位置:首页 > 蛋白库 > G137B_DANRE
G137B_DANRE
ID   G137B_DANRE             Reviewed;         373 AA.
AC   E7F594;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=G protein-coupled receptor 137Ba;
GN   Name=gpr137ba {ECO:0000312|ZFIN:ZDB-GENE-100721-1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   DISRUPTION PHENOTYPE, 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   [3]
RP   DISRUPTION PHENOTYPE, 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       (By similarity). 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). Acts also as a negative regulator of osteoclast
CC       activity (PubMed:31173907). May be involved in interleukin-4-induced M2
CC       macrophage polarization (By similarity). {ECO:0000250|UniProtKB:O60478,
CC       ECO:0000250|UniProtKB:Q8BNQ3, ECO:0000269|PubMed:31036939,
CC       ECO:0000269|PubMed:31173907}.
CC   -!- FUNCTION: Acts also as a negative regulator of osteoclast activity
CC       (PubMed:31173907). May be involved in interleukin-4-induced M2
CC       macrophage polarization (By similarity). {ECO:0000250|UniProtKB:Q8BNQ3,
CC       ECO:0000269|PubMed:31173907}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O60478};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Knockout zebrafish are viable and fertile and
CC       display no obvious morphological defects as adults (PubMed:31173907,
CC       PubMed:31036939). However deficient zebrafish have abnormal microglial
CC       with expended lysosomes (PubMed:31036939). They also display increased
CC       bone resorption (PubMed:31173907). {ECO:0000269|PubMed:31036939,
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; CU651583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_001341229.1; XM_001341193.6.
DR   AlphaFoldDB; E7F594; -.
DR   STRING; 7955.ENSDARP00000037177; -.
DR   PaxDb; E7F594; -.
DR   Ensembl; ENSDART00000031858; ENSDARP00000037177; ENSDARG00000078448.
DR   GeneID; 100001171; -.
DR   KEGG; dre:100001171; -.
DR   CTD; 100001171; -.
DR   ZFIN; ZDB-GENE-100721-1; gpr137ba.
DR   eggNOG; ENOG502QQ83; Eukaryota.
DR   GeneTree; ENSGT00940000153986; -.
DR   HOGENOM; CLU_050057_0_0_1; -.
DR   InParanoid; E7F594; -.
DR   OMA; WNISPQG; -.
DR   OrthoDB; 1399303at2759; -.
DR   PhylomeDB; E7F594; -.
DR   TreeFam; TF329003; -.
DR   PRO; PR:E7F594; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000078448; Expressed in intestine and 16 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:0046849; P:bone remodeling; IMP:ZFIN.
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; IMP:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; IMP:UniProtKB.
DR   InterPro; IPR029723; GPR137.
DR   PANTHER; PTHR15146; PTHR15146; 1.
PE   3: Inferred from homology;
KW   Autophagy; Lysosome; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..373
FT                   /note="G protein-coupled receptor 137Ba"
FT                   /id="PRO_0000448976"
FT   TOPO_DOM        1..15
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        16..36
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        56..76
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..84
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        85..105
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        136..156
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..176
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        177..197
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        214..234
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..268
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        269..289
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..373
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   373 AA;  42892 MW;  F81E0C08031FB066 CRC64;
     MQKDSLPTLS PAVPPYVMLG LTVAYTIFYC LLFVFVYVQL WLVLRYRHKR FSYQTVFLFL
     CLLWAALRAL LFSFYFKNCV TANTLGPFCF WLLYCFPVCL QFFTLSLMNL YFAQVIFKAK
     SKYSPELQKY RLPLYLLFLS ISLLFLLVNL TCALLVKINR ANTETVVLVR VTVNDSLFVL
     CAVSLSLCLY RIAKMSLANI YLEAKGTSVC QVTLIGVTVV LLYSSRACYN LVVLALTKIK
     SINSFDYDWY NVSDQADLKS TLGDAGYVVF GVILFVWELL PTSLVVYFFR VRKPTLDRSA
     SVIPGHMFSS RAYFFDNPRR YDSDDDLAWS IIPQNIQASF TSDSYDWSCR NNSFTAYTEA
     EESHLAPEEL NPY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024