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Protein

G-protein coupled receptor Mth

Gene

mth

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in biological aging and stress response. Essential for adult survival. Required in the presynaptic motor neuron to up-regulate neurotransmitter exocytosis at larval glutamatergic neuromuscular junctions (NMJs). Regulates a step associated with docking and clustering of vesicles at release sites. Sun, Acp70A/SP and eys/SPAM are agonists that activate mth.2 Publications

GO - Molecular functioni

  • G-protein coupled peptide receptor activity Source: FlyBase
  • G-protein coupled receptor activity Source: UniProtKB
  • peptide binding Source: FlyBase

GO - Biological processi

  • aging Source: FlyBase
  • cell surface receptor signaling pathway Source: InterPro
  • determination of adult lifespan Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • response to heat Source: UniProtKB
  • response to oxidative stress Source: FlyBase
  • response to paraquat Source: FlyBase
  • response to reactive oxygen species Source: UniProtKB
  • response to starvation Source: UniProtKB
  • synaptic vesicle exocytosis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Exocytosis, Neurotransmitter transport, Transport

Protein family/group databases

TCDBi9.A.14.14.2. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
G-protein coupled receptor Mth
Alternative name(s):
Protein methuselah
Gene namesi
Name:mth
ORF Names:CG6936
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0023000. mth.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 218194ExtracellularSequence analysisAdd
BLAST
Transmembranei219 – 23921Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini240 – 2489CytoplasmicSequence analysis
Transmembranei249 – 26921Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini270 – 2789ExtracellularSequence analysis
Transmembranei279 – 29921Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini300 – 32021CytoplasmicSequence analysisAdd
BLAST
Transmembranei321 – 34121Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini342 – 37029ExtracellularSequence analysisAdd
BLAST
Transmembranei371 – 39121Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini392 – 42433CytoplasmicSequence analysisAdd
BLAST
Transmembranei425 – 44521Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini446 – 4549ExtracellularSequence analysis
Transmembranei455 – 47521Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini476 – 51439CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytosol Source: GOC
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: FlyBase
  • presynapse Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Increase in average life-span and enhanced resistance to various forms of stress, including starvation, high temperature and dietary paraquat, a free-radical generator.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 514490G-protein coupled receptor MthPRO_0000013020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 83
Glycosylationi45 – 451N-linked (GlcNAc...)
Disulfide bondi85 ↔ 90
Disulfide bondi94 ↔ 188
Disulfide bondi95 ↔ 106
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence analysis
Glycosylationi123 – 1231N-linked (GlcNAc...)
Disulfide bondi150 ↔ 209
Glycosylationi170 – 1701N-linked (GlcNAc...)
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence analysis
Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO97148.
PRIDEiO97148.

Expressioni

Gene expression databases

BgeeiO97148.
ExpressionAtlasiO97148. differential.
GenevisibleiO97148. DM.

Interactioni

Subunit structurei

Homodimer. Interacts with sun, Acp70A/SP and eys/SPAM.3 Publications

Protein-protein interaction databases

STRINGi7227.FBpp0072470.

Structurei

Secondary structure

1
514
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 333Combined sources
Beta strandi40 – 423Combined sources
Beta strandi48 – 503Combined sources
Beta strandi53 – 553Combined sources
Helixi57 – 593Combined sources
Beta strandi60 – 678Combined sources
Beta strandi73 – 8210Combined sources
Helixi84 – 863Combined sources
Beta strandi90 – 956Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi105 – 1073Combined sources
Helixi112 – 1176Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi131 – 1355Combined sources
Turni136 – 1394Combined sources
Beta strandi140 – 1434Combined sources
Helixi161 – 1633Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi173 – 1753Combined sources
Turni176 – 1794Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi186 – 19510Combined sources
Beta strandi197 – 20812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJRX-ray2.30A/B25-219[»]
2PZXX-ray3.50A/B/C/D25-212[»]
ProteinModelPortaliO97148.
SMRiO97148. Positions 25-212.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO97148.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4193. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00530000064566.
InParanoidiO97148.
KOiK04599.
OMAiGFYNCWI.
OrthoDBiEOG776SPZ.
PhylomeDBiO97148.

Family and domain databases

Gene3Di2.170.180.11. 1 hit.
InterProiIPR017981. GPCR_2-like.
IPR000832. GPCR_2_secretin-like.
IPR023311. Methusela_ecto_dom_2.
IPR010596. Methuselah_N_dom.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF06652. Methuselah_N. 1 hit.
[Graphical view]
PROSITEiPS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: O97148-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKTLLVLRIS TVILVVLVIQ KSYADILECD YFDTVDISAA QKLQNGSYLF
60 70 80 90 100
EGLLVPAILT GEYDFRILPD DSKQKVARHI RGCVCKLKPC VRFCCPHDHI
110 120 130 140 150
MDNGVCYDNM SDEELAELDP FLNVTLDDGS VSRRHFKNEL IVQWDLPMPC
160 170 180 190 200
DGMFYLDNRE EQDKYTLFEN GTFFRHFDRV TLRKREYCLQ HLTFADGNAT
210 220 230 240 250
SIRIAPHNCL IVPSITGQTV VMISSLICMV LTIAVYLFVK KLQNLHGKCF
260 270 280 290 300
ICYMVCLFMG YLFLLLDLWQ ISISFCKPAG FLGYFFVMAA FFWLSVISLH
310 320 330 340 350
LWNTFRGSSH KANRFLFEHR FLAYNTYAWG MAVVLTGITV LADNIVENQD
360 370 380 390 400
WNPRVGHEGH CWIYTQAWSA MLYFYGPMVF LIAFNITMFI LTAKRILGVK
410 420 430 440 450
KDIQNFAHRQ ERKQKLNSDK QTYTFFLRLF IIMGLSWSLE IGSYFSQSNQ
460 470 480 490 500
TWANVFLVAD YLNWSQGIII FILFVLKRST WRLLQESIRG EGEEVNNSEE
510
EISLENTTTR NVLL
Length:514
Mass (Da):59,644
Last modified:May 1, 1999 - v1
Checksum:iF2A5370CECCD1D5C
GO
Isoform B (identifier: O97148-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     487-514: SIRGEGEEVNNSEEEISLENTTTRNVLL → RNHPKSTRSVISNRSMASRITVGTTPKNKARNSPLA

Note: No experimental confirmation available.
Show »
Length:522
Mass (Da):60,446
Checksum:i81C85F368E891600
GO

Sequence cautioni

The sequence AAG22708.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22709.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22710.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22711.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22712.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22713.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22714.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22715.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22716.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22717.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22718.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22719.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22720.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22721.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22722.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22723.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22724.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22725.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22726.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22727.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22728.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22729.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22730.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22731.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22732.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22733.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22734.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22735.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22736.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22737.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG22738.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541L → I in strain: MA97_6. 1 Publication
Natural varianti132 – 1321S → A in strain: ZIM(S)49 and ZIM(H)44. 1 Publication
Natural varianti151 – 1511D → N in strain: CT97_3, MFL97_1 and ZIM(S)37. 1 Publication
Natural varianti281 – 2811F → V in strain: ZIM(S)49 and ZIM(H)44. 1 Publication
Natural varianti357 – 3571H → N in strain: DPF96_3.0, HFL97_15, JFL97_1, JFL97_9 and ZIM(S)37. 1 Publication
Natural varianti387 – 3871T → N in strain: ZIM(S)35. 1 Publication
Natural varianti407 – 4071A → V in strain: ZIM(H)23. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei487 – 51428SIRGE…RNVLL → RNHPKSTRSVISNRSMASRI TVGTTPKNKARNSPLA in isoform B. 2 PublicationsVSP_002023Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF109308 mRNA. Translation: AAD16981.1.
AF280552 Genomic DNA. Translation: AAG22708.1. Sequence problems.
AF280553 Genomic DNA. Translation: AAG22709.1. Sequence problems.
AF280554 Genomic DNA. Translation: AAG22710.1. Sequence problems.
AF280555 Genomic DNA. Translation: AAG22711.1. Sequence problems.
AF280556 Genomic DNA. Translation: AAG22712.1. Sequence problems.
AF280557 Genomic DNA. Translation: AAG22713.1. Sequence problems.
AF280558 Genomic DNA. Translation: AAG22714.1. Sequence problems.
AF280559 Genomic DNA. Translation: AAG22715.1. Sequence problems.
AF280560 Genomic DNA. Translation: AAG22716.1. Sequence problems.
AF280561 Genomic DNA. Translation: AAG22717.1. Sequence problems.
AF280562 Genomic DNA. Translation: AAG22718.1. Sequence problems.
AF280563 Genomic DNA. Translation: AAG22719.1. Sequence problems.
AF280564 Genomic DNA. Translation: AAG22720.1. Sequence problems.
AF280565 Genomic DNA. Translation: AAG22721.1. Sequence problems.
AF280566 Genomic DNA. Translation: AAG22722.1. Sequence problems.
AF280567 Genomic DNA. Translation: AAG22723.1. Sequence problems.
AF280568 Genomic DNA. Translation: AAG22724.1. Sequence problems.
AF280569 Genomic DNA. Translation: AAG22725.1. Sequence problems.
AF280570 Genomic DNA. Translation: AAG22726.1. Sequence problems.
AF280571 Genomic DNA. Translation: AAG22727.1. Sequence problems.
AF280572 Genomic DNA. Translation: AAG22728.1. Sequence problems.
AF280573 Genomic DNA. Translation: AAG22729.1. Sequence problems.
AF280574 Genomic DNA. Translation: AAG22730.1. Sequence problems.
AF280575 Genomic DNA. Translation: AAG22731.1. Sequence problems.
AF280576 Genomic DNA. Translation: AAG22732.1. Sequence problems.
AF280577 Genomic DNA. Translation: AAG22733.1. Sequence problems.
AF280578 Genomic DNA. Translation: AAG22734.1. Sequence problems.
AF280579 Genomic DNA. Translation: AAG22735.1. Sequence problems.
AF280580 Genomic DNA. Translation: AAG22736.1. Sequence problems.
AF280581 Genomic DNA. Translation: AAG22737.1. Sequence problems.
AF280582 Genomic DNA. Translation: AAG22738.1. Sequence problems.
AE014296 Genomic DNA. Translation: AAF47379.2.
AE014296 Genomic DNA. Translation: AAN11440.1.
AY052111 mRNA. Translation: AAK93535.1.
BT044433 mRNA. Translation: ACH92498.1.
RefSeqiNP_001246535.1. NM_001259606.2. [O97148-1]
NP_523871.1. NM_079147.4. [O97148-1]
NP_728521.1. NM_167829.3. [O97148-2]
UniGeneiDm.4379.

Genome annotation databases

EnsemblMetazoaiFBtr0072570; FBpp0072469; FBgn0023000. [O97148-1]
FBtr0306850; FBpp0297746; FBgn0023000. [O97148-1]
GeneIDi38058.
KEGGidme:Dmel_CG6936.
UCSCiCG6936-RA. d. melanogaster. [O97148-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF109308 mRNA. Translation: AAD16981.1.
AF280552 Genomic DNA. Translation: AAG22708.1. Sequence problems.
AF280553 Genomic DNA. Translation: AAG22709.1. Sequence problems.
AF280554 Genomic DNA. Translation: AAG22710.1. Sequence problems.
AF280555 Genomic DNA. Translation: AAG22711.1. Sequence problems.
AF280556 Genomic DNA. Translation: AAG22712.1. Sequence problems.
AF280557 Genomic DNA. Translation: AAG22713.1. Sequence problems.
AF280558 Genomic DNA. Translation: AAG22714.1. Sequence problems.
AF280559 Genomic DNA. Translation: AAG22715.1. Sequence problems.
AF280560 Genomic DNA. Translation: AAG22716.1. Sequence problems.
AF280561 Genomic DNA. Translation: AAG22717.1. Sequence problems.
AF280562 Genomic DNA. Translation: AAG22718.1. Sequence problems.
AF280563 Genomic DNA. Translation: AAG22719.1. Sequence problems.
AF280564 Genomic DNA. Translation: AAG22720.1. Sequence problems.
AF280565 Genomic DNA. Translation: AAG22721.1. Sequence problems.
AF280566 Genomic DNA. Translation: AAG22722.1. Sequence problems.
AF280567 Genomic DNA. Translation: AAG22723.1. Sequence problems.
AF280568 Genomic DNA. Translation: AAG22724.1. Sequence problems.
AF280569 Genomic DNA. Translation: AAG22725.1. Sequence problems.
AF280570 Genomic DNA. Translation: AAG22726.1. Sequence problems.
AF280571 Genomic DNA. Translation: AAG22727.1. Sequence problems.
AF280572 Genomic DNA. Translation: AAG22728.1. Sequence problems.
AF280573 Genomic DNA. Translation: AAG22729.1. Sequence problems.
AF280574 Genomic DNA. Translation: AAG22730.1. Sequence problems.
AF280575 Genomic DNA. Translation: AAG22731.1. Sequence problems.
AF280576 Genomic DNA. Translation: AAG22732.1. Sequence problems.
AF280577 Genomic DNA. Translation: AAG22733.1. Sequence problems.
AF280578 Genomic DNA. Translation: AAG22734.1. Sequence problems.
AF280579 Genomic DNA. Translation: AAG22735.1. Sequence problems.
AF280580 Genomic DNA. Translation: AAG22736.1. Sequence problems.
AF280581 Genomic DNA. Translation: AAG22737.1. Sequence problems.
AF280582 Genomic DNA. Translation: AAG22738.1. Sequence problems.
AE014296 Genomic DNA. Translation: AAF47379.2.
AE014296 Genomic DNA. Translation: AAN11440.1.
AY052111 mRNA. Translation: AAK93535.1.
BT044433 mRNA. Translation: ACH92498.1.
RefSeqiNP_001246535.1. NM_001259606.2. [O97148-1]
NP_523871.1. NM_079147.4. [O97148-1]
NP_728521.1. NM_167829.3. [O97148-2]
UniGeneiDm.4379.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJRX-ray2.30A/B25-219[»]
2PZXX-ray3.50A/B/C/D25-212[»]
ProteinModelPortaliO97148.
SMRiO97148. Positions 25-212.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0072470.

Protein family/group databases

TCDBi9.A.14.14.2. the g-protein-coupled receptor (gpcr) family.
GPCRDBiSearch...

Proteomic databases

PaxDbiO97148.
PRIDEiO97148.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072570; FBpp0072469; FBgn0023000. [O97148-1]
FBtr0306850; FBpp0297746; FBgn0023000. [O97148-1]
GeneIDi38058.
KEGGidme:Dmel_CG6936.
UCSCiCG6936-RA. d. melanogaster. [O97148-1]

Organism-specific databases

CTDi38058.
FlyBaseiFBgn0023000. mth.

Phylogenomic databases

eggNOGiKOG4193. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00530000064566.
InParanoidiO97148.
KOiK04599.
OMAiGFYNCWI.
OrthoDBiEOG776SPZ.
PhylomeDBiO97148.

Miscellaneous databases

EvolutionaryTraceiO97148.
GenomeRNAii38058.
PROiO97148.

Gene expression databases

BgeeiO97148.
ExpressionAtlasiO97148. differential.
GenevisibleiO97148. DM.

Family and domain databases

Gene3Di2.170.180.11. 1 hit.
InterProiIPR017981. GPCR_2-like.
IPR000832. GPCR_2_secretin-like.
IPR023311. Methusela_ecto_dom_2.
IPR010596. Methuselah_N_dom.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF06652. Methuselah_N. 1 hit.
[Graphical view]
PROSITEiPS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Extended life-span and stress resistance in the Drosophila mutant methuselah."
    Lin Y.-J., Seroude L., Benzer S.
    Science 282:943-946(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DISRUPTION PHENOTYPE.
    Strain: Canton-S.
    Tissue: Embryo.
  2. "Adaptive evolution of a candidate gene for aging in Drosophila."
    Schmidt P.S., Duvernell D.D., Eanes W.F.
    Proc. Natl. Acad. Sci. U.S.A. 97:10861-10865(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), VARIANTS ILE-54; ALA-132; ASN-151; VAL-281; ASN-357; ASN-387 AND VAL-407.
    Strain: CT97_1, CT97_3, CT97_4, DPF96_3.0, DPF96_74.2, HFL97_12, HFL97_15, HFL97_16, HFL97_8, JFL97_1, JFL97_5, JFL97_9, MA97_1, MA97_4, MA97_6, MFL97_1, MFL97_3, MFL97_6, SC96_19.4, VT97_1, VT97_39, VT97_41, ZIM(H)23, ZIM(H)26, ZIM(H)39, ZIM(H)44, ZIM(S)15, ZIM(S)24, ZIM(S)35, ZIM(S)37 and ZIM(S)49.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
    Tissue: Embryo.
  6. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
  7. "Presynaptic regulation of neurotransmission in Drosophila by the G protein-coupled receptor methuselah."
    Song W., Ranjan R., Dawson-Scully K., Bronk P., Marin L., Seroude L., Lin Y.J., Nie Z., Atwood H.L., Benzer S., Zinsmaier K.E.
    Neuron 36:105-119(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "The endogenous ligand Stunted of the GPCR Methuselah extends lifespan in Drosophila."
    Cvejic S., Zhu Z., Felice S.J., Berman Y., Huang X.Y.
    Nat. Cell Biol. 6:540-546(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUN.
  9. "The Drosophila G protein-coupled receptor, Methuselah, exhibits a promiscuous response to peptides."
    Ja W.W., Carvalho G.B., Madrigal M., Roberts R.W., Benzer S.
    Protein Sci. 18:2203-2208(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACP70A AND EYS.
  10. "Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan."
    West A.P. Jr., Llamas L.L., Snow P.M., Benzer S., Bjorkman P.J.
    Proc. Natl. Acad. Sci. U.S.A. 98:3744-3749(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-219.
  11. "Extension of Drosophila melanogaster life span with a GPCR peptide inhibitor."
    Ja W.W., West A.P. Jr., Delker S.L., Bjorkman P.J., Benzer S., Roberts R.W.
    Nat. Chem. Biol. 3:415-419(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 25-212 IN COMPLEX WITH SYNTHETIC RWR MOTIF CONTAINING PEPTIDES.

Entry informationi

Entry nameiMTH_DROME
AccessioniPrimary (citable) accession number: O97148
Secondary accession number(s): B5RJF9
, Q9GN21, Q9GN78, Q9GND6, Q9GNE8, Q9GT57, Q9GT58, Q9GT59, Q9GT60, Q9W0R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Agonists of mth share minimal sequence homology, suggesting a remarkable promiscuity of mth for activation.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.