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LMIP_MOUSE
ID   LMIP_MOUSE              Reviewed;         173 AA.
AC   P56563; Q0VEF3; Q3TNV8; Q99PA6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Lens fiber membrane intrinsic protein;
DE   AltName: Full=MP17;
DE   AltName: Full=MP18;
DE   AltName: Full=MP19;
DE   AltName: Full=MP20;
GN   Name=Lim2;
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 [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=11290961;
RA   Zhou L., Li X.L., Church R.L.;
RT   "The mouse lens fiber-cell intrinsic membrane protein MP19 gene (Lim2) and
RT   granule membrane protein GMP-17 gene (Nkg7): isolation and sequence
RT   analysis of two neighboring genes.";
RL   Mol. Vis. 7:79-88(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Head;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   VARIANT TO3 VAL-15, AND DISEASE.
RX   PubMed=9238094;
RA   Steele E.C. Jr., Kerscher S., Lyon M.F., Glenister P.H., Favor J., Wang J.,
RA   Church R.L.;
RT   "Identification of a mutation in the MP19 gene, Lim2, in the cataractous
RT   mouse mutant To3.";
RL   Mol. Vis. 3:5-5(1997).
CC   -!- FUNCTION: Present in the thicker 16-17 nm junctions of mammalian lens
CC       fiber cells, where it may contribute to cell junctional organization.
CC       Acts as a receptor for calmodulin. May play an important role in both
CC       lens development and cataractogenesis.
CC   -!- SUBUNIT: Seems to be associated with itself or another lens membrane
CC       component via disulfide bonds. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DISEASE: Note=Defects in Lim2 are the cause of the cataractous mouse
CC       mutant with total opacity of lens 3 (To3). Mice heterozygous or
CC       homozygous for the To3 mutation have total opacity of the lens with a
CC       dense cataract. In addition, the To3/To3 homozygotes exhibit
CC       microphthalmia, abnormally small eyes. {ECO:0000269|PubMed:9238094}.
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. {ECO:0000305}.
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DR   EMBL; AF320075; AAK08062.1; -; Genomic_DNA.
DR   EMBL; AK029354; BAC26414.1; -; mRNA.
DR   EMBL; AK164958; BAE37979.1; -; mRNA.
DR   EMBL; BC119253; AAI19254.1; -; mRNA.
DR   EMBL; BC119255; AAI19256.1; -; mRNA.
DR   CCDS; CCDS21168.1; -.
DR   RefSeq; NP_808361.1; NM_177693.3.
DR   AlphaFoldDB; P56563; -.
DR   SMR; P56563; -.
DR   STRING; 10090.ENSMUSP00000004732; -.
DR   GlyGen; P56563; 3 sites.
DR   PhosphoSitePlus; P56563; -.
DR   PaxDb; P56563; -.
DR   PRIDE; P56563; -.
DR   ProteomicsDB; 290132; -.
DR   Antibodypedia; 46114; 139 antibodies from 22 providers.
DR   DNASU; 233187; -.
DR   Ensembl; ENSMUST00000004732; ENSMUSP00000004732; ENSMUSG00000118560.
DR   GeneID; 233187; -.
DR   KEGG; mmu:233187; -.
DR   UCSC; uc009gmp.1; mouse.
DR   CTD; 3982; -.
DR   MGI; MGI:104698; Lim2.
DR   VEuPathDB; HostDB:ENSMUSG00000118560; -.
DR   eggNOG; ENOG502QSWZ; Eukaryota.
DR   GeneTree; ENSGT01050000244814; -.
DR   HOGENOM; CLU_113769_0_0_1; -.
DR   InParanoid; P56563; -.
DR   OMA; IMAFAQQ; -.
DR   OrthoDB; 1279397at2759; -.
DR   PhylomeDB; P56563; -.
DR   TreeFam; TF330587; -.
DR   BioGRID-ORCS; 233187; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Lhx2; mouse.
DR   PRO; PR:P56563; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P56563; protein.
DR   Bgee; ENSMUSG00000118560; Expressed in lens of camera-type eye and 8 other tissues.
DR   Genevisible; P56563; MM.
DR   GO; GO:0005923; C:bicellular tight junction; TAS:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0005212; F:structural constituent of eye lens; TAS:MGI.
DR   GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR   GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR   InterPro; IPR003935; LMIP.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR004032; PMP22_EMP_MP20.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01453; EPMEMFAMILY.
DR   PRINTS; PR01457; LENSMEMPROT.
DR   PROSITE; PS01221; PMP22_1; 1.
DR   PROSITE; PS01222; PMP22_2; 1.
PE   1: Evidence at protein level;
KW   Disease variant; Disulfide bond; Eye lens protein; Glycoprotein; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..173
FT                   /note="Lens fiber membrane intrinsic protein"
FT                   /id="PRO_0000164665"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..66
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..140
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..173
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         171
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P20274"
FT   CARBOHYD        43
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P20274"
FT   CARBOHYD        61
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P20274"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         15
FT                   /note="G -> V (in To3)"
FT                   /evidence="ECO:0000269|PubMed:9238094"
SQ   SEQUENCE   173 AA;  19621 MW;  C41FA9CF0618D57F CRC64;
     MYSFMGGGLF CAWVGTILLV VATATDHWMQ YRLSGSFAHQ GLWRYCLGNK CFLQTESIAY
     WNATRAFMIL SALCATSGII MGVLAFAQQS TFTRLSRPFS AGIMFFASTL FVLLALAIYT
     GVTVSFLGRR FGDWRFSWSY ILGWVALLMT FFAGIFYMCA YRMHECRRLA TPR
 
 
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