G137B_MOUSE
ID G137B_MOUSE Reviewed; 385 AA.
AC Q8BNQ3; Q3T9U4; Q99LK4; Q9JHD9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Integral membrane protein GPR137B;
DE AltName: Full=Transmembrane 7 superfamily member 1 protein;
GN Name=Gpr137b; Synonyms=Tm7sf1;
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 [MRNA].
RC STRAIN=Japanese fancy;
RA Spangenberg C., Kos S., Truebenbach J., Enklaar T., Loebbert R.W.,
RA Winterpacht A., Zabel B.U.;
RT "Isolation and characterization of the murine gene Tm7sf1.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Adipose tissue, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=31173907; DOI=10.1016/j.bone.2019.06.002;
RA Urso K., Caetano-Lopes J., Lee P.Y., Yan J., Henke K., Sury M., Liu H.,
RA Zgoda M., Jacome-Galarza C., Nigrovic P.A., Duryea J., Harris M.P.,
RA Charles J.F.;
RT "A role for G protein-coupled receptor 137b in bone remodeling in mouse and
RT zebrafish.";
RL Bone 127:104-113(2019).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30595385; DOI=10.1016/j.bbrc.2018.12.140;
RA Islam Z., Inui T., Ishibashi O.;
RT "Gpr137b is an orphan G-protein-coupled receptor associated with M2
RT macrophage polarization.";
RL Biochem. Biophys. Res. Commun. 509:657-663(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 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 (PubMed:31173907). Involved in
CC interleukin-4-induced M2 macrophage polarization (PubMed:30595385).
CC {ECO:0000250|UniProtKB:O60478, ECO:0000269|PubMed:30595385,
CC ECO:0000269|PubMed:31173907}.
CC -!- FUNCTION: Acts also as a negative regulator of osteoclast activity
CC (PubMed:31173907). Involved in interleukin-4-induced M2 macrophage
CC polarization (PubMed:30595385). {ECO:0000269|PubMed:30595385,
CC ECO:0000269|PubMed:31173907}.
CC -!- SUBUNIT: Interaction with RRAGA; increases RRAGA recruitment to
CC lysosomes. Interacts with MTOR; this interaction is amino acid
CC sensitive. {ECO:0000250|UniProtKB:O60478}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:31173907};
CC Multi-pass membrane protein {ECO:0000255}. Note=Colocalized with MTOR
CC in lysosome after amino acid stimulation.
CC {ECO:0000250|UniProtKB:O60478}.
CC -!- TISSUE SPECIFICITY: Widely expressed with high expression in bone
CC marrow and kidney (PubMed:30595385). Highly expressed in osteoclasts
CC (at protein level) (PubMed:31173907). {ECO:0000269|PubMed:30595385,
CC ECO:0000269|PubMed:31173907}.
CC -!- INDUCTION: Up-regulated during osteoclastogenesis (in vitro).
CC {ECO:0000269|PubMed:31173907}.
CC -!- SIMILARITY: Belongs to the GPR137 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF154337; AAF73259.1; -; mRNA.
DR EMBL; AK080884; BAC38061.1; -; mRNA.
DR EMBL; AK172286; BAE42926.1; -; mRNA.
DR EMBL; BC003212; AAH03212.1; -; mRNA.
DR CCDS; CCDS26243.1; -.
DR RefSeq; NP_114388.2; NM_031999.2.
DR AlphaFoldDB; Q8BNQ3; -.
DR STRING; 10090.ENSMUSP00000021738; -.
DR GlyGen; Q8BNQ3; 2 sites.
DR PhosphoSitePlus; Q8BNQ3; -.
DR SwissPalm; Q8BNQ3; -.
DR MaxQB; Q8BNQ3; -.
DR PaxDb; Q8BNQ3; -.
DR PRIDE; Q8BNQ3; -.
DR ProteomicsDB; 273403; -.
DR GeneID; 83924; -.
DR KEGG; mmu:83924; -.
DR UCSC; uc007plu.2; mouse.
DR CTD; 7107; -.
DR MGI; MGI:1891463; Gpr137b.
DR eggNOG; ENOG502QQ83; Eukaryota.
DR InParanoid; Q8BNQ3; -.
DR PhylomeDB; Q8BNQ3; -.
DR TreeFam; TF329003; -.
DR BioGRID-ORCS; 83924; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gpr137b; mouse.
DR PRO; PR:Q8BNQ3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BNQ3; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0045779; P:negative regulation of bone resorption; IMP:UniProtKB.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP: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 GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR GO; GO:0043030; P:regulation of macrophage activation; IMP: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..385
FT /note="Integral membrane protein GPR137B"
FT /id="PRO_0000304801"
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..96
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..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..277
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 233
FT /note="T -> A (in Ref. 1; AAF73259)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="C -> Y (in Ref. 2; BAC38061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 44055 MW; 24AB0B7A9CA64535 CRC64;
MEAPPWEPVR NDSLPPTLSP AVPPYVKLGL TAVYTVFYAL LFVFIYAQLW LVLRYRHKRL
SYQSVFLFLC LFWASLRTVL FSFYFRDFVA ANSFSPFVFW LLYCFPVCLQ FFTLTLMNLY
FTQVIFKAKS KYSPELLKYR LPLYLASLFI SLVFLLVNLT CAVLVKTGDW DRKVIVSVRV
AINDTLFVLC AISLSICLYK ISKMSLANIY LESKGSSVCQ VTAIGVTVIL LYTSRACYNL
FILSFSQIKN VHSFDYDWYN VSDQADLKSQ LGDAGYVVFG VVLFVWELLP TTLVVYFFRV
RNPTKDLTNP GMVPSHGFSP RSYFFDNPRR YDSDDDLAWN IAPQGLQGSF APDYCDWGQQ
NNSFLAQAGT LHQDSTLDPD KASQG
