ID   G137B_XENLA             Reviewed;         372 AA.
AC   Q6DCW7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Integral membrane protein GPR137B;
GN   Name=gpr137b;
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=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lysosomal integral membrane protein that regulates the
CC       localization and activity of mTORC1, a signaling complex promoting cell
CC       growth in response to growth factors, energy levels, and amino acids.
CC       Interacts with Rag GTPases and increases the lysosomial localization
CC       and activity of Rag GTPases and thereby regulates mTORC1 translocation
CC       and activity in lysosome. Involved in the regulation of lysosomal
CC       morphology and autophagy (By similarity). Acts also as a negative
CC       regulator of osteoclast activity (By similarity).
CC       {ECO:0000250|UniProtKB:O60478, ECO:0000250|UniProtKB:Q8BNQ3}.
CC   -!- FUNCTION: Acts also as a negative regulator of osteoclast activity.
CC       {ECO:0000250|UniProtKB:Q8BNQ3}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O60478};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the GPR137 family. {ECO:0000305}.
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DR   EMBL; BC077871; AAH77871.1; -; mRNA.
DR   RefSeq; NP_001086993.2; NM_001093524.1.
DR   AlphaFoldDB; Q6DCW7; -.
DR   DNASU; 446828; -.
DR   GeneID; 446828; -.
DR   KEGG; xla:446828; -.
DR   CTD; 446828; -.
DR   Xenbase; XB-GENE-987554; gpr137b.L.
DR   OrthoDB; 1399303at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 446828; Expressed in spleen and 18 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0045779; P:negative regulation of bone resorption; ISS:UniProtKB.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISS:UniProtKB.
DR   GO; GO:0150032; P:positive regulation of protein localization to lysosome; ISS:UniProtKB.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; ISS:UniProtKB.
DR   InterPro; IPR029723; GPR137.
DR   PANTHER; PTHR15146; PTHR15146; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Glycoprotein; Lysosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..372
FT                   /note="Integral membrane protein GPR137B"
FT                   /id="PRO_0000304802"
FT   TOPO_DOM        1..32
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        33..53
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        65..85
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..93
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        94..114
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        145..165
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..173
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        174..194
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..222
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        223..243
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..276
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        277..297
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   372 AA;  42728 MW;  4BC8727F72E9ECED CRC64;
     MESPAWDATK NDSLPPTLTP AVPPYVKLGL TTVYTIFYLL LFAFVYVQLW LVLHYKHKRF
     SYQTVFLFLC LLWASLRAVL FSFYFRNFVE ANRLGAFTFW LLYCFPVCLQ FFTLTLMNLY
     FARVIYKAKS KYLPELIKYR LPLYLAFLVI SLLFLVVNLT CAILVKTDYA ETKVIVSIRV
     AINDTLFVLC AVSLSVCLYK ISKMSLAGVY LESKGSSVCQ VTCIGVTVIL LYTSRACYNL
     VVLSLSDSRY SSFDYDWYNV SDQADLKCKL GDAGYVVFGI ILFIWELFPT SLVVYFFRVR
     NSAQDMTNPG MVPGFNPRSY FFDNPRRYDS DDDLAWNITP QSLQGSFGPD YFDWGNRNSF
     GSQTGSLQRD ST