MIP_RAT
ID MIP_RAT Reviewed; 261 AA.
AC P09011;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Lens fiber major intrinsic protein;
DE AltName: Full=Aquaporin-0;
DE AltName: Full=MIP26;
DE Short=MP26;
DE Flags: Fragment;
GN Name=Mip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Eye;
RX PubMed=2377471; DOI=10.1093/nar/18.14.4256;
RA Kent N.A., Shiels A.;
RT "Nucleotide and derived amino-acid sequence of the major intrinsic protein
RT of rat eye-lens.";
RL Nucleic Acids Res. 18:4256-4256(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF ASN-244.
RX PubMed=7848273; DOI=10.1042/bj3050753;
RA Dilsiz N., Crabbe M.J.C.;
RT "Heterologous expression in Escherichia coli of native and mutant forms of
RT the major intrinsic protein of rat eye lens (MIP26).";
RL Biochem. J. 305:753-759(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 132-261.
RC STRAIN=Sprague-Dawley;
RX PubMed=3174458; DOI=10.1093/nar/16.19.9348;
RA Shiels A., Kent N.A., McHale M., Bangham J.A.;
RT "Homology of MIP26 to Nod26.";
RL Nucleic Acids Res. 16:9348-9348(1988).
RN [4]
RP PHOSPHORYLATION AT SER-233.
RX PubMed=10067969;
RA Schey K.L., Fowler J.G., Shearer T.R., David L.;
RT "Modifications to rat lens major intrinsic protein in selenite-induced
RT cataract.";
RL Invest. Ophthalmol. Vis. Sci. 40:657-667(1999).
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 Lys-236. The acyl modifications, in decreasing
CC order of ion abundance, are: oleoyl (C18:1) > palmitoyl (C16:0) >
CC stearoyl (C18:0) > eicosenoyl (C20:1) > dihomo-gamma-linolenoyl (C20:3)
CC > palmitoleoyl (C16:1) > eicosadienoyl (C20:2).
CC {ECO:0000250|UniProtKB:P30301}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; X12514; CAA31035.1; -; mRNA.
DR EMBL; X53052; CAA37219.1; -; mRNA.
DR PIR; S01439; S01439.
DR PIR; S53423; S53423.
DR AlphaFoldDB; P09011; -.
DR SMR; P09011; -.
DR STRING; 10116.ENSRNOP00000004223; -.
DR iPTMnet; P09011; -.
DR PhosphoSitePlus; P09011; -.
DR PaxDb; P09011; -.
DR UCSC; RGD:3090; rat.
DR RGD; 3090; Mip.
DR eggNOG; KOG0223; Eukaryota.
DR InParanoid; P09011; -.
DR PhylomeDB; P09011; -.
DR Reactome; R-RNO-432047; Passive transport by Aquaporins.
DR Proteomes; UP000002494; Unplaced.
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; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; ISO:RGD.
DR GO; GO:0015250; F:water channel activity; IDA:RGD.
DR GO; GO:0015722; P:canalicular bile acid transport; IDA:RGD.
DR GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
DR GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
DR GO; GO:0006833; P:water transport; IDA:RGD.
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; Eye lens protein; Gap junction; Lipoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN <1..261
FT /note="Lens fiber major intrinsic protein"
FT /id="PRO_0000063914"
FT TOPO_DOM <1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 31..36
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 60..65
FT /evidence="ECO:0000250"
FT INTRAMEM 66..76
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 77..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 83..105
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 106..124
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 146..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 158..174
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 175..181
FT /evidence="ECO:0000250"
FT INTRAMEM 182..192
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 193..198
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 218..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 225..235
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250"
FT REGION 238..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 66..68
FT /note="NPA 1"
FT MOTIF 182..184
FT /note="NPA 2"
FT SITE 147
FT /note="Important for water channel gating"
FT /evidence="ECO:0000250"
FT SITE 244
FT /note="Interaction with BFSP1"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT SITE 248
FT /note="interaction with BFSP1"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10067969"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT MUTAGEN 244
FT /note="N->D: No effects."
FT /evidence="ECO:0000269|PubMed:7848273"
FT CONFLICT 132..133
FT /note="EI -> RF (in Ref. 2; CAA31035)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 261 AA; 27891 MW; 703C3FDBA113AA95 CRC64;
ELRSASFWRA IFAEFFATLF YVFFGLGSSL RWAPGPLHVL QVALAFGLAL ATLVQTVGHI
SGAHVNPAVT FAFLVGSQMS LLRAFCYIAA QLLGAVAGAA VLYSVTPPAV RGNLALNTLH
AGVSVGQATT VEIFLTLQFV LCIFATYDER RNGRMGSVAL AVGFSLTLGH LFGMYYTGAG
MNPARSFAPA ILTRNFSNHW VYWVGPIIGG GLGSLLYDFL LFPRLKSVSE RLSILKGARP
SDSNGQPEGT GEPVELKTQA L
