LMIP_RAT
ID LMIP_RAT Reviewed; 173 AA.
AC P54825;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=7679355; DOI=10.1006/exer.1993.1006;
RA Kumar N.M., Jarvis L.J., Tenbroek E., Louis C.F.;
RT "Cloning and expression of a major rat lens membrane protein, MP20.";
RL Exp. Eye Res. 56:35-43(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=8137630; DOI=10.3109/02713689309033503;
RA Church R.L., Wang J.H.;
RT "The human lens fiber-cell intrinsic membrane protein MP19 gene: isolation
RT and sequence analysis.";
RL Curr. Eye Res. 12:1057-1065(1993).
RN [3]
RP PROTEIN SEQUENCE OF 1-31.
RC TISSUE=Lens;
RX PubMed=2584203; DOI=10.1016/s0021-9258(19)47205-0;
RA Louis C.F., Hur K.C., Galvan A.C., Tenbroek E.M., Jarvis L.J.,
RA Eccleston E.D., Howard J.B.;
RT "Identification of an 18,000-dalton protein in mammalian lens fiber cell
RT membranes.";
RL J. Biol. Chem. 264:19967-19973(1989).
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.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Eye lens specific.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. {ECO:0000305}.
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DR EMBL; S55224; AAB25334.1; -; mRNA.
DR EMBL; M87053; AAA41631.1; -; mRNA.
DR EMBL; L04191; AAB02792.1; -; mRNA.
DR PIR; A49182; A49182.
DR RefSeq; NP_446223.1; NM_053771.1.
DR AlphaFoldDB; P54825; -.
DR SMR; P54825; -.
DR STRING; 10116.ENSRNOP00000023858; -.
DR TCDB; 8.A.16.3.1; the ca(+) channel auxiliary subunit Gama1-Gama8 (ccaGama) family.
DR GlyGen; P54825; 3 sites.
DR PaxDb; P54825; -.
DR Ensembl; ENSRNOT00000023858; ENSRNOP00000023858; ENSRNOG00000017681.
DR GeneID; 114903; -.
DR KEGG; rno:114903; -.
DR UCSC; RGD:621482; rat.
DR CTD; 3982; -.
DR RGD; 621482; Lim2.
DR eggNOG; ENOG502QSWZ; Eukaryota.
DR GeneTree; ENSGT01050000244814; -.
DR HOGENOM; CLU_113769_0_0_1; -.
DR InParanoid; P54825; -.
DR OMA; IMAFAQQ; -.
DR OrthoDB; 1279397at2759; -.
DR PhylomeDB; P54825; -.
DR TreeFam; TF330587; -.
DR PRO; PR:P54825; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017681; Expressed in heart and 3 other tissues.
DR Genevisible; P54825; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
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 Direct protein sequencing; Disulfide bond; Eye lens protein; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..173
FT /note="Lens fiber membrane intrinsic protein"
FT /id="PRO_0000164666"
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 MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20274"
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 CONFLICT 28
FT /note="W -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 173 AA; 19637 MW; C41FA9D76618D57F CRC64;
MYSFMGGGLF CAWVGTILLV VATATDHWMQ YRLSGSFAHQ GLWRYCLGNK CFLQTESIAY
WNATRAFMIL SALCATSGII MGVLAFAQQS TFTRLSRPFS AGIMFFASTL FVLLALAIYT
GVTVSFLGRR FGDWRFSWSY ILGWVALLMT FFAGIFYMCA YRMHECRRLS TPR
