Lens fiber major intrinsic protein

MIP
Identifiers
Aliases	MIP , AQP0, CTRCT15, LIM1, MIP26, MP26, major intrinsic protein of lens fiber
External IDs	OMIM: 154050 MGI: 96990 HomoloGene: 40627 GeneCards: MIP
Gene location (Human)
Chr.	Chromosome 12 (human)
End	56,469,166 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	128,067,681 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; left adrenal gland; ; body of pancreas; ; thymus; ; human skelet; ; Achilles tendon; ; placenta; ; prefrontal cortex; ; endometrium; ; rectum;
	Top expressed in
	mirror; ; ciliary body; ; morula; ; conjunctival fornix; ; yolk sac; ; corneal stroma; ; iris; ; striated muscle tissue; ; skeletal muscle tissue; ; inferior colliculus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	calmodulin binding ; structural constituent of eye lens ; water channel activity ; channel activity ;
Cellular component	integral component of membrane ; membrane ; plasma membrane ; cell junction ; apical plasma membrane ; endoplasmic reticulum ; gap junction ; integral component of plasma membrane ;
Biological process	response to stimulus ; water transport ; ion transmembrane transport ; lens development in camera-type eye ; protein homotetramerization ; visual perception ; positive regulation of cell adhesion ; gap junction-mediated intercellular transport ; transmembrane transport ;
	Sources:Amigo / QuickGO
Orthologs
	4284
	17339
	ENSG00000135517
	ENSMUSG00000025389
	P30301
	P51180
	NM_012064
	NM_008600
	NP_036196
	NP_032626
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 13, 2023

Lens fiber major intrinsic protein also known as aquaporin-0 is a protein that in humans is encoded by the MIP gene.^[5]^[6]^[7]

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.^[7]

Related Research Articles

The lens, or crystalline lens, is a transparent biconvex structure in most land vertebrate eyes. Along with the cornea, aqueous and vitreous humours it refracts light, focusing it onto the retina. In many land animals the shape of the lens can be altered, effectively changing the focal length of the eye, enabling them to focus on objects at various distances. This adjustment of the lens is known as accommodation. In many fully aquatic vertebrates such as fish other methods of accommodation are used such as changing the lens's position relative to the retina rather than changing lens shape. Accommodation is analogous to the focusing of a photographic camera via changing its lenses. In land vertebrates the lens is flatter on its anterior side than on its posterior side, while in fish the lens is often close to spherical.

Aquaporin-2 (AQP-2) is found in the apical cell membranes of the kidney's collecting duct principal cells and in intracellular vesicles located throughout the cell. It is encoded by the AQP2 gene.

Aquaporin 3 (AQP-3) is the protein product of the human AQP3 gene. It is found in the basolateral cell membrane of principal collecting duct cells and provides a pathway for water to exit these cells. Aquaporin-3 is also permeable to glycerol, ammonia, urea, and hydrogen peroxide. It is expressed in various tissues including the skin, respiratory tract, and kidneys as well as various types of cancers. In the kidney, aquaproin-3 is unresponsive to the antidiuretic hormone vasopressin, unlike aquaporin-2. This protein is also a determinant for the GIL blood group system.

<span class="mw-page-title-main">Aquaporin-1</span> Protein-coding gene in the species Homo sapiens

Aquaporin 1 (AQP-1) is a protein that in humans is encoded by the AQP1 gene.

Alpha-crystallin B chain is a protein that in humans is encoded by the CRYAB gene. It is part of the small heat shock protein family and functions as molecular chaperone that primarily binds misfolded proteins to prevent protein aggregation, as well as inhibit apoptosis and contribute to intracellular architecture. Post-translational modifications decrease the ability to chaperone. Mutations in CRYAB cause different cardiomyopathies, skeletal myopathies mainly myofibrillar myopathy, and also cataracts. In addition, defects in this gene/protein have been associated with cancer and neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.

Major intrinsic proteins comprise a large superfamily of transmembrane protein channels that are grouped together on the basis of homology. The MIP superfamily includes three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins.

The aquaporins (AQPs) are water selective.
The aquaglyceroporins are permeable to water, but also to other small uncharged molecules such as glycerol.
The third subfamily, with little conserved amino acid sequences around the NPA boxes, include 'superaquaporins' (S-aquaporins).

Gamma-crystallin D is a protein that in humans is encoded by the CRYGD gene.

Beta-crystallin B2 is a protein that in humans is encoded by the CRYBB2 gene.

Gamma-crystallin S is a protein that in humans is encoded by the CRYGS gene.

Gap junction alpha-8 protein is a protein that in humans is encoded by the GJA8 gene. It is also known as connexin 50.

Aquaporin-5 (AQP-5) is a protein that in humans is encoded by the AQP5 gene.

Aquaporin-9 (AQP-9) is a protein that in humans is encoded by the AQP9 gene.

BFSP1 is a gene that encodes the protein filensin in humans.

Beta-crystallin A4 is a protein that in humans is encoded by the CRYBA4 gene.

Aquaporin-8 is a protein that in humans is encoded by the AQP8 gene.

Aquaporin-7 (AQP-7) is a protein that in humans is encoded by the AQP7 gene.

Gamma-crystallin A is a protein that in humans is encoded by the CRYGA gene.

Lens fiber membrane intrinsic protein is a protein that in humans is encoded by the LIM2 gene.

Alpha-crystallin A chain is a protein that in humans is encoded by the CRYAA gene.

Aquaporin-6, (AQP-6) also known as kidney-specific aquaporin is a protein in humans that is encoded by the AQP6 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000135517 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025389 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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 . hdl:2066/21519. 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. S2CID 40684631.
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. S2CID 53227438.
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. doi: 10.1242/jcs.111.15.2109 . 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. S2CID 22878198.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000135517 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025389 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1840563-5] 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.

[pmid7536742-6] 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 . hdl:2066/21519. PMID 7536742.

[entrez-7] 1 2 "Entrez Gene: MIP major intrinsic protein of lens fiber".

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Lens fiber major intrinsic protein

Contents

Function

Related Research Articles

References

Further reading