MIP_LITPI
ID MIP_LITPI Reviewed; 263 AA.
AC Q06019;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Lens fiber major intrinsic protein;
DE AltName: Full=MIP26;
DE Short=MP26;
OS Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8404;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-263, AND PROTEIN SEQUENCE OF 1-4 AND 6-14.
RC TISSUE=Lens;
RX PubMed=7916707; DOI=10.1016/0378-1119(93)90410-5;
RA Austin L.R., Rice S.J., Baldo G.J., Lange A.J., Haspel H.C., Mathias R.T.;
RT "The cDNA sequence encoding the major intrinsic protein of frog lens.";
RL Gene 124:303-304(1993).
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.
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 -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; X56970; CAA40291.1; -; mRNA.
DR AlphaFoldDB; Q06019; -.
DR SMR; Q06019; -.
DR TCDB; 1.A.8.8.14; the major intrinsic protein (mip) family.
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: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: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 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; Direct protein sequencing; Eye lens protein;
KW Gap junction; Membrane; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..263
FT /note="Lens fiber major intrinsic protein"
FT /id="PRO_0000063917"
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 241..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"
SQ SEQUENCE 263 AA; 28383 MW; 9A12B84961E6C6EF CRC64;
MWEFRSFSFW RAVFAEFFGT MFYVFFGLGA SLKWAAGPAN VLVIALAFGL VLATMVQSIG
HVSGAHINPA VTFAFLIGSQ MSLFRAIFYI AAQLLGAVAG AAVLYGVTPA AIRGNLALNT
LHPGVSLGQA TTVEIFLTLQ FVLCIFATYD ERRNGRLGSV SLAIGFSLTL GHLFGLYYTG
ASMNPARSFA PAVLTRNFTN HWVYWVGPII GGALGGLVYD FILFPRMRGL SERLSILKGA
RPAEPEGQQE ATGEPIELKT QSL
