ID   GLMPB_XENLA             Reviewed;         404 AA.
AC   A8WH34; A0JMV6;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Glycosylated lysosomal membrane protein B {ECO:0000250|UniProtKB:Q8WWB7};
DE   AltName: Full=Lysosomal protein NCU-G1-B {ECO:0000250|UniProtKB:Q8WWB7};
DE   Flags: Precursor;
GN   Name=glmp-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Intestine, and Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2007) 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   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9JHJ3};
CC       Single-pass type I membrane protein {ECO:0000255}; Lumenal side
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GLMP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI26022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI54957.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC126021; AAI26022.1; ALT_INIT; mRNA.
DR   EMBL; BC154956; AAI54957.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; A8WH34; -.
DR   SMR; A8WH34; -.
DR   Proteomes; UP000186698; Genome assembly.
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   2: Evidence at transcript level;
KW   Glycoprotein; Lysosome; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..404
FT                   /note="Glycosylated lysosomal membrane protein B"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000381839"
FT   TOPO_DOM        25..364
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        386..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        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        169
FT                   /note="T -> A (in Ref. 1; AAI26022)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="R -> S (in Ref. 1; AAI26022)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   404 AA;  44427 MW;  1F8CE5D2437B14B4 CRC64;
     MSCTRGWRLI LLGLLCVGLL GTRGQDESRK VSVQYNPGSS DTSVNVVHVR AVGDGNTIHY
     VWSTLGTPTV LLIYTHSETS QLQVNWTKLL SPAPQGALRV EPEESVSYAT ALLFTRIFEY
     QDVNNTANFS GTDEKYFYPP YNLSEFLWEN ANATVNATSL SANLTGSNTT DPSGSFHNGS
     VSFRISAYNT SGRDSSPPRL RHTANCTKLE FLVSGVRPRG NNSRFALEMV TIEKEGRRKM
     KSVLSIDDEY TPTIFEMMQL VAVAPNSSHA RGFLQWKSVA YGSPSGSRAD LLPCQLYPLQ
     PLNATFTATS IAHAYFGDDL ADAYNLEAFN ISFGIADGDF YDKHEFLSWS ALIGYGDPPR
     DSFSILVICI MAVALGTPLL LLIIGTVLVT AVRHKVYPNY QPIN