P97718 (ADA1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-1A adrenergic receptor

Alternative name(s):
Alpha-1A adrenoreceptor
Short name=Alpha-1A adrenoceptor
Alpha-1C adrenergic receptor

Gene names

Name:	Adra1a
Synonyms:	Adra1c

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G11 proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes By similarity.
Subunit structure	Homo- and heterooligomer By similarity. Heterooligomerizes with ADRA1B homooligomers in cardiac myocytes By similarity.
Subcellular location	Nucleus membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein By similarity. Note: Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes By similarity. Ref.6
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA1A sub-subfamily.
Sequence caution	The sequence AAB47044.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Nucleus
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of phospholipase C activity Inferred from electronic annotation. Source: Compara adult heart development Inferred from genetic interaction PubMed 12782680. Source: MGI aging Inferred from electronic annotation. Source: Compara calcium ion transport into cytosol Inferred from electronic annotation. Source: Compara cell growth Inferred from genetic interaction PubMed 12782680. Source: MGI micturition Inferred from electronic annotation. Source: Compara negative regulation of Rho protein signal transduction Inferred from sequence orthology PubMed 18332105. Source: MGI negative regulation of heart rate involved in baroreceptor response to increased systemic arterial blood pressure Inferred from mutant phenotype PubMed 12093905. Source: MGI negative regulation of synaptic transmission, GABAergic Inferred from electronic annotation. Source: Compara norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure Inferred from mutant phenotype PubMed 12093905. Source: MGI organ growth Inferred from genetic interaction PubMed 12782680. Source: MGI phospholipase C-activating G-protein coupled receptor signaling pathway Inferred from direct assay PubMed 9590558. Source: MGI pilomotor reflex Inferred from direct assay PubMed 21335239. Source: BHF-UCL positive regulation of ERK1 and ERK2 cascade Inferred from electronic annotation. Source: Compara positive regulation of MAPK cascade Inferred from genetic interaction PubMed 12782680. Source: MGI positive regulation of action potential Inferred from electronic annotation. Source: Compara positive regulation of cardiac muscle contraction Inferred from electronic annotation. Source: Compara positive regulation of heart rate by epinephrine-norepinephrine Inferred from genetic interaction PubMed 12782680. Source: MGI positive regulation of protein kinase C signaling cascade Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle contraction Inferred from direct assay PubMed 21335239. Source: BHF-UCL positive regulation of systemic arterial blood pressure Inferred from electronic annotation. Source: Compara positive regulation of the force of heart contraction by epinephrine-norepinephrine Inferred from genetic interaction PubMed 12595294. Source: MGI positive regulation of vasoconstriction Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to hormone stimulus Inferred from electronic annotation. Source: Compara response to stress Inferred from electronic annotation. Source: Compara
Cellular_component	T-tubule Inferred from electronic annotation. Source: Compara Z disc Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	alpha1-adrenergic receptor activity Inferred from direct assay Ref.1. Source: MGI protein heterodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 466	466	Alpha-1A adrenergic receptor		PRO_0000069064
Regions
	Topological domain	1 – 27	27	Extracellular By similarity
	Transmembrane	28 – 51	24	Helical; Name=1; By similarity
	Topological domain	52 – 64	13	Cytoplasmic By similarity
	Transmembrane	65 – 88	24	Helical; Name=2; By similarity
	Topological domain	89 – 99	11	Extracellular By similarity
	Transmembrane	100 – 122	23	Helical; Name=3; By similarity
	Topological domain	123 – 143	21	Cytoplasmic By similarity
	Transmembrane	144 – 167	24	Helical; Name=4; By similarity
	Topological domain	168 – 181	14	Extracellular By similarity
	Transmembrane	182 – 205	24	Helical; Name=5; By similarity
	Topological domain	206 – 273	68	Cytoplasmic By similarity
	Transmembrane	274 – 297	24	Helical; Name=6; By similarity
	Topological domain	298 – 305	8	Extracellular By similarity
	Transmembrane	306 – 329	24	Helical; Name=7; By similarity
	Topological domain	330 – 466	137	Cytoplasmic By similarity
	Region	334 – 349	16	Nuclear localization signal By similarity
Amino acid modifications
	Modified residue	215	1	Phosphoserine; by PKA Potential
	Lipidation	345	1	S-palmitoyl cysteine Potential
	Glycosylation	7	1	N-linked (GlcNAc...) Potential
	Glycosylation	13	1	N-linked (GlcNAc...) Potential
	Glycosylation	22	1	N-linked (GlcNAc...) Potential
	Disulfide bond	99 ↔ 176		By similarity
Experimental info
	Sequence conflict	369	1	G → E in AAC02658. Ref.1
	Sequence conflict	395	1	R → C in AAC02658. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P97718 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 8C5FE5C67E885795	FASTA	466	51,744
	10 20 30 40 50 60 MVLLSENASE GSNCTHPPAQ VNISKAILLG VILGGLIIFG VLGNILVILS VACHRHLHSV 70 80 90 100 110 120 THYYIVNLAV ADLLLTSTVL PFSAIFEILG YWAFGRVFCN IWAAVDVLCC TASIMGLCII 130 140 150 160 170 180 SIDRYIGVSY PLRYPTIVTQ RRGVRALLCV WALSLVISIG PLFGWRQQAP EDETICQINE 190 200 210 220 230 240 EPGYVLFSAL GSFYVPLTII LVMYCRVYVV AKRESRGLKS GLKTDKSDSE QVTLRIHRKN 250 260 270 280 290 300 VPAEGSGVSS AKNKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIGSFFPN 310 320 330 340 350 360 FKPPETVFKI VFWLGYLNSC INPIIYPCSS QEFKKAFQNV LRIQCLRRRQ SSKHALGYTL 370 380 390 400 410 420 HPPSQAVEGQ HRGMVRIPVG SGETFYKISK TDGVREWKFF SSMPQGSARI TMPKDQSACT 430 440 450 460 TARVRSKSFL QVCCCVGSST PRPEENHQVP TIKIHTISLG ENGEEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, expression and characterization of cDNA encoding a mouse alpha1a-adrenoceptor." Xiao L., Scofield M.A., Jeffries W.B. Br. J. Pharmacol. 124:213-221(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Strain: CD-1. Tissue: Brain and Kidney.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Spinal cord.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Molecular cloning of alpha 1d-adrenergic receptor and tissue distribution of three alpha 1-adrenergic receptor subtypes in mouse." Alonso-Llamazares A., Zamanillo D., Casanova E., Ovalle S., Calvo P., Chinchetru M.A. J. Neurochem. 65:2387-2392(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 197-280. Tissue: Brain.
[6]	"Nuclear localization drives alpha1-adrenergic receptor oligomerization and signaling in cardiac myocytes." Wright C.D., Wu S.C., Dahl E.F., Sazama A.J., O'Connell T.D. Cell. Signal. 24:794-802(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF031431 mRNA. Translation: AAC02658.1. AK079597 mRNA. Translation: BAC37694.1. CH466535 Genomic DNA. Translation: EDL35992.1. BC113139 mRNA. Translation: AAI13140.1. S80220 mRNA. Translation: AAB47044.1. Different initiation.
IPI	IPI00128843.
RefSeq	NP_001258689.1. NM_001271760.1. NP_038489.2. NM_013461.4.
UniGene	Mm.57064.
3D structure databases
ProteinModelPortal	P97718.
SMR	P97718. Positions 29-341.
ModBase	Search...
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P97718.
Proteomic databases
PRIDE	P97718.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000054661; ENSMUSP00000053703; ENSMUSG00000045875. ENSMUST00000159068; ENSMUSP00000124570; ENSMUSG00000045875. ENSMUST00000161339; ENSMUSP00000125354; ENSMUSG00000045875.
GeneID	11549.
KEGG	mmu:11549.
Organism-specific databases
CTD	148.
MGI	MGI:104773. Adra1a.
Phylogenomic databases
eggNOG	NOG253615.
GeneTree	ENSGT00700000104182.
HOGENOM	HOG000239244.
HOVERGEN	HBG106962.
InParanoid	Q8BV77.
KO	K04135.
OMA	NCTHPPA.
OrthoDB	EOG40VVPS.
Gene expression databases
ArrayExpress	P97718.
Bgee	P97718.
CleanEx	MM_ADRA1A.
Genevestigator	P97718.
GermOnline	ENSMUSG00000045875. Mus musculus.
Family and domain databases
InterPro	IPR001004. Adrene_rcpt_A1Cs. IPR002233. Adrnrgc_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR01103. ADRENERGICR. PR00557. ADRENRGCA1AR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P97718.
ChEMBL	CHEMBL2822.
NextBio	279030.
SOURCE	Search...

Entry information

Entry name

ADA1A_MOUSE

Accession

Primary (citable) accession number: P97718
Secondary accession number(s): O54913, Q8BV77

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program