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P83119 (MTH12_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable G-protein coupled receptor Mth-like 12
Alternative name(s):
Protein methuselah-like 12
Gene names
Name:mthl12
Synonyms:Mth-like-12
ORF Names:CG32853
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the G-protein coupled receptor 2 family. Mth subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 488471Probable G-protein coupled receptor Mth-like 12
PRO_0000013035

Regions

Topological domain18 – 215198Extracellular Potential
Transmembrane216 – 23621Helical; Name=1; Potential
Topological domain237 – 24711Cytoplasmic Potential
Transmembrane248 – 26821Helical; Name=2; Potential
Topological domain269 – 28315Extracellular Potential
Transmembrane284 – 30421Helical; Name=3; Potential
Topological domain305 – 31511Cytoplasmic Potential
Transmembrane316 – 33621Helical; Name=4; Potential
Topological domain337 – 37337Extracellular Potential
Transmembrane374 – 39421Helical; Name=5; Potential
Topological domain395 – 41622Cytoplasmic Potential
Transmembrane417 – 43721Helical; Name=6; Potential
Topological domain438 – 45417Extracellular Potential
Transmembrane455 – 47521Helical; Name=7; Potential
Topological domain476 – 48813Cytoplasmic Potential

Amino acid modifications

Glycosylation191N-linked (GlcNAc...) Potential
Glycosylation341N-linked (GlcNAc...) Potential
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation3651N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 81 By similarity
Disulfide bond83 ↔ 88 By similarity
Disulfide bond92 ↔ 189 By similarity
Disulfide bond93 ↔ 104 By similarity
Disulfide bond155 ↔ 209 By similarity

Sequences

Sequence LengthMass (Da)Tools
P83119 [UniParc].

Last modified July 11, 2003. Version 2.
Checksum: 3CE6B05F8D1DC103

FASTA48856,781
        10         20         30         40         50         60 
MFLWLKCFCT LIIVTIAKNS SAKIPHCKYD ETINISHFKR LNDAYIYEHF EIPANLTGEF 

        70         80         90        100        110        120 
DYKELMDGSK VPTEFPNLRG CICKVRPCIR ICCARKNILS NGECSDGVKN EIKLTMLDLT 

       130        140        150        160        170        180 
MQDILLTDPT LAELNMIPQY NSTELLILRE QFQPCDEIVS LKRDEYTILK DGSILLHTSA 

       190        200        210        220        230        240 
EILSNDQYCL YPEIYSDFPE TIRIINRRCY RNVMPGIAQL SVISVVGFIL TLAVYLSVEK 

       250        260        270        280        290        300 
LRNLLGKCLI CSLFSMFMEY FIWTMDYFRL LQSICSAAGY MKYFFSMSSY LWFSVVSFHL 

       310        320        330        340        350        360 
WELFTSLNRH EPQYRFLIYN TFVWCTAAIP TVVIFSMNQM WENDPGKSEW LPLVGYFGCS 

       370        380        390        400        410        420 
VKDWNSSSWF YSHIPIVILN SFNVIMFVLT AIYIWKVKKG VKSFAQHDER NTTCLEFNVQ 

       430        440        450        460        470        480 
TYIQFVRLFL IMGASWLLDQ LTRLAEDSHL LLDTIVLNLT VYLNAAFGIL IFVLLILKGS 


TFKMIMER 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"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: IDENTIFICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014297 Genomic DNA. Translation: AAN13556.2.
RefSeqNP_731791.2. NM_169508.2.
UniGeneDm.26413.

3D structure databases

ProteinModelPortalP83119.
SMRP83119. Positions 23-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0082214.

Protein family/group databases

GPCRDBSearch...

Proteomic databases

PaxDbP83119.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082746; FBpp0082214; FBgn0045442.
GeneID261599.
KEGGdme:Dmel_CG32853.

Organism-specific databases

CTD261599.
FlyBaseFBgn0045442. mthl12.

Phylogenomic databases

eggNOGKOG4193.
GeneTreeENSGT00530000064566.
InParanoidP83119.
OrthoDBEOG75QR3P.
PhylomeDBP83119.

Family and domain databases

Gene3D2.170.180.11. 1 hit.
InterProIPR022343. GCR1-cAMP_receptor.
IPR017981. GPCR_2-like.
IPR023311. Methusela_ecto_dom_2.
IPR010596. Methuselah_N_dom.
[Graphical view]
PfamPF06652. Methuselah_N. 1 hit.
[Graphical view]
PRINTSPR02001. GCR1CAMPR.
PROSITEPS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi261599.
NextBio843695.

Entry information

Entry nameMTH12_DROME
AccessionPrimary (citable) accession number: P83119
Secondary accession number(s): Q8INH4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: July 11, 2003
Last modified: March 19, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries