MIP (gene)

Major intrinsic protein of lens fiber

PDB rendering based on 1sor.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1sor, 1ymg, 2b6o, 2b6p, 2c32

Identifiers

Symbols

MIP ; AQP0; CTRCT15; LIM1; MIP26; MP26

External IDs

OMIM: 154050 MGI: 96990 HomoloGene: 40627 IUPHAR: 687 GeneCards: MIP Gene

EC number

1.11.1.6

Gene ontology
Molecular function	• structural constituent of eye lens • transporter activity • calmodulin binding • water channel activity • glycerol channel activity
Cellular component	• plasma membrane • integral component of plasma membrane • gap junction • apical plasma membrane • intracellular membrane-bounded organelle • intracellular canaliculus
Biological process	• lens development in camera-type eye • water transport • visual perception • cellular water homeostasis • canalicular bile acid transport • glycerol transport • ion transmembrane transport • response to stimulus • transmembrane transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
56.45 – 56.47 Mb

Chr 10:
128.23 – 128.23 Mb

PubMed search

Lens fiber major intrinsic protein is a protein that in humans is encoded by the MIP gene.^[1]^[2]^[3]

Function

Major intrinsic protein is a member of the water-transporting aquaporins as well as the original member of the MIP family of channel proteins. The function of the fiber cell membrane protein encoded by this gene is undetermined, yet this protein is speculated to play a role in intracellular communication. The MIP protein is expressed in the ocular lens and is required for correct lens function. This gene has been mapped among aquaporins AQP2, AQP5, and AQP6, in a potential gene cluster at 12q13.^[3]

References

↑ Pisano MM, Chepelinsky AB (Mar 1992). "Genomic cloning, complete nucleotide sequence, and structure of the human gene encoding the major intrinsic protein (MIP) of the lens". Genomics 11 (4): 981–90. doi:10.1016/0888-7543(91)90023-8. PMID 1840563.
↑ Mulders SM, Preston GM, Deen PM, Guggino WB, van Os CH, Agre P (May 1995). "Water channel properties of major intrinsic protein of lens". J Biol Chem 270 (15): 9010–16. doi:10.1074/jbc.270.15.9010. PMID 7536742.
1 2 "Entrez Gene: MIP major intrinsic protein of lens fiber".

Chepelinsky AB, Piatigorsky J, Pisano MM, et al. (1991). "Lens protein gene expression: alpha-crystallins and MIP.". Lens and eye toxicity research 8 (2–3): 319–44. PMID 1911643.
Griffin CS, Shiels A (1992). "In situ hybridisation localises the gene for the major intrinsic protein of eye lens fibre cell membranes to human chromosome 12q14". Cytogenet. Cell Genet. 61 (1): 8–9. doi:10.1159/000133360. PMID 1505237.
Girsch SJ, Peracchia C (1992). "Calmodulin interacts with a C-terminus peptide from the lens membrane protein MIP26". Curr. Eye Res. 10 (9): 839–49. doi:10.3109/02713689109013880. PMID 1790714.
Lampe PD, Johnson RG (1991). "Amino acid sequence of in vivo phosphorylation sites in the main intrinsic protein (MIP) of lens membranes". Eur. J. Biochem. 194 (2): 541–7. doi:10.1111/j.1432-1033.1990.tb15650.x. PMID 2176601.
Manenti S, Dunia I, Benedetti EL (1990). "Fatty acid acylation of lens fiber plasma membrane proteins. MP26 and alpha-crystallin are palmitoylated". FEBS Lett. 262 (2): 356–8. doi:10.1016/0014-5793(90)80228-B. PMID 2335219.
Peracchia C, Girsch SJ (1991). "Calmodulin site at the C-terminus of the putative lens gap junction protein MIP26". Lens and eye toxicity research 6 (4): 613–21. PMID 2487274.
Saito F, Sasaki S, Chepelinsky AB, et al. (1994). "Human AQP2 and MIP genes, two members of the MIP family, map within chromosome band 12q13 on the basis of two-color FISH". Cytogenet. Cell Genet. 68 (1–2): 45–8. doi:10.1159/000133885. PMID 7525161.
Jarvis LJ, Louis CF (1996). "Purification and oligomeric state of the major lens fiber cell membrane proteins". Curr. Eye Res. 14 (9): 799–808. doi:10.3109/02713689508995802. PMID 8529419.
Wang XY, Ohtaka-Maruyama C, Pisano MM, et al. (1996). "Isolation and characterization of the 5'-flanking sequence of the human ocular lens MIP gene". Gene 167 (1–2): 321–5. doi:10.1016/0378-1119(95)00637-0. PMID 8566800.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Prabhakaram M, Katz ML, Ortwerth BJ (1997). "Glycation mediated crosslinking between alpha-crystallin and MP26 in intact lens membranes". Mech. Ageing Dev. 91 (1): 65–78. doi:10.1016/0047-6374(96)01781-2. PMID 8910261.
Ma T, Yang B, Umenishi F, Verkman AS (1997). "Closely spaced tandem arrangement of AQP2, AQP5, and AQP6 genes in a 27-kilobase segment at chromosome locus 12q13". Genomics 43 (3): 387–9. doi:10.1006/geno.1997.4836. PMID 9268644.
Ohtaka-Maruyama C, Wang X, Ge H, Chepelinsky AB (1998). "Overlapping Sp1 and AP2 binding sites in a promoter element of the lens-specific MIP gene". Nucleic Acids Res. 26 (2): 407–14. doi:10.1093/nar/26.2.407. PMC 147274. PMID 9421492.
Dunia I, Recouvreur M, Nicolas P, et al. (1998). "Assembly of connexins and MP26 in lens fiber plasma membranes studied by SDS-fracture immunolabeling". J. Cell. Sci. 111 (15): 2109–20. PMID 9664032.
Schey KL, Fowler JG, Shearer TR, David L (1999). "Modifications to rat lens major intrinsic protein in selenite-induced cataract". Invest. Ophthalmol. Vis. Sci. 40 (3): 657–67. PMID 10067969.
Schey KL, Little M, Fowler JG, Crouch RK (2000). "Characterization of human lens major intrinsic protein structure". Invest. Ophthalmol. Vis. Sci. 41 (1): 175–82. PMID 10634618.
Berry V, Francis P, Kaushal S, et al. (2000). "Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q". Nat. Genet. 25 (1): 15–7. doi:10.1038/75538. PMID 10802646.

PDB gallery

1sor: Aquaporin-0 membrane junctions reveal the structure of a closed water pore

2b6o: electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3

Voltage-gated	L-type/Ca_vα 1.1 1.2 1.3 1.4 N-type/Ca_vα2.2 P-type/Ca_vα 2.1 Q-type/Ca_vα2.1 R-type/Ca_vα2.3 T-type/Ca_vα 3.1 3.2 3.3 α₂δ-subunits 1 2 β-subunits β1 β2 β3 β4 γ-subunits γ1 γ2 γ3 γ4 Cation channels of sperm 1 2 3 4 Two-pore channel 1 2

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel α β γ δ

Proton-gated	Amiloride-sensitive cation channel 1 2 3 4

Voltage-gated	Na_vα 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 7A Na_vβ 1 2 3 4

K⁺: Potassium channel

Calcium-activated	BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 K_Ca 1.1 2.1 2.2 2.3 3.1 4.1 4.2 5.1

Inward-rectifier	K_ATP K_ir 1.1 2.1 2.2 2.3 2.4 2.6 GIRK/K_ir 3.1 3.2 3.3 3.4 K_ir 4.1 4.2 5.1 6.1 6.2 7.1

Tandem pore domain	K2P 1 2 3 4 5 6 7 9 10 12 13 15 16 17 18

Voltage-gated	K_vα1-6 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 2.1 2.2 3.1 3.2 3.3 3.4 4.1 4.2 4.3 5.1 6.1 6.2 6.3 6.4 K_vα7-12 7.1 7.2 7.3 7.4 7.5 8.1 8.2 9.1 9.2 9.3 10.1 10.2 11.1/hERG 11.2 11.3 12.1 12.2 12.3 K_vβ 1 2 3 KCNIP 1 2 3 4 minK/ISK minK/ISK-like MiRP 1 2 3 Shaker gene

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B

H⁺: Proton channel	HVCN1

M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4

M⁺: TRP cation channel	TRPA (1) TRPC 1 2 3 4 4AP 5 6 7 TRPM 1 2 3 4 5 6 7 8 TRPML 1 2 3 TRPN TRPP 1 2 TRPV 1 2 3 4 5 6

H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family

Cytoplasm: Gap junction	Connexin: A GJA1 GJA3 GJA4 GJA5 GJA8 GJA9 GJA10 B GJB1 GJB2 GJB3 GJB4 GJB5 GJB6 GJB7 C GJC1 GJC2 GJC3 D GJD2 GJD3 GJD4) Innexin

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

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MIP (gene)

Function

References

Further reading