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DOPR2_DROME
ID   DOPR2_DROME             Reviewed;         539 AA.
AC   Q24563; Q24569; Q9VAJ8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Dopamine receptor 2;
DE   AltName: Full=Dopamine 1-like receptor 2;
GN   Name=Dop1R2; Synonyms=DAMB, DopR2, DopR99B; ORFNames=CG18741;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RC   STRAIN=Canton-S; TISSUE=Head;
RX   PubMed=8656286; DOI=10.1523/jneurosci.16-12-03925.1996;
RA   Feng G., Hannan F., Reale V., Hon Y.Y., Kousky C.T., Evans P.D., Hall L.M.;
RT   "Cloning and functional characterization of a novel dopamine receptor from
RT   Drosophila melanogaster.";
RL   J. Neurosci. 16:3925-3933(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Canton-S;
RX   PubMed=8663989; DOI=10.1016/s0896-6273(00)80139-7;
RA   Han K.-A., Millar N.S., Grotewiel M.S., Davis R.L.;
RT   "DAMB, a novel dopamine receptor expressed specifically in Drosophila
RT   mushroom bodies.";
RL   Neuron 16:1127-1135(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Head;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for dopamine. The activity of this receptor is
CC       mediated by G proteins which activate adenylyl cyclase. Also capable of
CC       generating a calcium signal. In terms of antagonist responses, would be
CC       classed with the D1-like dopamine receptor group. This receptor is an
CC       attractive candidate for initiating biochemical cascades underlying
CC       olfactory learning. {ECO:0000269|PubMed:8656286,
CC       ECO:0000269|PubMed:8663989}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q24563-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q24563-2; Sequence=VSP_001877;
CC   -!- TISSUE SPECIFICITY: Expressed in both central and peripheral nervous
CC       systems. {ECO:0000269|PubMed:8663989}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U34383; AAC47161.1; -; mRNA.
DR   EMBL; U61264; AAB08000.1; -; mRNA.
DR   EMBL; AE014297; AAF56908.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAN14180.1; -; Genomic_DNA.
DR   EMBL; BT010212; AAQ23530.1; -; mRNA.
DR   RefSeq; NP_524548.1; NM_079824.4. [Q24563-1]
DR   RefSeq; NP_733299.1; NM_170420.2. [Q24563-2]
DR   AlphaFoldDB; Q24563; -.
DR   SMR; Q24563; -.
DR   BioGRID; 68348; 1.
DR   DIP; DIP-22945N; -.
DR   STRING; 7227.FBpp0084834; -.
DR   GlyGen; Q24563; 4 sites.
DR   PaxDb; Q24563; -.
DR   EnsemblMetazoa; FBtr0085467; FBpp0084833; FBgn0266137. [Q24563-2]
DR   EnsemblMetazoa; FBtr0085468; FBpp0084834; FBgn0266137. [Q24563-1]
DR   GeneID; 43484; -.
DR   KEGG; dme:Dmel_CG18741; -.
DR   CTD; 43484; -.
DR   FlyBase; FBgn0266137; Dop1R2.
DR   VEuPathDB; VectorBase:FBgn0266137; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000154484; -.
DR   InParanoid; Q24563; -.
DR   OMA; YVHEQRA; -.
DR   PhylomeDB; Q24563; -.
DR   Reactome; R-DME-381753; Olfactory Signaling Pathway.
DR   Reactome; R-DME-390696; Adrenoceptors.
DR   Reactome; R-DME-416476; G alpha (q) signalling events.
DR   Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR   BioGRID-ORCS; 43484; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 43484; -.
DR   PRO; PR:Q24563; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0266137; Expressed in brain and 6 other tissues.
DR   ExpressionAtlas; Q24563; baseline and differential.
DR   Genevisible; Q24563; DM.
DR   GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISM:FlyBase.
DR   GO; GO:0030285; C:integral component of synaptic vesicle membrane; IC:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR   GO; GO:0004935; F:adrenergic receptor activity; IEA:InterPro.
DR   GO; GO:0004952; F:dopamine neurotransmitter receptor activity; ISS:FlyBase.
DR   GO; GO:0001588; F:dopamine neurotransmitter receptor activity, coupled via Gs; IDA:UniProtKB.
DR   GO; GO:0008227; F:G protein-coupled amine receptor activity; ISS:FlyBase.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0008226; F:tyramine receptor activity; IDA:CACAO.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:FlyBase.
DR   GO; GO:0001306; P:age-dependent response to oxidative stress; IMP:FlyBase.
DR   GO; GO:1903351; P:cellular response to dopamine; IMP:FlyBase.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; ISS:FlyBase.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:UniProtKB.
DR   GO; GO:0042321; P:negative regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR   GO; GO:1903223; P:positive regulation of oxidative stress-induced neuron death; IMP:FlyBase.
DR   GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IMP:FlyBase.
DR   GO; GO:1990834; P:response to odorant; IMP:FlyBase.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..539
FT                   /note="Dopamine receptor 2"
FT                   /id="PRO_0000069370"
FT   TOPO_DOM        1..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..189
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..206
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..227
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..266
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        442..453
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        454..474
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        475..539
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          326..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           492
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           493
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        182..261
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         511..539
FT                   /note="RFATRRCYSTCSLHGIQHVRHNSCEQTYI -> CHVAAAMVAASTSFGYHSV
FT                   NQIDRTLM (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:8663989"
FT                   /id="VSP_001877"
FT   CONFLICT        496
FT                   /note="K -> E (in Ref. 5; AAQ23530)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   539 AA;  59505 MW;  32FDDC0E935AF4B3 CRC64;
     MVDDNGSSPE VEGAEGAGAP LLALLRVDGL NQTQTRSPSP SFFGSYNISE DVYFYFNGLP
     TSTELVLNAT TSATSATLSP AMVATGGGGT TTPEPDLSEF LEALPNDRVG LLAFLFLFSF
     ATVFGNSLVI LAVIRERYLH TATNYFITSL AVADCLVGLV VMPFSALYEV LENTWFFGTD
     WCDIWRSLDV LFSTASILNL CVISLDRYWA ITDPFSYPMR MTVKRAAGLI AAVWICSSAI
     SFPAIVWWRA ARDGEMPAYK CTFTEHLGYL VFSSTISFYL PLLVMVFTYC RIYRAAVIQT
     RSLKIGTKQV LMASGELQLT LRIHRGGTTR DQQNQVSGGG GGGGGGGGGG GSLSHSHSHS
     HHHHHNHGGG TTTSTPEEPD DEPLSALHNN GLARHRHMGK NFSLSRKLAK FAKEKKAAKT
     LGIVMGVFII CWLPFFVVNL LSGFCIECIE HEEIVSAIVT WLGWINSCMN PVIYACWSRD
     FRRAFVRLLC MCCPRKIRRK YQPTMRSKSQ RFATRRCYST CSLHGIQHVR HNSCEQTYI
 
 
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