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Protein

Lens fiber major intrinsic protein

Gene

Mip

Organism
Mus musculus (Mouse)
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

  • calmodulin binding Source: UniProtKB
  • channel activity Source: UniProtKB
  • gap junction channel activity Source: UniProtKB
  • structural constituent of eye lens Source: MGI
  • water channel activity Source: UniProtKB

GO - Biological processi

  • canalicular bile acid transport Source: Ensembl
  • cell communication Source: UniProtKB
  • gap junction-mediated intercellular transport Source: UniProtKB
  • lens development in camera-type eye Source: MGI
  • positive regulation of cell adhesion Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • response to stimulus Source: UniProtKB-KW
  • transmembrane transport Source: GOC
  • visual perception Source: MGI
  • water transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Keywords - Biological processi

Sensory transduction, Transport, Vision

Enzyme and pathway databases

ReactomeiR-MMU-432047. Passive transport by Aquaporins.

Names & Taxonomyi

Protein namesi
Recommended name:
Lens fiber major intrinsic protein
Alternative name(s):
Aquaporin-0
MIP26
Short name:
MP26
Gene namesi
Name:Mip
Synonyms:Palm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:96990. 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 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

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

Keywords - Cellular componenti

Cell junction, Cell membrane, Gap junction, Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in Mip are a cause of autosomal dominant cataract. The cataract Fraser mutation (Cat-Fr or Shrivelled) is a transposon-induced splicing error that substitutes a long terminal repeat sequence for the C-terminus of Mip. The lens opacity mutation (LOP) is an AA substitution that inhibits targeting of Mip to the cell-membrane.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Lens fiber major intrinsic proteinPRO_0000063913Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei235 – 2351PhosphoserineBy similarity
Modified residuei243 – 2431PhosphoserineBy similarity
Modified residuei245 – 2451PhosphoserineBy 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

MaxQBiP51180.
PaxDbiP51180.
PRIDEiP51180.

PTM databases

iPTMnetiP51180.
PhosphoSiteiP51180.
SwissPalmiP51180.

Expressioni

Tissue specificityi

Major component of lens fiber gap junctions.

Gene expression databases

BgeeiP51180.
CleanExiMM_MIP.
MM_PALM.
GenevisibleiP51180. MM.

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

STRINGi10090.ENSMUSP00000026455.

Structurei

3D structure databases

ProteinModelPortaliP51180.
SMRiP51180. Positions 2-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 385Important for formation of cell junctionBy similarity
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.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP51180.
KOiK09863.
OMAiCELVFVI.
OrthoDBiEOG7N8ZWD.
PhylomeDBiP51180.
TreeFamiTF312940.

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: Complete.

P51180-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWELRSASFW RAIFAEFFAT LFYVFFGLGA SLRWAPGPLH VLQVALAFGL
60 70 80 90 100
ALATLVQTVG HISGAHVNPA VTFAFLVGSQ MSLLRAFCYI AAQLLGAVAG
110 120 130 140 150
AAVLYSVTPP AVRGNLALNT LHAGVSVGQA TTVEIFLTLQ FVLCIFATYD
160 170 180 190 200
ERRNGRMGSV ALAVGFSLTL GHLFGMYYTG AGMNPARSFA PAILTRNFSN
210 220 230 240 250
HWVYWVGPII GGGLGSLLYD FLLFPRLKSV SERLSILKGA RPSDSNGQPE
260
GTGEPVELKT QAL
Length:263
Mass (Da):28,193
Last modified:May 10, 2004 - v2
Checksum:i3D141F7986A7ED16
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301A → S in AAC03168 (Ref. 2) Curated
Sequence conflicti123 – 1231A → T in AAC52416 (PubMed:8563764).Curated
Sequence conflicti259 – 2591K → N in AAC03168 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511A → P in LOP. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27502 mRNA. Translation: AAC52416.1.
AF000143 mRNA. Translation: AAC03168.1.
AK053490 mRNA. Translation: BAC35401.1.
AK053494 mRNA. Translation: BAC35402.1.
AK136287 mRNA. Translation: BAE22916.1.
CCDSiCCDS24265.1.
RefSeqiNP_032626.2. NM_008600.5.
UniGeneiMm.31625.
Mm.396469.

Genome annotation databases

EnsembliENSMUST00000026455; ENSMUSP00000026455; ENSMUSG00000025389.
GeneIDi17339.
KEGGimmu:17339.
UCSCiuc007hlr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27502 mRNA. Translation: AAC52416.1.
AF000143 mRNA. Translation: AAC03168.1.
AK053490 mRNA. Translation: BAC35401.1.
AK053494 mRNA. Translation: BAC35402.1.
AK136287 mRNA. Translation: BAE22916.1.
CCDSiCCDS24265.1.
RefSeqiNP_032626.2. NM_008600.5.
UniGeneiMm.31625.
Mm.396469.

3D structure databases

ProteinModelPortaliP51180.
SMRiP51180. Positions 2-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026455.

PTM databases

iPTMnetiP51180.
PhosphoSiteiP51180.
SwissPalmiP51180.

Proteomic databases

MaxQBiP51180.
PaxDbiP51180.
PRIDEiP51180.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026455; ENSMUSP00000026455; ENSMUSG00000025389.
GeneIDi17339.
KEGGimmu:17339.
UCSCiuc007hlr.1. mouse.

Organism-specific databases

CTDi4284.
MGIiMGI:96990. Mip.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP51180.
KOiK09863.
OMAiCELVFVI.
OrthoDBiEOG7N8ZWD.
PhylomeDBiP51180.
TreeFamiTF312940.

Enzyme and pathway databases

ReactomeiR-MMU-432047. Passive transport by Aquaporins.

Miscellaneous databases

PROiP51180.
SOURCEiSearch...

Gene expression databases

BgeeiP51180.
CleanExiMM_MIP.
MM_PALM.
GenevisibleiP51180. MM.

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

« Hide 'large scale' publications
  1. "Mutations in the founder of the MIP gene family underlie cataract development in the mouse."
    Shiels A., Bassnett S.
    Nat. Genet. 12:212-215(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LOP PRO-51.
    Strain: MF1.
    Tissue: Lens.
  2. de Peyer O.S., Crabbe M.J.C.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye.

Entry informationi

Entry nameiMIP_MOUSE
AccessioniPrimary (citable) accession number: P51180
Secondary accession number(s): O00285, Q3UWJ9, Q8BHA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2004
Last modified: June 8, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Ref. 2 sequence was originally thought to originate from Human.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.