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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
 
 
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