GLMP_PONAB
ID GLMP_PONAB Reviewed; 404 AA.
AC Q5RBU0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 38.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR858543; CAH90770.1; -; Transcribed_RNA.
DR AlphaFoldDB; Q5RBU0; -.
DR SMR; Q5RBU0; -.
DR Proteomes; UP000001595; Unplaced.
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: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 3: Inferred from homology;
KW Glycoprotein; Lysosome; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..404
FT /note="Glycosylated lysosomal membrane protein"
FT /evidence="ECO:0000305"
FT /id="PRO_0000284486"
FT TOPO_DOM 36..371
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..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 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 404 AA; 43569 MW; FA698617DA9F652C CRC64;
MRGSVERGWG WGHCASSPLL LWTLLLFAAP FGLLGEKTRQ LSLEVIPNWL GPLQNLLHIR
AVGTNSTLHY VWSSLGPLAV VMVATNTPHS TLSVNWSRLL SPEPDGGLMV LPKDSIQFSS
ALVFTRLLEF DSTNVSNTAA KPPGRPYPPY SLADFSWNNI TDSLPATLSA TFQGHPMNDP
TRTFANGSLA FRVQAFSRSS RPAQPPRLLH TADTCQLEVA LVGASPRGNH SLFGLEVATL
GQGPDCPSMQ EQHSIDDEYA PAVFQLDQLL WGSLPAGFAQ WRPVAYSQKP GGRESALPCQ
ASPLHPALAY SLPQSPIVRA FFGSQNNFCA FNLTFGASTG PGYWDQHYLS WNAPGCGLPS
SGRLVPTSPG HHGSALGAPG LMLLGGGLVL LLHHRKYSEY QSIN