LMIP_BOVIN
ID LMIP_BOVIN Reviewed; 173 AA.
AC P20274;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Lens fiber membrane intrinsic protein;
DE AltName: Full=MP18;
DE AltName: Full=MP19;
DE AltName: Full=MP20;
DE AltName: Full=MP21;
DE AltName: Full=MP23;
GN Name=LIM2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2276272; DOI=10.3109/02713689009069931;
RA Gutekunst K.A., Rao G.N., Church R.L.;
RT "Molecular cloning and complete nucleotide sequence of the cDNA encoding a
RT bovine lens intrinsic membrane protein (MP19).";
RL Curr. Eye Res. 9:955-961(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-20.
RC TISSUE=Lens;
RX PubMed=2473922; DOI=10.1016/0014-5793(89)80781-1;
RA Rao G.N., Gutekunst K.A., Church R.L.;
RT "Bovine lens 23, 21 and 19 kDa intrinsic membrane proteins have an
RT identical amino-terminal amino acid sequence.";
RL FEBS Lett. 250:483-486(1989).
RN [3]
RP PROTEIN SEQUENCE OF 1-23.
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).
RN [4]
RP PHOSPHORYLATION AT SER-170 AND THR-171, GLYCOSYLATION AT TRP-43 AND TRP-61,
RP AND LACK OF GLYCOSYLATION AT ASN-62 AND TRP-134.
RX PubMed=15671292; DOI=10.1167/iovs.04-0894;
RA Ervin L.A., Ball L.E., Crouch R.K., Schey K.L.;
RT "Phosphorylation and glycosylation of bovine lens MP20.";
RL Invest. Ophthalmol. Vis. Sci. 46:627-635(2005).
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 -!- DEVELOPMENTAL STAGE: Higher expression in lenses from pre-natal (1-5
CC months gestation) than those from postnatal (4-6 months) calves.
CC -!- PTM: Predominantly monophosphorylated on Ser-170. Only about 15%
CC diphosphorylated on both Ser-170 and Thr-171.
CC -!- PTM: C-glycosylated. Trp-43 is more extensively C-glycosylated than
CC Trp-61. C-glycosylation may be involved in membrane trafficking.
CC {ECO:0000269|PubMed:15671292}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. {ECO:0000305}.
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DR EMBL; L04188; AAA30621.1; -; mRNA.
DR PIR; A48300; A48300.
DR RefSeq; NP_776527.1; NM_174102.2.
DR AlphaFoldDB; P20274; -.
DR SMR; P20274; -.
DR STRING; 9913.ENSBTAP00000004191; -.
DR iPTMnet; P20274; -.
DR SwissPalm; P20274; -.
DR PaxDb; P20274; -.
DR PRIDE; P20274; -.
DR Ensembl; ENSBTAT00000004191; ENSBTAP00000004191; ENSBTAG00000003231.
DR GeneID; 281282; -.
DR KEGG; bta:281282; -.
DR CTD; 3982; -.
DR VEuPathDB; HostDB:ENSBTAG00000003231; -.
DR VGNC; VGNC:30885; LIM2.
DR eggNOG; ENOG502QSWZ; Eukaryota.
DR GeneTree; ENSGT01050000244814; -.
DR HOGENOM; CLU_113769_0_0_1; -.
DR InParanoid; P20274; -.
DR OMA; IMAFAQQ; -.
DR OrthoDB; 1279397at2759; -.
DR TreeFam; TF330587; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000003231; Expressed in pigment epithelium of eye and 28 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
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_0000164663"
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 SITE 62
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:15671292"
FT SITE 134
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:15671292"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15671292"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15671292"
FT CARBOHYD 43
FT /note="C-linked (Man) tryptophan; partial"
FT /evidence="ECO:0000269|PubMed:15671292"
FT CARBOHYD 61
FT /note="C-linked (Man) tryptophan; partial"
FT /evidence="ECO:0000269|PubMed:15671292"
SQ SEQUENCE 173 AA; 19684 MW; F5793067F95757CE CRC64;
MYSFMGGGLF CAWVGTILLV VATATDHWMQ YRLSGAFAHQ GLWRYCLGTK CYLQTESIAY
WNATRAFMIL SSLCATSGII MGIVAFAQQP TFTRLSRPFS AGIMFFASTF FVLLALAIYT
GVTVSFLGRR FGDWRFSWSY ILGWVALLMT FFAGIFYMCA YRMHECRRLS TPR
