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ADRB3_SHEEP
ID   ADRB3_SHEEP             Reviewed;         405 AA.
AC   Q9XT58; Q9GJS6; Q9GJT0; Q9GL56; Q9GL57;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Beta-3 adrenergic receptor;
DE   AltName: Full=Beta-3 adrenoreceptor;
DE            Short=Beta-3 adrenoceptor;
GN   Name=ADRB3; Synonyms=B3AR;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Merino;
RX   PubMed=10834601; DOI=10.2527/2000.7851397x;
RA   Forrest R.H., Hickford J.G.H.;
RT   "Rapid communication: nucleotide sequences of the bovine, caprine, and
RT   ovine beta3-adrenergic receptor genes.";
RL   J. Anim. Sci. 78:1397-1398(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-52; VAL-270; VAL-322
RP   AND GLN-376.
RC   STRAIN=Dorset Down, and Merino;
RX   PubMed=12580782; DOI=10.1046/j.1365-2052.2003.00936.x;
RA   Forrest R.H., Hickford J.G.H., Hogan A., Frampton C.;
RT   "Polymorphism at the ovine beta3-adrenergic receptor locus: associations
RT   with birth weight, growth rate, carcass composition and cold survival.";
RL   Anim. Genet. 34:19-25(2003).
CC   -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced
CC       activation of adenylate cyclase through the action of G proteins. Beta-
CC       3 is involved in the regulation of lipolysis and thermogenesis.
CC   -!- SUBUNIT: Interacts with ARRDC3. {ECO:0000250|UniProtKB:P13945}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRB3 sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF109928; AAD26147.1; -; Genomic_DNA.
DR   EMBL; AF314200; AAG31163.1; -; Genomic_DNA.
DR   EMBL; AF314201; AAG31164.1; -; Genomic_DNA.
DR   EMBL; AF314202; AAG31165.1; -; Genomic_DNA.
DR   EMBL; AF314203; AAG31166.1; -; Genomic_DNA.
DR   EMBL; AF314204; AAG31167.1; -; Genomic_DNA.
DR   EMBL; AF314205; AAG31168.1; -; Genomic_DNA.
DR   RefSeq; NP_001153229.1; NM_001159757.1.
DR   AlphaFoldDB; Q9XT58; -.
DR   SMR; Q9XT58; -.
DR   STRING; 9940.ENSOARP00000001138; -.
DR   GeneID; 100294559; -.
DR   KEGG; oas:100294559; -.
DR   CTD; 155; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   OrthoDB; 614199at2759; -.
DR   Proteomes; UP000002356; Unplaced.
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:0043235; C:receptor complex; ISS:HGNC-UCL.
DR   GO; GO:0004939; F:beta-adrenergic receptor activity; ISS:HGNC-UCL.
DR   GO; GO:0015052; F:beta3-adrenergic receptor activity; ISS:HGNC-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:HGNC-UCL.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:HGNC-UCL.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR000681; ADRB3_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00563; ADRENRGCB3AR.
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   3: Inferred from homology;
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..405
FT                   /note="Beta-3 adrenergic receptor"
FT                   /id="PRO_0000069149"
FT   TOPO_DOM        1..36
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        37..63
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        64..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        73..91
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        92..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        112..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        134..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        156..178
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        179..203
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        204..225
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        226..292
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        293..314
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        315..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        327..347
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        348..405
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          247..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           361
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        110..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        189..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         52
FT                   /note="V -> A (in allele B3AR-D)"
FT                   /evidence="ECO:0000269|PubMed:12580782"
FT   VARIANT         270
FT                   /note="A -> V (in allele B3AR-A and allele B3AR-B/F)"
FT                   /evidence="ECO:0000269|PubMed:12580782"
FT   VARIANT         322
FT                   /note="L -> V (in allele B3AR-D)"
FT                   /evidence="ECO:0000269|PubMed:12580782"
FT   VARIANT         376
FT                   /note="R -> Q (in allele B3AR-A)"
FT                   /evidence="ECO:0000269|PubMed:12580782"
FT   CONFLICT        10
FT                   /note="S -> F (in Ref. 1; AAD26147)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="A -> D (in Ref. 1; AAD26147)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   405 AA;  42928 MW;  A0DD3AEBAF814E75 CRC64;
     MAPWPPGNSS LTPWPDIPTL APNTANASGL PGVPWAVALA GALLALAVLA TVGGNLLVIV
     AIARTPRLQT MTNVFVTSLA TADLVVGLLV VPPGATLALT GHWPLGVTGC ELWTSVDVLC
     VTASIETLCA LAVDRYLAVT NPLRYGALVT KRRARAAVVL VWVVSAAVSF APIMSKWWRV
     GADAEAQRCH SNPRCCTFAS NMPYALLSSS VSFYLPLLVM LFVYARVFVV ATRQLRLLRR
     ELGRFPPEES PPAPSRSGSP GPAGPYASPA GVPSYGRRPA RLLPLREHRA LRTLGLIMGT
     FTLCWLPFFV VNVVRALGGP SLVSGPTFLA LNWLGYANSA FNPLIYCRSP DFRSAFRRLL
     CRCPPEEHLA AASPPRAPSG APTVLTSPAG PRQPSPLDGA SCGLS
 
 
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