT09161.1.
RefSeqiNP_001153230.1. NM_001159758.1.
UniGeneiOar.19891.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SORX-ray3.00A5-239[»]
2B6OX-ray1.90A1-263[»]
2B6PX-ray2.40A1-263[»]
3J41electron microscopy25.0A/B/C/D1-263[»]
3M9Ielectron microscopy2.50A7-226[»]
ProteinModelPortaliQ6J8I9.
SMRiQ6J8I9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46234N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOART00000009579; ENSOARP00000009442; ENSOARG00000008796.
GeneIDi100294602.
KEGGioas:100294602.

Organism-specific databases

CTDi4284.

Phylogenomic databases

GeneTreeiENSGT00760000119223.
HOVERGENiHBG000312.
KOiK09863.
OMAiMWELRST.
OrthoDBiEOG091G166T.

Miscellaneous databases

EvolutionaryTraceiQ6J8I9.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
InterProiView protein in InterPro
IPR023271. Aquaporin-like.
IPR034294. Aquaporin_transptr.
IPR000425. MIP.
IPR022357. MIP_CS.
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiView protein in Pfam
PF00230. MIP. 1 hit.
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiView protein in PROSITE
PS00221. MIP. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMIP_SHEEP
AccessioniPrimary (citable) accession number: Q6J8I9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2004
Last modified: March 15, 2017
This is version 82 of the entry and version 1 of the sequence. See 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.