Skip Header

Contribute Send feedback
Read comments (?) or add your own

P51180 (MIP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lens fiber major intrinsic protein
Alternative name(s):
Aquaporin-0
MIP26
Short name=MP26
Gene names
Name:Mip
Synonyms:Palm
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Water channel. 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.

Subunit structure

Homotetramer. Homooctamer formed by head-to-head interaction between homotetramers from adjoining membranes By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junction › gap junction.

Tissue specificity

Major component of lens fiber gap junctions.

Domain

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.

Post-translational modification

Subject to partial proteolytic cleavage in the eye lens core. Partial proteolysis promotes interactions between tetramers from adjoining membranes By similarity.

Involvement in disease

Note=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.

Sequence similarities

Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]

Caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263Lens fiber major intrinsic protein
PRO_0000063913

Regions

Topological domain1 – 88Cytoplasmic By similarity
Transmembrane9 – 3224Helical; By similarity
Topological domain33 – 386Extracellular By similarity
Transmembrane39 – 6123Helical; By similarity
Intramembrane62 – 676 By similarity
Intramembrane68 – 7811Helical; By similarity
Topological domain79 – 846Cytoplasmic By similarity
Transmembrane85 – 10723Helical; By similarity
Topological domain108 – 12619Extracellular By similarity
Transmembrane127 – 14721Helical; By similarity
Topological domain148 – 15912Cytoplasmic By similarity
Transmembrane160 – 17617Helical; By similarity
Intramembrane177 – 1837 By similarity
Intramembrane184 – 19411Helical; By similarity
Topological domain195 – 2006Extracellular By similarity
Transmembrane201 – 21919Helical; By similarity
Topological domain220 – 26344Cytoplasmic By similarity
Motif34 – 385Important for formation of cell junction By similarity
Motif68 – 703NPA 1
Motif184 – 1863NPA 2

Amino acid modifications

Modified residue2351Phosphoserine By similarity
Modified residue2431Phosphoserine By similarity
Modified residue2451Phosphoserine By similarity

Natural variations

Natural variant511A → P in LOP. Ref.1

Experimental info

Sequence conflict301A → S in AAC03168. Ref.2
Sequence conflict1231A → T in AAC52416. Ref.1
Sequence conflict2591K → N in AAC03168. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P51180 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 3D141F7986A7ED16

FASTA26328,193
        10         20         30         40         50         60 
MWELRSASFW RAIFAEFFAT LFYVFFGLGA SLRWAPGPLH VLQVALAFGL ALATLVQTVG 

        70         80         90        100        110        120 
HISGAHVNPA VTFAFLVGSQ MSLLRAFCYI AAQLLGAVAG AAVLYSVTPP AVRGNLALNT 

       130        140        150        160        170        180 
LHAGVSVGQA TTVEIFLTLQ FVLCIFATYD ERRNGRMGSV ALAVGFSLTL GHLFGMYYTG 

       190        200        210        220        230        240 
AGMNPARSFA PAILTRNFSN HWVYWVGPII GGGLGSLLYD FLLFPRLKSV SERLSILKGA 

       250        260 
RPSDSNGQPE GTGEPVELKT QAL

« Hide

References

« Hide 'large scale' references
[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: 8563764] [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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00119140.
RefSeqNP_032626.2. NM_008600.4.
UniGeneMm.31625.
Mm.396469.

3D structure databases

ProteinModelPortalP51180.
SMRP51180. Positions 5-239.
ModBaseSearch...

Protein-protein interaction databases

STRINGP51180.

PTM databases

PhosphoSiteP51180.

Proteomic databases

PRIDEP51180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026455; ENSMUSP00000026455; ENSMUSG00000025389.
GeneID17339.
KEGGmmu:17339.
UCSCuc007hlr.1. mouse.

Organism-specific databases

CTD4284.
MGIMGI:96990. Mip.

Phylogenomic databases

eggNOGroNOG07987.
HOGENOMHBG705794.
HOVERGENHBG000312.
InParanoidP51180.
OMADSNGQPE.
OrthoDBEOG4CJVHW.
PhylomeDBP51180.

Gene expression databases

ArrayExpressP51180.
BgeeP51180.
CleanExMM_MIP.
MM_PALM.
GenevestigatorP51180.
GermOnlineENSMUSG00000025389. Mus musculus.

Family and domain databases

InterProIPR012269. Aquaporin.
IPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
Gene3DG3DSA:1.20.1080.10. MIP. 1 hit.
KOK09863.
PANTHERPTHR19139. MIP. 1 hit.
PfamPF00230. MIP. 1 hit.
[Graphical view]
PRINTSPR00783. MINTRINSICP.
SUPFAMSSF81338. MIP. 1 hit.
TIGRFAMsTIGR00861. MIP. 1 hit.
PROSITEPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291908.
SOURCESearch...

Entry information

Entry nameMIP_MOUSE
AccessionPrimary (citable) accession number: P51180
Secondary accession number(s): O00285, Q3UWJ9, Q8BHA2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2004
Last modified: November 16, 2011
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents