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Lens fiber major intrinsic protein (Aquaporin-0) (MIP26) (MP26)

 MIP_HUMAN               Reviewed;         263 AA.
P30301; Q17R41;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
27-SEP-2017, entry version 167.
RecName: Full=Lens fiber major intrinsic protein;
AltName: Full=Aquaporin-0;
AltName: Full=MIP26;
Short=MP26;
Name=MIP; Synonyms=AQP0;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1840563; DOI=10.1016/0888-7543(91)90023-8;
Pisano M.M., Chepelinsky A.B.;
"Genomic cloning, complete nucleotide sequence, and structure of the
human gene encoding the major intrinsic protein (MIP) of the lens.";
Genomics 11:981-990(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION AT SER-235, DEAMIDATION AT ASN-246 AND ASN-259, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10634618;
Schey K.L., Little M., Fowler J.G., Crouch R.K.;
"Characterization of human lens major intrinsic protein structure.";
Invest. Ophthalmol. Vis. Sci. 41:175-182(2000).
[5]
INVOLVEMENT IN CTRCT15, AND VARIANTS CTRCT15 GLY-134 AND ARG-138.
PubMed=10802646; DOI=10.1038/75538;
Berry V., Francis P., Kaushal S., Moore A., Bhattacharya S.;
"Missense mutations in MIP underlie autosomal dominant 'polymorphic'
and lamellar cataracts linked to 12q.";
Nat. Genet. 25:15-17(2000).
[6]
INVOLVEMENT IN CTRCT15.
PubMed=16564824; DOI=10.1016/j.ajo.2005.11.008;
Geyer D.D., Spence M.A., Johannes M., Flodman P., Clancy K.P.,
Berry R., Sparkes R.S., Jonsen M.D., Isenberg S.J., Bateman J.B.;
"Novel single-base deletional mutation in major intrinsic protein
(MIP) in autosomal dominant cataract.";
Am. J. Ophthalmol. 141:761-763(2006).
[7]
FATTY ACYLATION.
PubMed=27378310; DOI=10.1016/j.bbamem.2016.06.026;
Ismail V.S., Mosely J.A., Tapodi A., Quinlan R.A., Sanderson J.M.;
"The lipidation profile of aquaporin-0 correlates with the acyl
composition of phosphoethanolamine lipids in lens membranes.";
Biochim. Biophys. Acta 1858:2763-2768(2016).
[8]
VARIANTS CTRCT15 GLY-134 AND ARG-138.
PubMed=11001937; DOI=10.1093/oxfordjournals.hmg.a018925;
Francis P., Chung J.-J., Yasui M., Berry V., Moore A., Wyatt M.K.,
Wistow G., Bhattacharya S.S., Agre P.;
"Functional impairment of lens aquaporin in two families with
dominantly inherited cataracts.";
Hum. Mol. Genet. 9:2329-2334(2000).
[9]
VARIANT CTRCT15 CYS-33.
PubMed=17893667;
Gu F., Zhai H., Li D., Zhao L., Li C., Huang S., Ma X.;
"A novel mutation in major intrinsic protein of the lens gene (MIP)
underlies autosomal dominant cataract in a Chinese family.";
Mol. Vis. 13:1651-1656(2007).
[10]
VARIANT CTRCT15 LYS-233.
PubMed=17960133;
Lin H., Hejtmancik J.F., Qi Y.;
"A substitution of arginine to lysine at the COOH-terminus of MIP
caused a different binocular phenotype in a congenital cataract
family.";
Mol. Vis. 13:1822-1827(2007).
[11]
VARIANT CTRCT15 ILE-107.
PubMed=20361015;
Wang W., Jiang J., Zhu Y., Li J., Jin C., Shentu X., Yao K.;
"A novel mutation in the major intrinsic protein (MIP) associated with
autosomal dominant congenital cataracts in a Chinese family.";
Mol. Vis. 16:534-539(2010).
[12]
VARIANT CTRCT15 CYS-187.
PubMed=21245956;
Wang K.J., Li S.S., Yun B., Ma W.X., Jiang T.G., Zhu S.Q.;
"A novel mutation in MIP associated with congenital nuclear cataract
in a Chinese family.";
Mol. Vis. 17:70-77(2011).
[13]
VARIANT CTRCT15 ASP-165, CHARACTERIZATION OF VARIANT CTRCT15 ASP-165,
AND SUBCELLULAR LOCATION.
PubMed=23116563; DOI=10.1016/j.exer.2012.10.010;
Senthil Kumar G., Kyle J.W., Minogue P.J., Dinesh Kumar K.,
Vasantha K., Berthoud V.M., Beyer E.C., Santhiya S.T.;
"An MIP/AQP0 mutation with impaired trafficking and function underlies
an autosomal dominant congenital lamellar cataract.";
Exp. Eye Res. 110:136-141(2013).
[14]
VARIANT CTRCT15 CYS-33, CHARACTERIZATION OF VARIANT CTRCT15 CYS-33,
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=24120416; DOI=10.1016/j.exer.2013.09.019;
Kumari S.S., Gandhi J., Mustehsan M.H., Eren S., Varadaraj K.;
"Functional characterization of an AQP0 missense mutation, R33C, that
causes dominant congenital lens cataract, reveals impaired cell-to-
cell adhesion.";
Exp. Eye Res. 116:371-385(2013).
[15]
VARIANT CTRCT15 HIS-150, CHARACTERIZATION OF VARIANT CTRCT15 HIS-150,
AND SUBCELLULAR LOCATION.
PubMed=25946197; DOI=10.1371/journal.pone.0126679;
Shentu X., Miao Q., Tang X., Yin H., Zhao Y.;
"Identification and functional analysis of a novel MIP gene mutation
associated with congenital cataract in a Chinese family.";
PLoS ONE 10:E0126679-E0126679(2015).
-!- FUNCTION: Water channel (PubMed:24120416). Channel activity is
down-regulated by CALM when cytoplasmic Ca(2+) levels are
increased. 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).
Plays a role in cell-to-cell adhesion and facilitates gap junction
coupling (PubMed:24120416). {ECO:0000250|UniProtKB:Q6J8I9,
ECO:0000269|PubMed:24120416}.
-!- SUBUNIT: Homotetramer (PubMed:24120416). Homooctamer formed by
head-to-head interaction between homotetramers from adjoining
membranes. Interacts with CALM; one CALM molecule interacts with
the cytoplasmic domains of two aquaporins, leading to channel
closure (By similarity). {ECO:0000250|UniProtKB:P06624,
ECO:0000269|PubMed:24120416}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23116563,
ECO:0000269|PubMed:24120416, ECO:0000269|PubMed:25946197}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell
junction, gap junction {ECO:0000269|PubMed:24120416}.
-!- 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). {ECO:0000250}.
-!- PTM: Subject to partial proteolytic cleavage in the eye lens core.
Partial proteolysis promotes interactions between tetramers from
adjoining membranes (By similarity). {ECO:0000250}.
-!- PTM: Fatty acylated at Met-1 and Lys-238. The acyl modifications,
in decreasing order of ion abundance, are: oleoyl (C18:1) >
palmitoyl (C16:0) > stearoyl (C18:0) > eicosenoyl (C20:1) >
dihomo-gamma-linolenoyl (C20:3) > palmitoleoyl (C16:1) >
eicosadienoyl (C20:2). {ECO:0000269|PubMed:27378310}.
-!- DISEASE: Cataract 15, multiple types (CTRCT15) [MIM:615274]: An
opacification of the crystalline lens of the eye that frequently
results in visual impairment or blindness. Opacities vary in
morphology, are often confined to a portion of the lens, and may
be static or progressive. CTRCT15 includes polymorphic,
progressive punctate lamellar, cortical, anterior and posterior
polar, nonprogressive lamellar with sutural opacities, embryonic
nuclear, and pulverulent cortical, among others.
{ECO:0000269|PubMed:10802646, ECO:0000269|PubMed:11001937,
ECO:0000269|PubMed:16564824, ECO:0000269|PubMed:17893667,
ECO:0000269|PubMed:17960133, ECO:0000269|PubMed:20361015,
ECO:0000269|PubMed:21245956, ECO:0000269|PubMed:23116563,
ECO:0000269|PubMed:24120416, ECO:0000269|PubMed:25946197}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U36308; AAC02794.2; -; Genomic_DNA.
EMBL; AC024884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC074913; AAH74913.1; -; mRNA.
EMBL; BC117474; AAI17475.1; -; mRNA.
CCDS; CCDS8919.1; -.
PIR; A55279; A55279.
RefSeq; NP_036196.1; NM_012064.3.
UniGene; Hs.574026; -.
ProteinModelPortal; P30301; -.
SMR; P30301; -.
BioGrid; 110430; 5.
IntAct; P30301; 5.
MINT; MINT-8415310; -.
STRING; 9606.ENSP00000257979; -.
iPTMnet; P30301; -.
PhosphoSitePlus; P30301; -.
BioMuta; MIP; -.
DMDM; 266537; -.
OGP; P30301; -.
PaxDb; P30301; -.
PeptideAtlas; P30301; -.
PRIDE; P30301; -.
DNASU; 4284; -.
Ensembl; ENST00000257979; ENSP00000257979; ENSG00000135517.
GeneID; 4284; -.
KEGG; hsa:4284; -.
UCSC; uc001slh.4; human.
CTD; 4284; -.
DisGeNET; 4284; -.
EuPathDB; HostDB:ENSG00000135517.6; -.
GeneCards; MIP; -.
HGNC; HGNC:7103; MIP.
HPA; HPA014940; -.
MalaCards; MIP; -.
MIM; 154050; gene.
MIM; 615274; phenotype.
neXtProt; NX_P30301; -.
OpenTargets; ENSG00000135517; -.
Orphanet; 98985; Cataract with Y-shaped suture opacities.
Orphanet; 98989; Cerulean cataract.
Orphanet; 98991; Nuclear cataract.
Orphanet; 98994; Total congenital cataract.
Orphanet; 98995; Zonular cataract.
PharmGKB; PA30821; -.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
GeneTree; ENSGT00760000119223; -.
HOGENOM; HOG000288286; -.
HOVERGEN; HBG000312; -.
InParanoid; P30301; -.
KO; K09863; -.
OMA; HLMGMYY; -.
OrthoDB; EOG091G166T; -.
PhylomeDB; P30301; -.
TreeFam; TF312940; -.
Reactome; R-HSA-432047; Passive transport by Aquaporins.
SIGNOR; P30301; -.
GeneWiki; MIP_(gene); -.
GenomeRNAi; 4284; -.
PMAP-CutDB; P30301; -.
PRO; PR:P30301; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135517; -.
CleanEx; HS_MIP; -.
Genevisible; P30301; HS.
GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
GO; GO:1990349; P:gap junction-mediated intercellular transport; IDA:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
GO; GO:0006833; P:water transport; ISS:UniProtKB.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
Cataract; Cell junction; Cell membrane; Complete proteome;
Disease mutation; Eye lens protein; Gap junction; Lipoprotein;
Membrane; Palmitate; Phosphoprotein; Reference proteome; Repeat;
Sensory transduction; Transmembrane; Transmembrane helix; Transport;
Vision.
CHAIN 1 263 Lens fiber major intrinsic protein.
/FTId=PRO_0000063912.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000250}.
TRANSMEM 9 32 Helical. {ECO:0000250}.
TOPO_DOM 33 38 Extracellular. {ECO:0000250}.
TRANSMEM 39 61 Helical. {ECO:0000250}.
INTRAMEM 62 67 {ECO:0000250}.
INTRAMEM 68 78 Helical. {ECO:0000250}.
TOPO_DOM 79 84 Cytoplasmic. {ECO:0000250}.
TRANSMEM 85 107 Helical. {ECO:0000250}.
TOPO_DOM 108 126 Extracellular. {ECO:0000250}.
TRANSMEM 127 147 Helical. {ECO:0000250}.
TOPO_DOM 148 159 Cytoplasmic. {ECO:0000250}.
TRANSMEM 160 176 Helical. {ECO:0000250}.
INTRAMEM 177 183 {ECO:0000250}.
INTRAMEM 184 194 Helical. {ECO:0000250}.
TOPO_DOM 195 200 Extracellular. {ECO:0000250}.
TRANSMEM 201 219 Helical. {ECO:0000250}.
TOPO_DOM 220 263 Cytoplasmic. {ECO:0000250}.
REGION 227 237 Interaction with CALM. {ECO:0000250}.
MOTIF 68 70 NPA 1.
MOTIF 184 186 NPA 2.
SITE 149 149 Important for water channel gating.
{ECO:0000250}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000269|PubMed:10634618}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000250|UniProtKB:P06624}.
MOD_RES 246 246 Deamidated asparagine; by deterioration.
{ECO:0000269|PubMed:10634618}.
MOD_RES 259 259 Deamidated asparagine; by deterioration.
{ECO:0000269|PubMed:10634618}.
VARIANT 33 33 R -> C (in CTRCT15; reduces cell-to-cell
adhesion, reduces cell-to-cell gap
junction coupling, no loss of cell
membrane localization, no loss of water
channel activity; dbSNP:rs864309693).
{ECO:0000269|PubMed:17893667,
ECO:0000269|PubMed:24120416}.
/FTId=VAR_071601.
VARIANT 107 107 V -> I (in CTRCT15; dbSNP:rs74641138).
{ECO:0000269|PubMed:20361015}.
/FTId=VAR_071602.
VARIANT 134 134 E -> G (in CTRCT15; non-progressive
lamellar cataract; loss of activity;
dbSNP:rs121917869).
{ECO:0000269|PubMed:10802646,
ECO:0000269|PubMed:11001937}.
/FTId=VAR_011497.
VARIANT 138 138 T -> R (in CTRCT15; progressive
polymorphic and lamellar cataract; loss
of activity; dbSNP:rs121917867).
{ECO:0000269|PubMed:10802646,
ECO:0000269|PubMed:11001937}.
/FTId=VAR_011498.
VARIANT 150 150 D -> H (in CTRCT15; loss of plasma
membrane expression).
{ECO:0000269|PubMed:25946197}.
/FTId=VAR_075528.
VARIANT 165 165 G -> D (in CTRCT15; loss of plasma
membrane expression).
{ECO:0000269|PubMed:23116563}.
/FTId=VAR_075529.
VARIANT 187 187 R -> C (in CTRCT15; dbSNP:rs267603585).
{ECO:0000269|PubMed:21245956}.
/FTId=VAR_071603.
VARIANT 233 233 R -> K (in CTRCT15).
{ECO:0000269|PubMed:17960133}.
/FTId=VAR_071604.
SEQUENCE 263 AA; 28122 MW; 6A864C8AA53CBC4B CRC64;
MWELRSASFW RAIFAEFFAT LFYVFFGLGS SLRWAPGPLH VLQVAMAFGL ALATLVQSVG
HISGAHVNPA VTFAFLVGSQ MSLLRAFCYM AAQLLGAVAG AAVLYSVTPP AVRGNLALNT
LHPAVSVGQA TTVEIFLTLQ FVLCIFATYD ERRNGQLGSV ALAVGFSLAL GHLFGMYYTG
AGMNPARSFA PAILTGNFTN HWVYWVGPII GGGLGSLLYD FLLFPRLKSI SERLSVLKGA
KPDVSNGQPE VTGEPVELNT QAL


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Genprice Inc, Invoices and accounting
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