Lens fiber major intrinsic protein

MIP

Identifiers

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)^[1]

Band	12q13.3	Start	56,449,502 bp^[1]
Band	12q13.3	End	56,469,166 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)^[2]

Band	10 D3\|10 76.49 cM	Start	128,061,707 bp^[2]
Band	10 D3\|10 76.49 cM	End	128,067,681 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right lobe of liver

left adrenal gland

body of pancreas

thymus

human skeleton

Achilles tendon

placenta

prefrontal cortex

endometrium

rectum

Top expressed in

lens

ciliary body

morula

conjunctival fornix

yolk sac

corneal stroma

iris

striated muscle tissue

skeletal muscle tissue

inferior colliculus

More reference expression data

BioGPS


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

Species

Human

Mouse

Entrez


4284


17339

Ensembl


ENSG00000135517


ENSMUSG00000025389

UniProt


P30301


P51180

RefSeq (mRNA)


NM_012064


NM_008600

RefSeq (protein)


NP_036196


NP_032626

Location (UCSC)

Chr 12: 56.45 – 56.47 Mb

Chr 10: 128.06 – 128.07 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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]

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Transcription

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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000135517 - Ensembl, May 2017
^ ^a ^b ^c 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.
^ ^a ^b "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.

v t e 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

This article on a gene on human chromosome 12 is a stub. You can help Wikipedia by expanding it.

This page was last edited on 2 January 2024, at 08:48

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Transcription

Function

References

Further reading