GLMP_BOVIN
ID GLMP_BOVIN Reviewed; 404 AA.
AC Q0P5L7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Glycosylated lysosomal membrane protein {ECO:0000250|UniProtKB:Q8WWB7};
DE AltName: Full=Lysosomal protein NCU-G1 {ECO:0000250|UniProtKB:Q8WWB7};
DE Flags: Precursor;
GN Name=GLMP {ECO:0000250|UniProtKB:Q8WWB7};
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required to protect lysosomal transporter MFSD1 from
CC lysosomal proteolysis and for MFSD1 lysosomal localization.
CC {ECO:0000250|UniProtKB:Q9JHJ3}.
CC -!- SUBUNIT: Interacts (via lumenal domain) with lysosomal protein MFSD1;
CC the interaction starts while both proteins are still in the endoplasmic
CC reticulum and is required for stability and lysosomal localization of
CC MFSD1. {ECO:0000250|UniProtKB:Q9JHJ3}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9JHJ3};
CC Single-pass type I membrane protein {ECO:0000255}; Lumenal side
CC {ECO:0000305}.
CC -!- PTM: Highly N-glycosylated. N-glycosylation is essential for GLMP
CC stability and for MFSD1 lysosomal localization.
CC {ECO:0000250|UniProtKB:Q9JHJ3}.
CC -!- SIMILARITY: Belongs to the GLMP family. {ECO:0000305}.
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DR EMBL; BC119876; AAI19877.1; -; mRNA.
DR RefSeq; NP_001098946.1; NM_001105476.1.
DR AlphaFoldDB; Q0P5L7; -.
DR SMR; Q0P5L7; -.
DR STRING; 9913.ENSBTAP00000008351; -.
DR PaxDb; Q0P5L7; -.
DR PRIDE; Q0P5L7; -.
DR Ensembl; ENSBTAT00000008351; ENSBTAP00000008351; ENSBTAG00000006364.
DR GeneID; 100125876; -.
DR KEGG; bta:100125876; -.
DR CTD; 112770; -.
DR VEuPathDB; HostDB:ENSBTAG00000006364; -.
DR VGNC; VGNC:29409; GLMP.
DR eggNOG; ENOG502QSBM; Eukaryota.
DR GeneTree; ENSGT00390000005131; -.
DR HOGENOM; CLU_040225_0_0_1; -.
DR InParanoid; Q0P5L7; -.
DR OMA; TLHYLWD; -.
DR OrthoDB; 562253at2759; -.
DR TreeFam; TF324431; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000006364; Expressed in digestive system secreted substance and 105 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR InterPro; IPR029382; NCU-G1.
DR PANTHER; PTHR31981; PTHR31981; 1.
DR Pfam; PF15065; NCU-G1; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Lysosome; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..404
FT /note="Glycosylated lysosomal membrane protein"
FT /evidence="ECO:0000305"
FT /id="PRO_0000284483"
FT TOPO_DOM 27..370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 400..404
FT /note="Lysosomal targeting motif"
FT /evidence="ECO:0000250|UniProtKB:Q9JHJ3"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 404 AA; 43531 MW; 298779EA45A56C53 CRC64;
MSGYEKPSRG WGFCALSPVL LSLLMAAPLG LLGEETRQVS LKVISNRLDF SQNLLHIRAV
GTNSTLHYVW SSLGPPAVLL VATNTPNSTL SVNWSLLLSS DPDGGLMVLP EESIQFSSAL
VFTRLFEFDS TNMSDAASRP LGKSYPPYSL ANFSWNNITD SLDPATLSAT FRGHPIRDPT
GAFTNGSLAF RVQAFSTSGR PAQPPRLLHS ADTCQLEVAL VGASPRGNRS LFGLEVATLG
QGPGCPSMQE QHSIDDEYTP AVFQLDQLLW GSLPSGFMQW RPVAFSQKRG SRDSAMPCQS
SPLHPTLAYL LPQSPIVRAF FKTQDHSCAF NLTFGASTGP GYWDQHYLSW SVLLGVGTPP
VDALSPLVLG IMAVALGAPA LMLLAGGLFL LLGRKRDSEY QSIN