ID A0A091CMA1_FUKDA Unreviewed; 183 AA.
AC A0A091CMA1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Lens fiber membrane intrinsic protein {ECO:0000256|RuleBase:RU363088};
GN ORFNames=H920_20067 {ECO:0000313|EMBL:KFO18548.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO18548.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO18548.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO18548.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU363088}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU363088}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363088}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family.
CC {ECO:0000256|ARBA:ARBA00006864, ECO:0000256|RuleBase:RU363088}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU363088}.
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DR EMBL; KN125364; KFO18548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CMA1; -.
DR STRING; 885580.ENSFDAP00000003314; -.
DR eggNOG; ENOG502QSWZ; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:InterPro.
DR Gene3D; 1.20.140.150; -; 1.
DR InterPro; IPR003935; LMIP.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR004032; PMP22_EMP_MP20.
DR PANTHER; PTHR10671; EPITHELIAL MEMBRANE PROTEIN-RELATED; 1.
DR PANTHER; PTHR10671:SF9; LENS FIBER MEMBRANE INTRINSIC PROTEIN; 1.
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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363088};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363088};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363088}.
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363088"
FT TRANSMEM 99..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363088"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363088"
SQ SEQUENCE 183 AA; 20482 MW; 6684AB380F7CD089 CRC64;
MYSFMGGGLF CAWVGTVLLV VATATDHWMQ YRLSGAFAHQ GLWRYCLGHK CYLQTESIAY
WNATRAFMIL STLCATLGII MGVLAFAQQS TFTRLSRPLS AAIMFSVSAL FVLLALAVYT
GVTISFLGRR FGDWRFSWSY ILGWVALLLT FLSVANPEEL AQCIIVIQVL FRVIFQSTEV
EIS
//
