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DRD5_XENLA
ID   DRD5_XENLA              Reviewed;         457 AA.
AC   P42290;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=D(1B) dopamine receptor;
DE   AltName: Full=D(5) dopamine receptor;
DE   AltName: Full=Dopamine D5 receptor;
GN   Name=drd5;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7937989; DOI=10.1073/pnas.91.22.10536;
RA   Sugamori K.S., Demchyshyn L.L., Chung M., Niznik H.B.;
RT   "D1A, D1B, and D1C dopamine receptors from Xenopus laevis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:10536-10540(1994).
CC   -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC       which activate adenylyl cyclase.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain and kidney.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U07864; AAA50829.1; -; Genomic_DNA.
DR   PIR; I51660; I51660.
DR   RefSeq; XP_018098149.1; XM_018242660.1.
DR   AlphaFoldDB; P42290; -.
DR   SMR; P42290; -.
DR   GeneID; 108705891; -.
DR   KEGG; xla:108705891; -.
DR   CTD; 108705891; -.
DR   Xenbase; XB-GENE-6500261; drd5.S.
DR   OMA; NNLANWT; -.
DR   OrthoDB; 1045889at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 108705891; Expressed in camera-type eye and 2 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR   InterPro; IPR000497; Dopamine_D5_rcpt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00566; DOPAMINED1BR.
DR   PRINTS; PR00242; DOPAMINER.
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   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..457
FT                   /note="D(1B) dopamine receptor"
FT                   /id="PRO_0000069410"
FT   TOPO_DOM        1..41
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..67
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..105
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..114
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..137
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..156
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..181
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..231
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..282
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..309
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..351
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        352..457
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           361
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        114..199
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   457 AA;  51657 MW;  A0A389311E4CD2FB CRC64;
     MYQPFQHLDS DQVASWQSPE MLMNKSVSRE SQRRKELVAG QIVTGSLLLL LIFWTLFGNI
     LVCTAVMRFR HLRSRVTNIF IVSLAVSDLL VALLVMPWKA VAEVAGHWPF GAFCDIWVAF
     DIMCSTASIL NLCVISVDRY WAISSPFRYE RKMTQRVALL MISTAWALSV LISFIPVQLS
     WHKSETEDHL LSNHSTGNCD SSLNRTYAIS SSLISFYIPV AIMIVTYTRI YRIAQIQIKR
     ISTLERAAEH AQSCRSNRVD SCSRHHQTSL RTSIKKETKV LKTLSIIMGV FVCCWLPFFI
     LNCMVPFCDR SPGHPQAGLP CVSETTFDIF VWFGWANSSL NPIIYAFNAD FRKVFSSLLG
     CGHWCSTTPV ETVNISNELI SYNQDTLFHK DIVTAYVNMI PNVVDCIDDN EDAFDHMSQI
     SQTSANNELA TDSMCELDSE VDISLHKITP SMSNGIH
 
 
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