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G137A_MOUSE
ID   G137A_MOUSE             Reviewed;         396 AA.
AC   Q80ZU9; Q80UB6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Integral membrane protein GPR137;
DE   AltName: Full=Transmembrane 7 superfamily member 1-like 1 protein;
GN   Name=Gpr137; Synonyms=Tm7sf1l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-86.
RX   PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=28975893; DOI=10.7554/elife.28366;
RA   Mager L.F., Koelzer V.H., Stuber R., Thoo L., Keller I., Koeck I.,
RA   Langenegger M., Simillion C., Pfister S.P., Faderl M., Genitsch V.,
RA   Tcymbarevich I., Juillerat P., Li X., Xia Y., Karamitopoulou E., Lyck R.,
RA   Zlobec I., Hapfelmeier S., Bruggmann R., McCoy K.D., Macpherson A.J.,
RA   Mueller C., Beutler B., Krebs P.;
RT   "The ESRP1-GPR137 axis contributes to intestinal pathogenesis.";
RL   Elife 6:0-0(2017).
CC   -!- FUNCTION: Lysosomal integral membrane protein that may regulate MTORC1
CC       complex translocation to lysosomes. May play a role in autophagy.
CC       {ECO:0000250|UniProtKB:Q96N19}.
CC   -!- FUNCTION: May activate Wnt/beta-catenin signaling to modulate
CC       epithelial cell function. {ECO:0000269|PubMed:28975893}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96N19};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the GPR137 family. {ECO:0000305}.
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DR   EMBL; BC048078; AAH48078.1; -; mRNA.
DR   EMBL; AY255566; AAO85078.1; -; mRNA.
DR   CCDS; CCDS29512.1; -.
DR   RefSeq; NP_001170831.1; NM_001177360.1.
DR   RefSeq; NP_997103.1; NM_207220.2.
DR   AlphaFoldDB; Q80ZU9; -.
DR   STRING; 10090.ENSMUSP00000130969; -.
DR   GlyGen; Q80ZU9; 2 sites.
DR   iPTMnet; Q80ZU9; -.
DR   PhosphoSitePlus; Q80ZU9; -.
DR   MaxQB; Q80ZU9; -.
DR   PaxDb; Q80ZU9; -.
DR   PRIDE; Q80ZU9; -.
DR   ProteomicsDB; 273402; -.
DR   Antibodypedia; 15349; 194 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000025909; ENSMUSP00000025909; ENSMUSG00000024958.
DR   Ensembl; ENSMUST00000166115; ENSMUSP00000130969; ENSMUSG00000024958.
DR   Ensembl; ENSMUST00000237934; ENSMUSP00000158264; ENSMUSG00000024958.
DR   GeneID; 107173; -.
DR   KEGG; mmu:107173; -.
DR   UCSC; uc008gjk.2; mouse.
DR   CTD; 56834; -.
DR   MGI; MGI:2147529; Gpr137.
DR   VEuPathDB; HostDB:ENSMUSG00000024958; -.
DR   eggNOG; ENOG502QQ83; Eukaryota.
DR   GeneTree; ENSGT00940000153986; -.
DR   InParanoid; Q80ZU9; -.
DR   OMA; RSYFFDH; -.
DR   OrthoDB; 1399303at2759; -.
DR   PhylomeDB; Q80ZU9; -.
DR   TreeFam; TF329003; -.
DR   BioGRID-ORCS; 107173; 3 hits in 72 CRISPR screens.
DR   PRO; PR:Q80ZU9; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q80ZU9; protein.
DR   Bgee; ENSMUSG00000024958; Expressed in primary visual cortex and 201 other tissues.
DR   ExpressionAtlas; Q80ZU9; baseline and differential.
DR   Genevisible; Q80ZU9; MM.
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; IBA:GO_Central.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; IBA:GO_Central.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR   GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
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..396
FT                   /note="Integral membrane protein GPR137"
FT                   /id="PRO_0000269997"
FT   TOPO_DOM        1..31
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        32..52
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..60
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        61..81
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..89
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        90..110
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        141..161
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..175
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        176..196
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        218..242
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..274
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        275..295
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..396
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   396 AA;  43574 MW;  4CA45B03848952BF CRC64;
     MESNLSGLVP AAGLVPALPP TVTLGLTAAY TALYALLFFS VYAQLWLVLL YGHKRLSYQT
     VFLALCLLWA ALRTTLFSFY FRDTPRANRL GPLPFWLLYC CPVCLQFFTL TLMNLYFVQV
     VFKAKAKRRP EMSRGLLAVR GAFVGASLLF LLVNVLCAVL SRQRQAQPWV LLLVRVLVSD
     SLFVICALSL AACLCLVARR APSTSIYLEA KGTSVCQAAA IGGAMVLLYA SRACYNLAAL
     ALAPRSRLDA FDYDWYNVSD QADLVNDLGN KGYLVFGLIL FVWELLPTTL LVGFFRVHRP
     PQDLSTSRIL NGQVFGSRSY FFDRAGHCED EGCSWEHSRS ESTSMSGSLG SGSWYGAIGR
     EPGWGGASQT RTTPLLFSQV PGPGSHHHSL YSTPQT
 
 
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