MIP_CAVPO
ID MIP_CAVPO Reviewed; 263 AA.
AC Q6RZ07;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 02-JUN-2021, entry version 83.
DE RecName: Full=Lens fiber major intrinsic protein;
DE AltName: Full=Aquaporin-0;
GN Name=MIP; Synonyms=AQP0;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP PHOSPHORYLATION AT SER-235, TISSUE SPECIFICITY, AND DEAMIDATION AT ASN-245
RP AND ASN-246.
RX PubMed=15064681;
RA Han J., Little M., David L.L., Giblin F.J., Schey K.L.;
RT "Sequence and peptide map of guinea pig aquaporin 0.";
RL Mol. Vis. 10:215-222(2004).
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: Detected in eye lens (at protein level).
CC {ECO:0000269|PubMed:15064681}.
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 -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AY485151; AAR37021.1; -; mRNA.
DR STRING; 10141.ENSCPOP00000002132; -.
DR iPTMnet; Q6RZ07; -.
DR eggNOG; KOG0223; Eukaryota.
DR InParanoid; Q6RZ07; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
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:0006833; P:water transport; ISS:UniProtKB.
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 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; Sensory transduction;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..263
FT /note="Lens fiber major intrinsic protein"
FT /id="PRO_0000063911"
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 238..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000269|PubMed:15064681"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06624"
FT MOD_RES 245
FT /note="Deamidated asparagine; by deterioration"
FT /evidence="ECO:0000269|PubMed:15064681"
FT MOD_RES 246
FT /note="Deamidated asparagine; by deterioration"
FT /evidence="ECO:0000269|PubMed:15064681"
SQ SEQUENCE 263 AA; 28369 MW; DCC8D03F80E67E9B CRC64;
MWELRSASFW RAIFAEFFAT LFYVFFGLGA SLRWAPGPLH VLQVALAFGL ALAXLVQTVG
HISGAHVNPA VTFXFLVGSQ MSLLRAFCYM AAQLLGAVAG AAVLYSVTPP AVRGNLALNT
LHAGVSVXQA TTVEIFLTLQ FVLCIFATYD ERRNGRLGSV ALAVGFSLTL GHLFGMYYTG
AGMNPARSFA PAILTRNFTN HWVYWVGPII GGGLGSLLYD FLLFPRLKSV SERLSILKGT
RPSDNNGQPE GTGEPVELKT QAL
