G137A_HUMAN
ID G137A_HUMAN Reviewed; 417 AA.
AC Q96N19; B4DTG7; B7Z7M1; Q4G0Y9; Q8N4K6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Integral membrane protein GPR137;
DE AltName: Full=Transmembrane 7 superfamily member 1-like 1 protein;
GN Name=GPR137; Synonyms=C11orf4, GPR137A, TM7SF1L1;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Pancreas;
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 SUBCELLULAR LOCATION, 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 may regulate MTORC1
CC complex translocation to lysosomes (PubMed:31036939). May play a role
CC in autophagy (PubMed:31036939). {ECO:0000269|PubMed:31036939}.
CC -!- FUNCTION: May activate Wnt/beta-catenin signaling to modulate
CC epithelial cell function. {ECO:0000250|UniProtKB:Q80ZU9}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:31036939};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96N19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96N19-2; Sequence=VSP_022122;
CC Name=3;
CC IsoId=Q96N19-3; Sequence=VSP_022121, VSP_022122;
CC Name=4;
CC IsoId=Q96N19-4; Sequence=VSP_043278;
CC Name=5;
CC IsoId=Q96N19-5; Sequence=VSP_043592, VSP_043593;
CC -!- SIMILARITY: Belongs to the GPR137 family. {ECO:0000305}.
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DR EMBL; AK056094; BAB71093.1; -; mRNA.
DR EMBL; AK300209; BAG61979.1; -; mRNA.
DR EMBL; AK302256; BAH13657.1; -; mRNA.
DR EMBL; AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033920; AAH33920.1; -; mRNA.
DR EMBL; BC035002; AAH35002.1; -; mRNA.
DR CCDS; CCDS53656.1; -. [Q96N19-2]
DR CCDS; CCDS53657.1; -. [Q96N19-5]
DR CCDS; CCDS53658.1; -. [Q96N19-3]
DR CCDS; CCDS8066.1; -. [Q96N19-1]
DR RefSeq; NP_001164197.1; NM_001170726.1.
DR RefSeq; NP_001164351.1; NM_001170880.1. [Q96N19-2]
DR RefSeq; NP_001164352.1; NM_001170881.1. [Q96N19-3]
DR RefSeq; NP_001170829.1; NM_001177358.1. [Q96N19-5]
DR RefSeq; NP_064540.3; NM_020155.3. [Q96N19-1]
DR RefSeq; XP_005274157.1; XM_005274100.2. [Q96N19-1]
DR RefSeq; XP_005274158.1; XM_005274101.2.
DR RefSeq; XP_005274159.1; XM_005274102.2. [Q96N19-1]
DR RefSeq; XP_005274161.1; XM_005274104.2. [Q96N19-1]
DR RefSeq; XP_011543471.1; XM_011545169.1. [Q96N19-1]
DR RefSeq; XP_016873503.1; XM_017018014.1.
DR RefSeq; XP_016873504.1; XM_017018015.1.
DR AlphaFoldDB; Q96N19; -.
DR BioGRID; 121207; 4.
DR IntAct; Q96N19; 4.
DR MINT; Q96N19; -.
DR STRING; 9606.ENSP00000411827; -.
DR GlyGen; Q96N19; 2 sites.
DR iPTMnet; Q96N19; -.
DR PhosphoSitePlus; Q96N19; -.
DR BioMuta; GPR137; -.
DR DMDM; 126302549; -.
DR jPOST; Q96N19; -.
DR MassIVE; Q96N19; -.
DR PaxDb; Q96N19; -.
DR PeptideAtlas; Q96N19; -.
DR PRIDE; Q96N19; -.
DR ProteomicsDB; 77448; -. [Q96N19-1]
DR ProteomicsDB; 77449; -. [Q96N19-2]
DR ProteomicsDB; 77450; -. [Q96N19-3]
DR ProteomicsDB; 77451; -. [Q96N19-4]
DR ProteomicsDB; 77452; -. [Q96N19-5]
DR Antibodypedia; 15349; 194 antibodies from 24 providers.
DR DNASU; 56834; -.
DR Ensembl; ENST00000313074.7; ENSP00000321698.3; ENSG00000173264.15. [Q96N19-1]
DR Ensembl; ENST00000377702.8; ENSP00000366931.4; ENSG00000173264.15. [Q96N19-3]
DR Ensembl; ENST00000411458.5; ENSP00000411827.1; ENSG00000173264.15. [Q96N19-4]
DR Ensembl; ENST00000438980.7; ENSP00000415698.2; ENSG00000173264.15. [Q96N19-2]
DR Ensembl; ENST00000539851.5; ENSP00000442792.1; ENSG00000173264.15. [Q96N19-5]
DR GeneID; 56834; -.
DR KEGG; hsa:56834; -.
DR MANE-Select; ENST00000438980.7; ENSP00000415698.2; NM_001170880.2; NP_001164351.1. [Q96N19-2]
DR UCSC; uc001nzf.4; human. [Q96N19-1]
DR CTD; 56834; -.
DR DisGeNET; 56834; -.
DR GeneCards; GPR137; -.
DR HGNC; HGNC:24300; GPR137.
DR HPA; ENSG00000173264; Tissue enhanced (testis).
DR neXtProt; NX_Q96N19; -.
DR OpenTargets; ENSG00000173264; -.
DR PharmGKB; PA143485482; -.
DR VEuPathDB; HostDB:ENSG00000173264; -.
DR eggNOG; ENOG502QQ83; Eukaryota.
DR GeneTree; ENSGT00940000153986; -.
DR HOGENOM; CLU_050057_0_0_1; -.
DR InParanoid; Q96N19; -.
DR OMA; RSYFFDH; -.
DR OrthoDB; 1399303at2759; -.
DR PhylomeDB; Q96N19; -.
DR TreeFam; TF329003; -.
DR PathwayCommons; Q96N19; -.
DR SignaLink; Q96N19; -.
DR BioGRID-ORCS; 56834; 51 hits in 1080 CRISPR screens.
DR ChiTaRS; GPR137; human.
DR GenomeRNAi; 56834; -.
DR Pharos; Q96N19; Tbio.
DR PRO; PR:Q96N19; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96N19; protein.
DR Bgee; ENSG00000173264; Expressed in right testis and 126 other tissues.
DR ExpressionAtlas; Q96N19; baseline and differential.
DR Genevisible; Q96N19; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IDA: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 Alternative splicing; Autophagy; Glycoprotein; Lysosome; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..417
FT /note="Integral membrane protein GPR137"
FT /id="PRO_0000269996"
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..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..241
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..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..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 344..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT VAR_SEQ 1
FT /note="M -> MLWAVRTRCYVVKAQLGPTVALEGRAPRAPGPSCLGNGNCQRPGPIT
FT SRNVTRASLPDM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043278"
FT VAR_SEQ 212..261
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022121"
FT VAR_SEQ 305..320
FT /note="STSHILNGQVFASRSY -> YVGQSRLWELVWCHRA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043592"
FT VAR_SEQ 321..417
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043593"
FT VAR_SEQ 344..417
FT /note="RCQDQAATTTVSTPPHRRDPPPSPTEYPGPSPPHPRPLCQVCLPLLAQDPGG
FT RGYPLLWPAPCCSCHSELVPSP -> SMSGSLGSGSWYGAIGREPGWYGGSQTKTTPLL
FT FSQVPGPGGHHHSLYSTPQT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022122"
FT CONFLICT 254
FT /note="D -> G (in Ref. 1; BAB71093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46059 MW; 4059610F4B822FCA CRC64;
MESNLSGLVP AAGLVPALPP AVTLGLTAAY TTLYALLFFS VYAQLWLVLL YGHKRLSYQT
VFLALCLLWA ALRTTLFSFY FRDTPRANRL GPLPFWLLYC CPVCLQFFTL TLMNLYFAQV
VFKAKVKRRP EMSRGLLAVR GAFVGASLLF LLVNVLCAVL SHRRRAQPWA LLLVRVLVSD
SLFVICALSL AACLCLVARR APSTSIYLEA KGTSVCQAAA MGGAMVLLYA SRACYNLTAL
ALAPQSRLDT FDYDWYNVSD QADLVNDLGN KGYLVFGLIL FVWELLPTTL LVGFFRVHRP
PQDLSTSHIL NGQVFASRSY FFDRAGHCED EGCSWEHSRG ESTRCQDQAA TTTVSTPPHR
RDPPPSPTEY PGPSPPHPRP LCQVCLPLLA QDPGGRGYPL LWPAPCCSCH SELVPSP
