MIP_MOUSE
ID MIP_MOUSE Reviewed; 263 AA.
AC P51180; O00285; Q3UWJ9; Q8BHA2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Lens fiber major intrinsic protein;
DE AltName: Full=Aquaporin-0;
DE AltName: Full=MIP26;
DE Short=MP26;
GN Name=Mip; Synonyms=Palm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LOP PRO-51.
RC STRAIN=MF1; TISSUE=Lens;
RX PubMed=8563764; DOI=10.1038/ng0296-212;
RA Shiels A., Bassnett S.;
RT "Mutations in the founder of the MIP gene family underlie cataract
RT development in the mouse.";
RL Nat. Genet. 12:212-215(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA de Peyer O.S., Crabbe M.J.C.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Water channel. Channel activity is down-regulated by CALM
CC when cytoplasmic Ca(2+) levels are increased. May be responsible for
CC regulating the osmolarity of the lens. Interactions between
CC homotetramers from adjoining membranes may stabilize cell junctions in
CC the eye lens core. Plays a role in cell-to-cell adhesion and
CC facilitates gap junction coupling (By similarity).
CC {ECO:0000250|UniProtKB:P30301, ECO:0000250|UniProtKB:Q6J8I9}.
CC -!- SUBUNIT: Homotetramer. Homooctamer formed by head-to-head interaction
CC between homotetramers from adjoining membranes. Interacts with CALM;
CC one CALM molecule interacts with the cytoplasmic domains of two
CC aquaporins, leading to channel closure. Interacts (via C-terminus) with
CC BFSP1 (via C-terminus) in aged lens fiber cells (By similarity).
CC {ECO:0000250|UniProtKB:P06624}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30301};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell
CC junction, gap junction {ECO:0000250|UniProtKB:P30301}.
CC -!- TISSUE SPECIFICITY: Major component of lens fiber gap junctions.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing two
CC membrane-spanning helices and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA). Each tandem repeat contains a loop and a short
CC helix that enter and leave the lipid bilayer on the same side (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Subject to partial proteolytic cleavage in the eye lens core.
CC Partial proteolysis promotes interactions between tetramers from
CC adjoining membranes (By similarity). {ECO:0000250}.
CC -!- PTM: Fatty acylated at Met-1 and Lys-238. The acyl modifications, in
CC decreasing order of ion abundance, are: oleoyl (C18:1) > palmitoyl
CC (C16:0) > stearoyl (C18:0) > eicosenoyl (C20:1) > dihomo-gamma-
CC linolenoyl (C20:3) > palmitoleoyl (C16:1) > eicosadienoyl (C20:2).
CC {ECO:0000250|UniProtKB:P30301}.
CC -!- DISEASE: Note=Defects in Mip are a cause of autosomal dominant
CC cataract. The cataract Fraser mutation (Cat-Fr or Shrivelled) is a
CC transposon-induced splicing error that substitutes a long terminal
CC repeat sequence for the C-terminus of Mip. The lens opacity mutation
CC (LOP) is an AA substitution that inhibits targeting of Mip to the cell-
CC membrane.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC -!- CAUTION: Ref.2 sequence was originally thought to originate from Human.
CC {ECO:0000305}.
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DR EMBL; U27502; AAC52416.1; -; mRNA.
DR EMBL; AF000143; AAC03168.1; -; mRNA.
DR EMBL; AK053490; BAC35401.1; -; mRNA.
DR EMBL; AK053494; BAC35402.1; -; mRNA.
DR EMBL; AK136287; BAE22916.1; -; mRNA.
DR CCDS; CCDS24265.1; -.
DR RefSeq; NP_032626.2; NM_008600.5.
DR AlphaFoldDB; P51180; -.
DR SMR; P51180; -.
DR STRING; 10090.ENSMUSP00000026455; -.
DR iPTMnet; P51180; -.
DR PhosphoSitePlus; P51180; -.
DR SwissPalm; P51180; -.
DR MaxQB; P51180; -.
DR PaxDb; P51180; -.
DR PRIDE; P51180; -.
DR ProteomicsDB; 290083; -.
DR Antibodypedia; 28228; 246 antibodies from 27 providers.
DR DNASU; 17339; -.
DR Ensembl; ENSMUST00000026455; ENSMUSP00000026455; ENSMUSG00000025389.
DR GeneID; 17339; -.
DR KEGG; mmu:17339; -.
DR UCSC; uc007hlr.1; mouse.
DR CTD; 4284; -.
DR MGI; MGI:96990; Mip.
DR VEuPathDB; HostDB:ENSMUSG00000025389; -.
DR eggNOG; KOG0223; Eukaryota.
DR GeneTree; ENSGT00940000156260; -.
DR HOGENOM; CLU_020019_3_3_1; -.
DR InParanoid; P51180; -.
DR OMA; WTPGPLH; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P51180; -.
DR TreeFam; TF312940; -.
DR Reactome; R-MMU-432047; Passive transport by Aquaporins.
DR BioGRID-ORCS; 17339; 1 hit in 72 CRISPR screens.
DR PRO; PR:P51180; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P51180; protein.
DR Bgee; ENSMUSG00000025389; Expressed in lens of camera-type eye and 22 other tissues.
DR Genevisible; P51180; MM.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0046691; C:intracellular canaliculus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0015267; F:channel activity; NAS:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IDA:MGI.
DR GO; GO:0015250; F:water channel activity; IMP:MGI.
DR GO; GO:0015722; P:canalicular bile acid transport; ISO:MGI.
DR GO; GO:0007154; P:cell communication; NAS:UniProtKB.
DR GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR GO; GO:0006833; P:water transport; IMP:MGI.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Disease variant; Eye lens protein;
KW Gap junction; Lipoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Sensory transduction; Transmembrane; Transmembrane helix;
KW Transport; Vision.
FT CHAIN 1..263
FT /note="Lens fiber major intrinsic protein"
FT /id="PRO_0000063913"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 9..32
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 33..38
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 62..67
FT /evidence="ECO:0000250"
FT INTRAMEM 68..78
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 79..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..107
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 108..126
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 148..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 160..176
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 177..183
FT /evidence="ECO:0000250"
FT INTRAMEM 184..194
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 195..200
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 220..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 227..237
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250"
FT REGION 240..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 34..38
FT /note="Important for formation of cell junction"
FT /evidence="ECO:0000250"
FT MOTIF 68..70
FT /note="NPA 1"
FT MOTIF 184..186
FT /note="NPA 2"
FT SITE 149
FT /note="Important for water channel gating"
FT /evidence="ECO:0000250"
FT SITE 246
FT /note="Interaction with BFSP1"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT SITE 250
FT /note="interaction with BFSP1"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT VARIANT 51
FT /note="A -> P (in LOP)"
FT /evidence="ECO:0000269|PubMed:8563764"
FT CONFLICT 30
FT /note="A -> S (in Ref. 2; AAC03168)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="A -> T (in Ref. 1; AAC52416)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="K -> N (in Ref. 2; AAC03168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 28193 MW; 3D141F7986A7ED16 CRC64;
MWELRSASFW RAIFAEFFAT LFYVFFGLGA SLRWAPGPLH VLQVALAFGL ALATLVQTVG
HISGAHVNPA VTFAFLVGSQ MSLLRAFCYI AAQLLGAVAG AAVLYSVTPP AVRGNLALNT
LHAGVSVGQA TTVEIFLTLQ FVLCIFATYD ERRNGRMGSV ALAVGFSLTL GHLFGMYYTG
AGMNPARSFA PAILTRNFSN HWVYWVGPII GGGLGSLLYD FLLFPRLKSV SERLSILKGA
RPSDSNGQPE GTGEPVELKT QAL
