Beta-3 adrenergic receptor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P13945 (ADRB3_HUMAN)

Last modified July 22, 2008. Version 102. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Beta-3 adrenergic receptor
Alternative name(s):
    Beta-3 adrenoreceptor
      Short name=Beta-3 adrenoceptor

Gene names

Name:	ADRB3
Synonyms:	ADRB3R, B3AR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Expressed mainly in adipose tissues.
Polymorphism	The variant Arg-64 seems to be associated with weight gain (obesity) and to is also associated with susceptibility to non-insulin-dependent diabetes mellitus (NIDDM).
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

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Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Disease	Diabetes mellitus Obesity
Domain	Transmembrane
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	G-protein signaling, coupled to cAMP nucleotide second messenger Traceable author statement. Source: ProtInc activation of adenylate cyclase activity Inferred from direct assay. Source: HGNC carbohydrate metabolic process Ref.1 Traceable author statement. Source: ProtInc energy reserve metabolic process Traceable author statement. Source: ProtInc positive regulation of MAPKKK cascade Inferred from direct assay. Source: HGNC
Cellular component	integral to plasma membrane Traceable author statement. Source: ProtInc receptor complex Inferred from direct assay. Source: HGNC
Molecular function	beta3-adrenergic receptor activity Inferred from mutant phenotype. Source: HGNC protein homodimerization activity Inferred from direct assay. Source: HGNC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 408

408

Beta-3 adrenergic receptor

Regions

Topological domain

1 – 36

Extracellular Potential

Transmembrane

37 – 63

1 Potential

Topological domain

64 – 72

Cytoplasmic Potential

Transmembrane

73 – 91

2 Potential

Topological domain

92 – 111

Extracellular Potential

Transmembrane

112 – 133

3 Potential

Topological domain

134 – 155

Cytoplasmic Potential

Transmembrane

156 – 178

4 Potential

Topological domain

179 – 203

Extracellular Potential

Transmembrane

204 – 225

5 Potential

Topological domain

226 – 292

Cytoplasmic Potential

Transmembrane

293 – 314

6 Potential

Topological domain

315 – 326

Extracellular Potential

Transmembrane

327 – 347

7 Potential

Topological domain

348 – 408

Cytoplasmic Potential

Amino acid modifications

Lipidation

361

S-palmitoyl cysteine By similarity

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

110 ↔ 189

By similarity

Natural variations

Natural variant

W → R: dbSNP rs4994.

Natural variant

249

E → K

Natural variant

265

T → M: dbSNP rs4995.

Natural variant

353

R → C

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Sequences

Sequence

Length

Mass (Da)

Tools

P13945-1 [UniParc].

Last modified February 1, 1994. Version 3.
Checksum: E98BD6C130DD977B
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FASTA

408

43,519

        10         20         30         40         50         60 
MAPWPHENSS LAPWPDLPTL APNTANTSGL PGVPWEAALA GALLALAVLA TVGGNLLVIV 

        70         80         90        100        110        120 
AIAWTPRLQT MTNVFVTSLA AADLVMGLLV VPPAATLALT GHWPLGATGC ELWTSVDVLC 

       130        140        150        160        170        180 
VTASIETLCA LAVDRYLAVT NPLRYGALVT KRCARTAVVL VWVVSAAVSF APIMSQWWRV 

       190        200        210        220        230        240 
GADAEAQRCH SNPRCCAFAS NMPYVLLSSS VSFYLPLLVM LFVYARVFVV ATRQLRLLRG 

       250        260        270        280        290        300 
ELGRFPPEES PPAPSRSLAP APVGTCAPPE GVPACGRRPA RLLPLREHRA LCTLGLIMGT 

       310        320        330        340        350        360 
FTLCWLPFFL ANVLRALGGP SLVPGPAFLA LNWLGYANSA FNPLIYCRSP DFRSAFRRLL 

       370        380        390        400 
CRCGRRLPPE PCAAARPALF PSGVPAARSS PAQPRLCQRL DGASWGVS

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of the human beta 3-adrenergic receptor." Emorine L.J., Marullo S., Briend-Sutren M.-M., Patey G., Tate K., Delavier-Klutchko C., Strosberg A.D. Science 245:1118-1121(1989) [PubMed: 2570461] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The promoter and intron/exon structure of the human and mouse beta 3-adrenergic-receptor genes." van Spronsen A., Nahmias C., Krief S., Briend-Sutren M.-M., Strosberg A.D., Emorine L.J. Eur. J. Biochem. 213:1117-1124(1993) [PubMed: 8389293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
[3]	"Molecular cloning of a human beta 3-adrenergic receptor cDNA." Lelias J.M., Kaghad M., Rodriguez M., Chalon P., Bonnin J., Dupre I., Delpech B., Bensaid M., Lefur G., Ferrara P., Caput D. FEBS Lett. 324:127-130(1993) [PubMed: 8389717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Kopatz S.A., Aronstam R.S., Sharma S.V. Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	SeattleSNPs program for genomic applications Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-64 AND CYS-353.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Rodent and human beta 3-adrenergic receptor genes contain an intron within the protein-coding block." Granneman J.G., Lahners K.N., Rao D.D. Mol. Pharmacol. 42:964-970(1992) [PubMed: 1336117] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 392-408.
[8]	"Genetic variation in the beta 3-adrenergic receptor and an increased capacity to gain weight in patients with morbid obesity." Clement K., Vaisse C., Manning B.S.J., Basdevant A., Guy-Grand B., Ruiz J., Silver K.D., Shuldiner A.R., Froguel P., Strosberg A.D. N. Engl. J. Med. 333:352-354(1995) [PubMed: 7609752] [Abstract] Cited for: VARIANT ARG-64.
[9]	"Association of Trp64Arg mutation of the beta3-adrenergic-receptor with NIDDM and body weight gain." Fujisawa T., Ikegami H., Yamato E., Takekawa K., Nakagawa Y., Hamada Y., Oga T., Ueda H., Shintani M., Fukuda M., Ogihara T. Diabetologia 39:349-352(1996) [PubMed: 8721782] [Abstract] Cited for: VARIANT ARG-64.
[10]	"Pharmacological characterization of a recently described human beta 3-adrenergic receptor mutant." Candelore M.R., Deng L., Tota L.M., Kelly L.J., Cascieri M.A., Strader C.D. Endocrinology 137:2638-2641(1996) [PubMed: 8641219] [Abstract] Cited for: VARIANT ARG-64.
[11]	"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis." Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A. Nat. Genet. 22:239-247(1999) [PubMed: 10391210] [Abstract] Cited for: VARIANTS ARG-64 AND MET-265.
+	Additional computationally mapped references.

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Web resources

SeattleSNPs

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Cross-references

Sequence databases

M29932 Genomic DNA. Translation: AAA35550.1. Different termination.
X72861 Genomic DNA. Translation: CAA51383.1.
X70811 mRNA. Translation: CAA50141.1.
X70812 Genomic DNA. Translation: CAA50142.1. Sequence problems.
X70812 Genomic DNA. Translation: CAA50143.1. Sequence problems.
AY487247 mRNA. Translation: AAR37414.1.
DQ104441 Genomic DNA. Translation: AAY88743.1.
BC075017 mRNA. Translation: AAH75017.1.
S53291 mRNA. Translation: AAB24837.1.

PIR

I57941.
QRHUBE. S33751.

RefSeq

NP_000016.1.

UniGene

Hs.2549

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CDW	model	-	A	1-408	[»]

ModBase

Search...

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P13945.

Genome annotation databases

Ensembl

ENSG00000188778. Homo sapiens. [Contig view]

GeneID

155.

KEGG

hsa:155.

Organism-specific databases

H-InvDB

HIX0034321.

HGNC

HGNC:288. ADRB3.

MIM

109691. gene.

PharmGKB

PA24598.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P13945.

HOVERGEN

P13945.

Gene expression databases

ArrayExpress

P13945.

CleanEx

HS_ADRB3.

GermOnline

ENSG00000188778. Homo sapiens.

Family and domain databases

InterPro

IPR000681. Adrgc_rcpt_B3.
IPR002233. Adrnrgc_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_supfam.
[Graphical view]

PANTHER

PTHR19266:SF44. Adrgc_rcpt_B3. 1 hit.

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR01103. ADRENERGICR.
PR00563. ADRENRGCB3AR.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProDom

P13945.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

DrugBank

DB00368. Norepinephrine.
DB00960. Pindolol.
DB00571. Propranolol.

SOURCE

Search...

ProtoNet

Search...

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Entry information

Entry name

ADRB3_HUMAN

Accession

Primary (citable) accession number: P13945
Secondary accession number(s): Q4JFT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 1, 1994
Last modified:	July 22, 2008
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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