Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9103-01021
Entry Name
UniProt Accession
Theoretical PI
9.31
Molecular Weight
54078.2
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Beta-1 adrenergic receptor
Protein Synonyms/Alias
Beta-1 adrenoreceptor; Beta-1 adrenoceptor; Beta-T;
Gene Name
ADRB1
Gene Synonyms/Alias
Created Date
01-APR-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
358
Canonical
KAFKRLLCFPRKADR
[1]
S-Palmitoylation
Organism
Meleagris gallopavo (Common turkey)
NCBI Taxa ID
9103
Reference
[1] Warne T, Serrano-Vega MJ, Tate CG, Schertler GF. Development andcrystallization of a minimal thermostabilised G protein-coupled receptor. ProteinExpr Purif. 2009 Jun;65(2):204-13.[PMID:19297694]
Functional Description
Beta-adrenergic receptors mediate the catecholamine- induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity.
Sequence Annotation
Topological domain: 1 38 Extracellular.
Transmembrane: 39 67 Helical; Name=1.
Topological domain: 68 76 Cytoplasmic.
Transmembrane: 77 103 Helical; Name=2.
Topological domain: 104 115 Extracellular.
Transmembrane: 116 137 Helical; Name=3.
Topological domain: 138 155 Cytoplasmic.
Transmembrane: 156 179 Helical; Name=4.
Topological domain: 180 205 Extracellular.
Transmembrane: 206 231 Helical; Name=5.
Topological domain: 232 285 Cytoplasmic.
Transmembrane: 286 315 Helical; Name=6.
Topological domain: 316 320 Extracellular.
Transmembrane: 321 343 Helical; Name=7.
Topological domain: 344 483 Cytoplasmic.
Region: 201 215 Agonist and antagonist binding.
Region: 303 310 Agonist and antagonist binding.
Region: 329 333 Agonist and antagonist binding.
Binding site: 121 121 Agonist or antagonist.
Binding site: 126 126 Agonist or antagonist.
Protein Length
483 AA.
Protein Sequence
(Canonical)
MGDGWLPPDC GPHNRSGGGG ATAAPTGSRQ VSAELLSQQW EAGMSLLMAL VVLLIVAGNV  60
LVIAAIGRTQ RLQTLTNLFI TSLACADLVM GLLVVPFGAT LVVRGTWLWG SFLCECWTSL  120
DVLCVTASIE TLCVIAIDRY LAITSPFRYQ SLMTRARAKV IICTVWAISA LVSFLPIMMH  180
WWRDEDPQAL KCYQDPGCCD FVTNRAYAIA SSIISFYIPL LIMIFVYLRV YREAKEQIRK  240
IDRCEGRFYG SQEQPQPPPL PQHQPILGNG RASKRKTSRV MAMREHKALK TLGIIMGVFT  300
LCWLPFFLVN IVNVFNRDLV PDWLFVFFNW LGYANSAFNP IIYCRSPDFR KAFKRLLCFP  360
RKADRRLHAG GQPAPLPGGF ISTLGSPEHS PGGTWSDCNG GTRGGSESSL EERHSKTSRS  420
ESKMEREKNI LATTRFYCTF LGNGDKAVFC TVLRIVKLFE DATCTCPHTH KLKMKWRFKQ  480
HQA                                                                483
FASTA
(Canonical)
>LipidDB-9103-01021|P07700
MGDGWLPPDCGPHNRSGGGGATAAPTGSRQVSAELLSQQWEAGMSLLMALVVLLIVAGNV
LVIAAIGRTQRLQTLTNLFITSLACADLVMGLLVVPFGATLVVRGTWLWGSFLCECWTSL
DVLCVTASIETLCVIAIDRYLAITSPFRYQSLMTRARAKVIICTVWAISALVSFLPIMMH
WWRDEDPQALKCYQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVYLRVYREAKEQIRK
IDRCEGRFYGSQEQPQPPPLPQHQPILGNGRASKRKTSRVMAMREHKALKTLGIIMGVFT
LCWLPFFLVNIVNVFNRDLVPDWLFVFFNWLGYANSAFNPIIYCRSPDFRKAFKRLLCFP
RKADRRLHAGGQPAPLPGGFISTLGSPEHSPGGTWSDCNGGTRGGSESSLEERHSKTSRS
ESKMEREKNILATTRFYCTFLGNGDKAVFCTVLRIVKLFEDATCTCPHTHKLKMKWRFKQ
HQA
Gene Ontology
GO:0005769; C:early endosome; ISS:UniProtKB
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; ISS:UniProtKB
GO:0004940; F:beta1-adrenergic receptor activity; IEA:InterPro
GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; ISS:UniProtKB
GO:0005057; F:receptor signaling protein activity; ISS:UniProtKB
GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB
GO:0035556; P:intracellular signal transduction; ISS:GOC
GO:0030819; P:positive regulation of cAMP biosynthetic process; ISS:UniProtKB
GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB
GO:0045823; P:positive regulation of heart contraction; IEA:InterPro
GO:0032320; P:positive regulation of Ras GTPase activity; ISS:UniProtKB
Interpro
InterPro; IPR002233; ADR_fam
InterPro; IPR000507; ADRB1_rcpt
InterPro; IPR000276; GPCR_Rhodpsn
InterPro; IPR017452; GPCR_Rhodpsn_7TM
Pfam
Pfam; PF00001; 7tm_1;
SMART
PROSITE
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1;
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2;
PRINTS
PRINTS; PR01103; ADRENERGICR;
PRINTS; PR00561; ADRENRGCB1AR;
PRINTS; PR00237; GPCRRHODOPSN;