G137B_HUMAN
ID G137B_HUMAN Reviewed; 399 AA.
AC O60478; Q53EK7; Q5TAE6; Q6FHI3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Integral membrane protein GPR137B;
DE AltName: Full=Transmembrane 7 superfamily member 1 protein;
GN Name=GPR137B; Synonyms=TM7SF1 {ECO:0000303|PubMed:22729905};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9521871; DOI=10.1006/geno.1997.5170;
RA Spangenberg C., Winterpacht A., Zabel B.U., Lobbert R.W.;
RT "Cloning and characterization of a novel gene (TM7SF1) encoding a putative
RT seven-pass transmembrane protein that is upregulated during kidney
RT development.";
RL Genomics 48:178-185(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22729905; DOI=10.1007/s11033-012-1755-0;
RA Gao J., Xia L., Lu M., Zhang B., Chen Y., Xu R., Wang L.;
RT "TM7SF1 (GPR137B): a novel lysosome integral membrane protein.";
RL Mol. Biol. Rep. 39:8883-8889(2012).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH RRAGA AND MTOR, AND FUNCTION.
RX PubMed=31036939; DOI=10.1038/s41556-019-0321-6;
RA Gan L., Seki A., Shen K., Iyer H., Han K., Hayer A., Wollman R., Ge X.,
RA Lin J.R., Dey G., Talbot W.S., Meyer T.;
RT "The lysosomal GPCR-like protein GPR137B regulates Rag and mTORC1
RT localization and activity.";
RL Nat. Cell Biol. 21:614-626(2019).
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 (PubMed:31036939). Interacts with Rag GTPases and increases the
CC lysosomial localization and activity of Rag GTPases and thereby
CC regulates mTORC1 translocation and activity in lysosome
CC (PubMed:31036939). Involved in the regulation of lysosomal morphology
CC and autophagy (PubMed:31036939). {ECO:0000269|PubMed:31036939}.
CC -!- FUNCTION: Acts also as a negative regulator of osteoclast activity (By
CC similarity). Involved in interleukin-4-induced M2 macrophage
CC polarization (By similarity). {ECO:0000250|UniProtKB:Q8BNQ3}.
CC -!- SUBUNIT: Interaction with RRAGA; increases RRAGA recruitment to
CC lysosomes (PubMed:31036939). Interacts with MTOR; this interaction is
CC amino acid sensitive (PubMed:31036939). {ECO:0000269|PubMed:31036939}.
CC -!- INTERACTION:
CC O60478; Q13049: TRIM32; NbExp=3; IntAct=EBI-18945347, EBI-742790;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:22729905,
CC ECO:0000269|PubMed:31036939}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22729905}. Note=Colocalized with MTOR in lysosome
CC after amino acid stimulation. {ECO:0000269|PubMed:31036939}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, heart, brain and placenta.
CC {ECO:0000269|PubMed:9521871}.
CC -!- SIMILARITY: Belongs to the GPR137 family. {ECO:0000305}.
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DR EMBL; AF027826; AAC39669.1; -; mRNA.
DR EMBL; AY242135; AAO92302.1; -; mRNA.
DR EMBL; CR541770; CAG46569.1; -; mRNA.
DR EMBL; AK223632; BAD97352.1; -; mRNA.
DR EMBL; AL122018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW70043.1; -; Genomic_DNA.
DR EMBL; BC012100; AAH12100.1; -; mRNA.
DR CCDS; CCDS1609.1; -.
DR RefSeq; NP_003263.1; NM_003272.3.
DR AlphaFoldDB; O60478; -.
DR BioGRID; 112962; 9.
DR IntAct; O60478; 9.
DR STRING; 9606.ENSP00000355551; -.
DR TCDB; 9.B.123.1.1; the lysosomal 7-tms (tm7sf1) family.
DR GlyGen; O60478; 3 sites.
DR iPTMnet; O60478; -.
DR PhosphoSitePlus; O60478; -.
DR BioMuta; GPR137B; -.
DR EPD; O60478; -.
DR jPOST; O60478; -.
DR MassIVE; O60478; -.
DR PaxDb; O60478; -.
DR PeptideAtlas; O60478; -.
DR PRIDE; O60478; -.
DR ProteomicsDB; 49420; -.
DR Antibodypedia; 20812; 133 antibodies from 29 providers.
DR DNASU; 7107; -.
DR Ensembl; ENST00000366592.8; ENSP00000355551.3; ENSG00000077585.14.
DR GeneID; 7107; -.
DR KEGG; hsa:7107; -.
DR MANE-Select; ENST00000366592.8; ENSP00000355551.3; NM_003272.4; NP_003263.1.
DR UCSC; uc001hxq.3; human.
DR CTD; 7107; -.
DR DisGeNET; 7107; -.
DR GeneCards; GPR137B; -.
DR HGNC; HGNC:11862; GPR137B.
DR HPA; ENSG00000077585; Tissue enhanced (retina).
DR MIM; 604658; gene.
DR neXtProt; NX_O60478; -.
DR OpenTargets; ENSG00000077585; -.
DR PharmGKB; PA36563; -.
DR VEuPathDB; HostDB:ENSG00000077585; -.
DR eggNOG; ENOG502QQ83; Eukaryota.
DR GeneTree; ENSGT00940000153986; -.
DR HOGENOM; CLU_050057_0_0_1; -.
DR InParanoid; O60478; -.
DR OMA; WNISPQG; -.
DR OrthoDB; 1399303at2759; -.
DR PhylomeDB; O60478; -.
DR TreeFam; TF329003; -.
DR PathwayCommons; O60478; -.
DR SignaLink; O60478; -.
DR BioGRID-ORCS; 7107; 4 hits in 1058 CRISPR screens.
DR ChiTaRS; GPR137B; human.
DR GenomeRNAi; 7107; -.
DR Pharos; O60478; Tbio.
DR PRO; PR:O60478; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60478; protein.
DR Bgee; ENSG00000077585; Expressed in pigmented layer of retina and 197 other tissues.
DR ExpressionAtlas; O60478; baseline and differential.
DR Genevisible; O60478; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
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; IMP:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0043030; P:regulation of macrophage activation; ISS:UniProtKB.
DR InterPro; IPR029723; GPR137.
DR PANTHER; PTHR15146; PTHR15146; 1.
PE 1: Evidence at protein level;
KW Autophagy; Glycoprotein; Lysosome; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..399
FT /note="Integral membrane protein GPR137B"
FT /id="PRO_0000072583"
FT TOPO_DOM 1..46
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..111
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 160..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..188
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 189..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..292
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 7
FT /note="R -> G (in Ref. 3; CAG46569)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="A -> S (in Ref. 3; CAG46569)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="V -> M (in Ref. 4; BAD97352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 45599 MW; FE788D618A590604 CRC64;
MRPERPRPRG SAPGPMETPP WDPARNDSLP PTLTPAVPPY VKLGLTVVYT VFYALLFVFI
YVQLWLVLRY RHKRLSYQSV FLFLCLFWAS LRTVLFSFYF KDFVAANSLS PFVFWLLYCF
PVCLQFFTLT LMNLYFTQVI FKAKSKYSPE LLKYRLPLYL ASLFISLVFL LVNLTCAVLV
KTGNWERKVI VSVRVAINDT LFVLCAVSLS ICLYKISKMS LANIYLESKG SSVCQVTAIG
VTVILLYTSR ACYNLFILSF SQNKSVHSFD YDWYNVSDQA DLKNQLGDAG YVLFGVVLFV
WELLPTTLVV YFFRVRNPTK DLTNPGMVPS HGFSPRSYFF DNPRRYDSDD DLAWNIAPQG
LQGGFAPDYY DWGQQTNSFL AQAGTLQDST LDPDKPSLG
