MIP_CHICK
ID MIP_CHICK Reviewed; 262 AA.
AC P28238; Q8QFW8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lens fiber major intrinsic protein;
DE AltName: Full=Aquaporin-0;
DE Short=AQP0;
DE AltName: Full=MIP26;
DE Short=MP26;
GN Name=MIP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH CX56
RP AND GJA8.
RC TISSUE=Embryonic lens;
RX PubMed=14762116; DOI=10.1242/jcs.00945;
RA Yu X.S., Jiang J.X.;
RT "Interaction of major intrinsic protein (aquaporin-0) with fiber connexins
RT in lens development.";
RL J. Cell Sci. 117:871-880(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 151-262.
RX PubMed=2373168; DOI=10.1016/0014-4835(90)90123-c;
RA Kodama R., Agata K., Mochii M., Eguchi G.;
RT "Partial amino acid sequence of the major intrinsic protein (MIP) of the
RT chicken lens deduced from the nucleotide sequence of a cDNA clone.";
RL Exp. Eye Res. 50:737-741(1990).
CC -!- FUNCTION: Water channel. May be responsible for regulating the
CC osmolarity of the lens. Interactions between homotetramers from
CC adjoining membranes may stabilize cell junctions in the eye lens core.
CC {ECO:0000250|UniProtKB:Q6J8I9}.
CC -!- SUBUNIT: Homotetramer. Homooctamer formed by head-to-head interaction
CC between homotetramers from adjoining membranes (By similarity). During
CC early stages of lens development, interacts through its C-terminal
CC region with Cx56 and GJA8/Cx45.6 (PubMed:14762116).
CC {ECO:0000250|UniProtKB:P06624, ECO:0000269|PubMed:14762116}.
CC -!- INTERACTION:
CC P28238; P36381: GJA8; NbExp=11; IntAct=EBI-867385, EBI-867402;
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 {ECO:0000269|PubMed:14762116}.
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 -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AY078179; AAL82573.1; -; mRNA.
DR PIR; A37203; A37203.
DR RefSeq; NP_989597.1; NM_204266.1.
DR AlphaFoldDB; P28238; -.
DR SMR; P28238; -.
DR IntAct; P28238; 1.
DR Ensembl; ENSGALT00000050001; ENSGALP00000049696; ENSGALG00000042119.
DR GeneID; 374124; -.
DR KEGG; gga:374124; -.
DR CTD; 4284; -.
DR VEuPathDB; HostDB:geneid_374124; -.
DR GeneTree; ENSGT00940000156260; -.
DR InParanoid; P28238; -.
DR OMA; WTPGPLH; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P28238; -.
DR PRO; PR:P28238; -.
DR Proteomes; UP000000539; 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:0005886; C:plasma membrane; 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:0002088; P:lens development in camera-type eye; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0006833; P:water transport; ISS:UniProtKB.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR023254; Aquaporin_6.
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; PR02018; AQUAPORIN6.
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; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..262
FT /note="Lens fiber major intrinsic protein"
FT /id="PRO_0000063916"
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..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 240..262
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"
SQ SEQUENCE 262 AA; 27072 MW; 5495332F0ECD95B2 CRC64;
MRELRSSSFW RAILAEFLGS LLYTLLGLGA SLRWAPGPHG VLGSALAFGL AQATLVQALG
HVSGGHINPA ITLAFLLASQ LSLPRALGYL LAQLLGALAG AGVLYGVTPA AVRGTLGLSA
LHPSVGPGQG TVVELLLTAQ FILCVFASFD DRHDGRPGSA ALPVGFSLAL GHLFGIPFTG
AGMNPARSFA PAVITRNFTN HWVFWAGPLL GAALAALLYE LALCPRARSM AERLAVLRGE
PPAAAPPPEP PAEPLELKTQ GL
