P09011 (MIP_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lens fiber major intrinsic protein

Alternative name(s):
Aquaporin-0
MIP26
Short name=MP26

Gene names

Name:

Mip

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	261 AA.
Sequence status	Fragment.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell junction Cell membrane Gap junction Membrane
Domain	Repeat Transmembrane Transmembrane helix
Molecular function	Eye lens protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	canalicular bile acid transport Inferred from direct assay. Source: RGD
Cellular component	gap junction Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular canaliculus Inferred from direct assay. Source: RGD microsome Inferred from direct assay. Source: RGD
Molecular function	structural constituent of eye lens Inferred from electronic annotation. Source: UniProtKB-KW water channel activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 261	›261	Lens fiber major intrinsic protein		PRO_0000063914
Regions
	Topological domain	‹1 – 6	›6	Cytoplasmic By similarity
	Transmembrane	7 – 30	24	Helical; By similarity
	Topological domain	31 – 36	6	Extracellular By similarity
	Transmembrane	37 – 59	23	Helical; By similarity
	Intramembrane	60 – 65	6	By similarity
	Intramembrane	66 – 76	11	Helical; By similarity
	Topological domain	77 – 82	6	Cytoplasmic By similarity
	Transmembrane	83 – 105	23	Helical; By similarity
	Topological domain	106 – 124	19	Extracellular By similarity
	Transmembrane	125 – 145	21	Helical; By similarity
	Topological domain	146 – 157	12	Cytoplasmic By similarity
	Transmembrane	158 – 174	17	Helical; By similarity
	Intramembrane	175 – 181	7	By similarity
	Intramembrane	182 – 192	11	Helical; By similarity
	Topological domain	193 – 198	6	Extracellular By similarity
	Transmembrane	199 – 217	19	Helical; By similarity
	Topological domain	218 – 261	44	Cytoplasmic By similarity
	Motif	66 – 68	3	NPA 1
	Motif	182 – 184	3	NPA 2
Amino acid modifications
	Modified residue	233	1	Phosphoserine Ref.4
	Modified residue	241	1	Phosphoserine By similarity
	Modified residue	243	1	Phosphoserine By similarity
Experimental info
	Mutagenesis	244	1	N → D: No effects. Ref.2
	Sequence conflict	132 – 133	2	EI → RF in CAA31035. Ref.2
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P09011 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 703C3FDBA113AA95	FASTA	261	27,891
	10 20 30 40 50 60 ELRSASFWRA IFAEFFATLF YVFFGLGSSL RWAPGPLHVL QVALAFGLAL ATLVQTVGHI 70 80 90 100 110 120 SGAHVNPAVT FAFLVGSQMS LLRAFCYIAA QLLGAVAGAA VLYSVTPPAV RGNLALNTLH 130 140 150 160 170 180 AGVSVGQATT VEIFLTLQFV LCIFATYDER RNGRMGSVAL AVGFSLTLGH LFGMYYTGAG 190 200 210 220 230 240 MNPARSFAPA ILTRNFSNHW VYWVGPIIGG GLGSLLYDFL LFPRLKSVSE RLSILKGARP 250 260 SDSNGQPEGT GEPVELKTQA L

References

[1]	"Nucleotide and derived amino-acid sequence of the major intrinsic protein of rat eye-lens." Kent N.A., Shiels A. Nucleic Acids Res. 18:4256-4256(1990) [PubMed: 2377471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Eye.
[2]	"Heterologous expression in Escherichia coli of native and mutant forms of the major intrinsic protein of rat eye lens (MIP26)." Dilsiz N., Crabbe M.J.C. Biochem. J. 305:753-759(1995) [PubMed: 7848273] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASN-244.
[3]	"Homology of MIP26 to Nod26." Shiels A., Kent N.A., McHale M., Bangham J.A. Nucleic Acids Res. 16:9348-9348(1988) [PubMed: 3174458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-261. Strain: Sprague-Dawley.
[4]	"Modifications to rat lens major intrinsic protein in selenite-induced cataract." Schey K.L., Fowler J.G., Shearer T.R., David L. Invest. Ophthalmol. Vis. Sci. 40:657-667(1999) [PubMed: 10067969] [Abstract] Cited for: PHOSPHORYLATION AT SER-233.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X12514 mRNA. Translation: CAA31035.1. X53052 mRNA. Translation: CAA37219.1.
IPI	IPI00231278.
PIR	S01439. S53423.
UniGene	Rn.23532.
3D structure databases
ProteinModelPortal	P09011.
SMR	P09011. Positions 1-261.
ModBase	Search...
Protein-protein interaction databases
STRING	P09011.
PTM databases
PhosphoSite	P09011.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	3090. Mip.
Phylogenomic databases
eggNOG	roNOG07987.
GeneTree	ENSGT00550000074347.
HOVERGEN	HBG000312.
InParanoid	P09011.
OrthoDB	EOG4CJVHW.
PhylomeDB	P09011.
Gene expression databases
ArrayExpress	P09011.
Genevestigator	P09011.
GermOnline	ENSRNOG00000003132. Rattus norvegicus.
Family and domain databases
InterPro	IPR012269. Aquaporin. IPR023271. Aquaporin-like. IPR000425. MIP. IPR022357. MIP_CS. [Graphical view]
Gene3D	G3DSA:1.20.1080.10. MIP. 1 hit.
PANTHER	PTHR19139. MIP. 1 hit.
Pfam	PF00230. MIP. 1 hit. [Graphical view]
PRINTS	PR00783. MINTRINSICP.
SUPFAM	SSF81338. MIP. 1 hit.
TIGRFAMs	TIGR00861. MIP. 1 hit.
PROSITE	PS00221. MIP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MIP_RAT

Accession

Primary (citable) accession number: P09011

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	February 1, 1991
Last modified:	September 21, 2011
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program