MTH2_DROYA
ID MTH2_DROYA Reviewed; 536 AA.
AC Q95NT6; Q95PK5; Q95PK6; Q95PK7; Q95WT7;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=G-protein coupled receptor Mth2;
DE AltName: Full=Protein methuselah-2;
DE Flags: Precursor;
GN Name=mth2;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245 {ECO:0000312|EMBL:AAK97894.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BG1013 {ECO:0000312|EMBL:AAK97892.1}, Yak_2, Yak_23, Yak_30, Yak_4,
RC Yak_5, and Yak_8;
RX PubMed=12694290; DOI=10.1046/j.1365-294x.2003.01841.x;
RA Duvernell D.D., Schmidt P.S., Eanes W.F.;
RT "Clines and adaptive evolution in the methuselah gene region in Drosophila
RT melanogaster.";
RL Mol. Ecol. 12:1277-1285(2003).
CC -!- FUNCTION: Involved in biological aging and stress response. Essential
CC for adult survival (By similarity). {ECO:0000250|UniProtKB:O97148}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O97148}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. Mth
CC subfamily. {ECO:0000305}.
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DR EMBL; AF300410; AAK97892.1; -; Genomic_DNA.
DR EMBL; AF300409; AAK97892.1; JOINED; Genomic_DNA.
DR EMBL; AF300412; AAK97893.1; -; Genomic_DNA.
DR EMBL; AF300411; AAK97893.1; JOINED; Genomic_DNA.
DR EMBL; AF300414; AAK97894.1; -; Genomic_DNA.
DR EMBL; AF300413; AAK97894.1; JOINED; Genomic_DNA.
DR EMBL; AF300415; AAK97895.1; -; Genomic_DNA.
DR EMBL; AF300417; AAK97896.1; -; Genomic_DNA.
DR EMBL; AF300416; AAK97896.1; JOINED; Genomic_DNA.
DR EMBL; AF300419; AAK97897.1; -; Genomic_DNA.
DR EMBL; AF300418; AAK97897.1; JOINED; Genomic_DNA.
DR EMBL; AF300421; AAK97898.1; -; Genomic_DNA.
DR EMBL; AF300420; AAK97898.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q95NT6; -.
DR SMR; Q95NT6; -.
DR eggNOG; ENOG502R627; Eukaryota.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR CDD; cd00251; Mth_Ecto; 1.
DR Gene3D; 2.30.160.11; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR044860; Methusela_ecto_dom_1.
DR InterPro; IPR010596; Methuselah_N_dom.
DR InterPro; IPR036272; Methuselah_N_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF06652; Methuselah_N; 1.
DR SUPFAM; SSF63877; SSF63877; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..536
FT /note="G-protein coupled receptor Mth2"
FT /id="PRO_0000013033"
FT TOPO_DOM 1..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..449
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 487..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 17..71
FT /evidence="ECO:0000250|UniProtKB:O97148"
FT DISULFID 73..78
FT /evidence="ECO:0000250|UniProtKB:O97148"
FT DISULFID 82..177
FT /evidence="ECO:0000250|UniProtKB:O97148"
FT DISULFID 83..96
FT /evidence="ECO:0000250|UniProtKB:O97148"
FT DISULFID 138..197
FT /evidence="ECO:0000250|UniProtKB:O97148"
FT VARIANT 481
FT /note="N -> K (in strain: Yak_5)"
FT VARIANT 526
FT /note="S -> N (in strain: Yak_4 and Yak_8)"
SQ SEQUENCE 536 AA; 61768 MW; 58E6124767361567 CRC64;
MAERDHYHTI DDPNVPCNFY DTVNLTGHTV FPNGSYDYYG TIVPAELVGT YDYIHSSLTE
RIEVREHVRG CVCKFKSCLN ICCPWRQVFN SEVDGCIIDH SDNRTWPDPP MLNITFRNDS
TILVNMFAQF AIQSFRPCPK MFSLQPETSH WDDYLLFENG SMLRVDDQQL IRKNEFCMVP
TYVNESDMFY TIHPANCDMQ DDNSTVKIIN AYAMMFSIPF MMLTIAVYLL IPELRNQHGK
SLVCYLVGLT VGYTSLCYVQ LYQVDATGDA CKVFGYTAYF FFMGAYMWLS VISFDLWHNF
RGTRGINRFQ EKKRFLFYSL YSWGIAVVFL AFTYIAQELT NLPAYLKPGI GDGVYCWLDM
SNWAAMIYFY GPILVIVVAN TIMFIMTAIK IHGVQREMAR IIASENSTKN LRTEKDKFGL
FLRLFLIMGI TWLTELISYF VGSDKGWSKL FYISDLANAM QGFLIFMLFV MKKKVKHLIT
NRCSSVRDGS NQRQSQYSTK TTSSSVANLS LHEKPSVEKP LVISSSVDPQ KTTIFR
