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Protein

Lens fiber major intrinsic protein

Gene

MIP

Organism
Cavia porcellus (Guinea pig)
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
Sitei149 – 1491Important for water channel gatingBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Keywords - Biological processi

Sensory transduction, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Lens fiber major intrinsic protein
Alternative name(s):
Aquaporin-0
Gene namesi
Name:MIP
Synonyms:AQP0
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

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 domaini1 – 88CytoplasmicBy similarity
Transmembranei9 – 3224HelicalBy similarityAdd
BLAST
Topological domaini33 – 386ExtracellularBy similarity
Transmembranei39 – 6123HelicalBy similarityAdd
BLAST
Intramembranei62 – 676By similarity
Intramembranei68 – 7811HelicalBy similarityAdd
BLAST
Topological domaini79 – 846CytoplasmicBy similarity
Transmembranei85 – 10723HelicalBy similarityAdd
BLAST
Topological domaini108 – 12619ExtracellularBy similarityAdd
BLAST
Transmembranei127 – 14721HelicalBy similarityAdd
BLAST
Topological domaini148 – 15912CytoplasmicBy similarityAdd
BLAST
Transmembranei160 – 17617HelicalBy similarityAdd
BLAST
Intramembranei177 – 1837By similarity
Intramembranei184 – 19411HelicalBy similarityAdd
BLAST
Topological domaini195 – 2006ExtracellularBy similarity
Transmembranei201 – 21919HelicalBy similarityAdd
BLAST
Topological domaini220 – 26344CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Gap junction, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Lens fiber major intrinsic proteinPRO_0000063911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei235 – 2351Phosphoserine1 Publication
Modified residuei243 – 2431PhosphoserineBy similarity
Modified residuei245 – 2451Deamidated asparagine; by deterioration1 Publication
Modified residuei246 – 2461Deamidated asparagine; by deterioration1 Publication

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

PTM databases

iPTMnetiQ6RZ07.

Expressioni

Tissue specificityi

Detected in eye lens (at protein level).1 Publication

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

STRINGi10141.ENSCPOP00000002132.

Structurei

3D structure databases

ProteinModelPortaliQ6RZ07.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni227 – 23711Interaction with CALMBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi68 – 703NPA 1
Motifi184 – 1863NPA 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.
InParanoidiQ6RZ07.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR000425. MIP.
[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.

Q6RZ07-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWELRSASFW RAIFAEFFAT LFYVFFGLGA SLRWAPGPLH VLQVALAFGL
60 70 80 90 100
ALAXLVQTVG HISGAHVNPA VTFXFLVGSQ MSLLRAFCYM AAQLLGAVAG
110 120 130 140 150
AAVLYSVTPP AVRGNLALNT LHAGVSVXQA TTVEIFLTLQ FVLCIFATYD
160 170 180 190 200
ERRNGRLGSV ALAVGFSLTL GHLFGMYYTG AGMNPARSFA PAILTRNFTN
210 220 230 240 250
HWVYWVGPII GGGLGSLLYD FLLFPRLKSV SERLSILKGT RPSDNNGQPE
260
GTGEPVELKT QAL
Length:263
Mass (Da):28,369
Last modified:July 5, 2004 - v1
Checksum:iDCC8D03F80E67E9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY485151 mRNA. Translation: AAR37021.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY485151 mRNA. Translation: AAR37021.1.

3D structure databases

ProteinModelPortaliQ6RZ07.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000002132.

PTM databases

iPTMnetiQ6RZ07.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiQ6RZ07.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR000425. MIP.
[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_CAVPO
AccessioniPrimary (citable) accession number: Q6RZ07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 75 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

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.