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P35348 (ADA1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1A adrenergic receptor
Alternative name(s):
Alpha-1A adrenoreceptor
Short name=Alpha-1A adrenoceptor
Alpha-1C adrenergic receptor
Alpha-adrenergic receptor 1c
Gene names
Name:ADRA1A
Synonyms:ADRA1C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.16 Ref.17

Subunit structure

Homo- and heterooligomer. Heterooligomerizes with ADRA1B homooligomers in cardiac myocytes. Ref.17

Subcellular location

Nucleus membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. 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. Ref.16 Ref.17

Tissue specificity

Expressed in heart, brain, liver and prostate, but not in kidney, lung, adrenal, aorta and pituitary. Within the prostate, expressed in the apex, base, periurethral and lateral lobe. Isoform 4 is the most abundant isoform expressedin the prostate with high levels also detected in liver and heart. Ref.5 Ref.7 Ref.15

Post-translational modification

C-terminal Ser or Thr residues may be phosphorylated By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA1A sub-subfamily.

Sequence caution

Isoform 2: The sequence BAA06901.1 differs from that shown. Reason: Frameshift at position 465.

Isoform 2: The sequence ACA05900.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of phospholipase C activity

Inferred from sequence or structural similarity. Source: BHF-UCL

adult heart development

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from sequence or structural similarity. Source: BHF-UCL

apoptotic process

Traceable author statement PubMed 10671514. Source: ProtInc

calcium ion transport into cytosol

Inferred from sequence or structural similarity. Source: BHF-UCL

cell growth

Inferred from electronic annotation. Source: Ensembl

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

intracellular signal transduction

Traceable author statement PubMed 10671514. Source: ProtInc

micturition

Inferred from electronic annotation. Source: Ensembl

negative regulation of Rho protein signal transduction

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cell proliferation

Traceable author statement PubMed 10860850. Source: ProtInc

negative regulation of heart rate involved in baroreceptor response to increased systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

negative regulation of synaptic transmission, GABAergic

Inferred from sequence or structural similarity. Source: BHF-UCL

norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

organ growth

Inferred from electronic annotation. Source: Ensembl

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

pilomotor reflex

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of action potential

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cardiac muscle contraction

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of heart rate by epinephrine-norepinephrine

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase C signaling

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

positive regulation of the force of heart contraction by epinephrine-norepinephrine

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasoconstriction

Inferred from sequence or structural similarity. Source: BHF-UCL

response to drug

Inferred from sequence or structural similarity. Source: BHF-UCL

response to hormone

Inferred from sequence or structural similarity. Source: BHF-UCL

smooth muscle contraction

Traceable author statement Ref.3. Source: ProtInc

   Cellular_componentT-tubule

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

nuclear membrane

Inferred from direct assay Ref.17. Source: UniProtKB

   Molecular_functionalpha1-adrenergic receptor activity

Non-traceable author statement Ref.7. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35348-1)

Also known as: Alpha 1c-1; Alpha(1A-1);

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P35348-2)

Also known as: Alpha 1c-2; Alpha(1A-2);

The sequence of this isoform differs from the canonical sequence as follows:
     424-466: VRSKSFLQVC...ISLSENGEEV → TKSRSVTRLE...CHQADATRPS
Isoform 3 (identifier: P35348-3)

Also known as: Alpha 1c-3; Alpha(1A-3);

The sequence of this isoform differs from the canonical sequence as follows:
     424-429: VRSKSF → GHTPMT
     430-466: Missing.
Isoform 4 (identifier: P35348-4)

Also known as: Alpha(1A-4);

The sequence of this isoform differs from the canonical sequence as follows:
     424-466: VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV → RGMDCRYFTKNCREHIKHVNFMMPPWRKGSEC
Isoform 5 (identifier: P35348-5)

The sequence of this isoform differs from the canonical sequence as follows:
     296-297: SF → KS
     298-466: Missing.
Isoform 6 (identifier: P35348-6)

The sequence of this isoform differs from the canonical sequence as follows:
     295-342: GSFFPDFKPS...FKKAFQNVLR → DEETEAQEGK...VSRKDTCGVW
     343-466: Missing.
Isoform 7 (identifier: P35348-7)

Also known as: 2b/3b;

The sequence of this isoform differs from the canonical sequence as follows:
     296-324: SFFPDFKPSETVFKIVFWLGYLNSCINPI → TYILKYDVLFWRKGLSVCTRLRERKEIKN
     325-466: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 8 (identifier: P35348-8)

Also known as: 2c;

The sequence of this isoform differs from the canonical sequence as follows:
     295-466: GSFFPDFKPS...ISLSENGEEV → DEVSLCHQAG...GQDDLDLLTS
Isoform 9 (identifier: P35348-9)

Also known as: 3c;

The sequence of this isoform differs from the canonical sequence as follows:
     296-466: SFFPDFKPSE...ISLSENGEEV → THTHDMKPAS...TVTDTGKTVT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Alpha-1A adrenergic receptor
PRO_0000069063

Regions

Topological domain1 – 2727Extracellular By similarity
Transmembrane28 – 5124Helical; Name=1; By similarity
Topological domain52 – 6413Cytoplasmic By similarity
Transmembrane65 – 8824Helical; Name=2; By similarity
Topological domain89 – 9911Extracellular By similarity
Transmembrane100 – 12223Helical; Name=3; By similarity
Topological domain123 – 14321Cytoplasmic By similarity
Transmembrane144 – 16724Helical; Name=4; By similarity
Topological domain168 – 18114Extracellular By similarity
Transmembrane182 – 20524Helical; Name=5; By similarity
Topological domain206 – 27368Cytoplasmic By similarity
Transmembrane274 – 29724Helical; Name=6; By similarity
Topological domain298 – 3058Extracellular By similarity
Transmembrane306 – 32924Helical; Name=7; By similarity
Topological domain330 – 466137Cytoplasmic By similarity
Region334 – 34916Nuclear localization signal

Amino acid modifications

Modified residue2151Phosphoserine; by PKA Potential
Lipidation3451S-palmitoyl cysteine Potential
Glycosylation71N-linked (GlcNAc...) Potential
Glycosylation131N-linked (GlcNAc...) Potential
Glycosylation221N-linked (GlcNAc...) Potential
Disulfide bond99 ↔ 176 By similarity

Natural variations

Alternative sequence295 – 466172GSFFP…NGEEV → DEVSLCHQAGVQWHDLGSLQ PPPPGFKRFSCLSLPSSWDY RDVPPGRRHQAQLIFVFLVE TGFHHVGQDDLDLLTS in isoform 8.
VSP_011046
Alternative sequence295 – 34248GSFFP…QNVLR → DEETEAQEGKNDSPSFKQPV HHAAVLGLEVMEKENLEGVS RKDTCGVW in isoform 6.
VSP_011053
Alternative sequence296 – 466171SFFPD…NGEEV → THTHDMKPASRPRLLSLLPK EGEHETHHWSCDPLSLESTP GAQEPCLTLGFTSLSSIHLT KAQIQHVTVTDTGKTVT in isoform 9.
VSP_011049
Alternative sequence296 – 32429SFFPD…CINPI → TYILKYDVLFWRKGLSVCTR LRERKEIKN in isoform 7.
VSP_011047
Alternative sequence296 – 2972SF → KS in isoform 5.
VSP_011051
Alternative sequence298 – 466169Missing in isoform 5.
VSP_011052
Alternative sequence325 – 466142Missing in isoform 7.
VSP_011048
Alternative sequence343 – 466124Missing in isoform 6.
VSP_011054
Alternative sequence424 – 46643VRSKS…NGEEV → TKSRSVTRLECSGMILAHCN LRLPGSRDSPASASQAAGTT GMCHQADATRPS in isoform 2.
VSP_011055
Alternative sequence424 – 46643VRSKS…NGEEV → RGMDCRYFTKNCREHIKHVN FMMPPWRKGSEC in isoform 4.
VSP_011050
Alternative sequence424 – 4296VRSKSF → GHTPMT in isoform 3.
VSP_011044
Alternative sequence430 – 46637Missing in isoform 3.
VSP_011045
Natural variant401G → W in a breast cancer sample; somatic mutation. Ref.20
VAR_035756
Natural variant2001I → S.
Corresponds to variant rs2229125 [ dbSNP | Ensembl ].
VAR_049370
Natural variant3471C → R Frequent polymorphism. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.14 Ref.15 Ref.18 Ref.19
Corresponds to variant rs1048101 [ dbSNP | Ensembl ].
VAR_019509
Natural variant4141K → R.
Corresponds to variant rs3730247 [ dbSNP | Ensembl ].
VAR_049371
Natural variant4651E → D.
Corresponds to variant rs2229126 [ dbSNP | Ensembl ].
VAR_049372

Experimental info

Mutagenesis3341K → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-335; A-342; A-348 and A-349. Ref.17
Mutagenesis3351K → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-342; A-348 and A-349. Ref.17
Mutagenesis3421R → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-348 and A-349. Ref.17
Mutagenesis3481R → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-349. Ref.17
Mutagenesis3491K → A: Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-348. Ref.17
Sequence conflict431G → C in AAA93114. Ref.4
Sequence conflict1291S → T in AAA93114. Ref.4
Sequence conflict1301Y → H in AAK77197. Ref.9
Sequence conflict1851V → A in AAH95512. Ref.14
Sequence conflict3381Q → C Ref.2
Sequence conflict3591T → P in AAA93114. Ref.4
Sequence conflict3841T → A in AAK77197. Ref.9
Sequence conflict3871R → G in AAK77197. Ref.9
Sequence conflict3901K → R in AAK77197. Ref.9
Sequence conflict4311Q → E in BAA04960. Ref.1
Sequence conflict4371G → E in AAK77197. Ref.9
Sequence conflict4421S → C in AAA93114. Ref.4
Isoform 4:
Sequence conflict4531S → L in AAC06138. Ref.7
Isoform 6:
Sequence conflict3021E → Q in AAR84650. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha 1c-1) (Alpha(1A-1)) [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 1A50487531DECDF0

FASTA46651,487
        10         20         30         40         50         60 
MVFLSGNASD SSNCTQPPAP VNISKAILLG VILGGLILFG VLGNILVILS VACHRHLHSV 

        70         80         90        100        110        120 
THYYIVNLAV ADLLLTSTVL PFSAIFEVLG YWAFGRVFCN IWAAVDVLCC TASIMGLCII 

       130        140        150        160        170        180 
SIDRYIGVSY PLRYPTIVTQ RRGLMALLCV WALSLVISIG PLFGWRQPAP EDETICQINE 

       190        200        210        220        230        240 
EPGYVLFSAL GSFYLPLAII LVMYCRVYVV AKRESRGLKS GLKTDKSDSE QVTLRIHRKN 

       250        260        270        280        290        300 
APAGGSGMAS AKTKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIGSFFPD 

       310        320        330        340        350        360 
FKPSETVFKI VFWLGYLNSC INPIIYPCSS QEFKKAFQNV LRIQCLCRKQ SSKHALGYTL 

       370        380        390        400        410        420 
HPPSQAVEGQ HKDMVRIPVG SRETFYRISK TDGVCEWKFF SSMPRGSARI TVSKDQSSCT 

       430        440        450        460 
TARVRSKSFL QVCCCVGPST PSLDKNHQVP TIKVHTISLS ENGEEV 

« Hide

Isoform 2 (Alpha 1c-2) (Alpha(1A-2)) [UniParc].

Checksum: DE3CEEDD1AB3E56D
Show »

FASTA47552,205
Isoform 3 (Alpha 1c-3) (Alpha(1A-3)) [UniParc].

Checksum: E67B19B5CA668687
Show »

FASTA42947,461
Isoform 4 (Alpha(1A-4)) [UniParc].

Checksum: 80C61B88FA608B6C
Show »

FASTA45550,777
Isoform 5 [UniParc].

Checksum: 4871F9BE42A87D6E
Show »

FASTA29732,433
Isoform 6 [UniParc].

Checksum: 2B6E7CC81B9CBE50
Show »

FASTA34237,468
Isoform 7 (2b/3b) [UniParc].

Checksum: 608DACD5497EE83E
Show »

FASTA32435,829
Isoform 8 (2c) [UniParc].

Checksum: F00E717A4C4A59AC
Show »

FASTA37040,725
Isoform 9 (3c) [UniParc].

Checksum: 839C5750F9B428F5
Show »

FASTA37240,638

References

« Hide 'large scale' references
[1]"Cloning, functional expression and tissue distribution of human cDNA for the alpha 1C-adrenergic receptor."
Hirasawa A., Horie K., Tanaka T., Takagaki K., Murai M., Yano J., Tsujimoto G.
Biochem. Biophys. Res. Commun. 195:902-909(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT ARG-347.
Tissue: Prostate.
[2]"Cloning, expression and characterization of human alpha adrenergic receptors alpha 1a, alpha 1b and alpha 1c."
Weinberg D.H., Trivedi P., Tan C.P., Mitra S., Perkins-Barrow A., Borkowski D., Strader C.D., Bayne M.
Biochem. Biophys. Res. Commun. 201:1296-1304(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-347.
Tissue: Heart.
[3]"The alpha 1-adrenergic receptor that mediates smooth muscle contraction in human prostate has the pharmacological properties of the cloned human alpha 1c subtype."
Forray C., Bard J.A., Wetzel J.M., Chiu G., Shapiro E., Tang R., Lepor H., Hartig P.R., Weinshank R.L., Branchek T.A., Gluchowski C.
Mol. Pharmacol. 45:703-708(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Tissue: Hippocampus and Lymphocyte.
[4]"The alpha 1C-adrenoceptor in human prostate: cloning, functional expression, and localization to specific prostatic cell types."
Tseng-Crank J., Kost T., Goetz A., Hazum S., Roberson K.M., Haizlip J., Godinot N., Robertson C.N., Saussy D.
Br. J. Pharmacol. 115:1475-1485(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-347.
[5]"Cloning, functional expression and tissue distribution of human alpha 1c-adrenoceptor splice variants."
Hirasawa A., Shibata K., Horie K., Takei Y., Obika K., Tanaka T., Muramoto N., Takagaki K., Yano J., Tsujimoto G.
FEBS Lett. 363:256-260(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANT ARG-347, TISSUE SPECIFICITY.
Tissue: Prostate.
[6]"Cloning and pharmacological characterization of human alpha-1 adrenergic receptors: sequence corrections and direct comparison with other species homologues."
Schwinn D.A., Johnston G.I., Page S.O., Mosley M.J., Wilson K.H., Worman N.P., Campbell S., Fidock M.D., Furness L.M., Parry-Smith D.J., Peter B., Bailey D.S.
J. Pharmacol. Exp. Ther. 272:134-142(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-347.
[7]"Molecular cloning, genomic characterization and expression of novel human alpha1A-adrenoceptor isoforms."
Chang D.J., Chang T.K., Yamanishi S.S., Salazar F.H.R., Kosaka A.H., Khare R., Bhakta S., Jasper J.R., Shieh I.-S., Lesnick J.D., Ford A.P.D.W., Daniels D.V., Clarke D.E., Bach C.T., Chan H.W.
FEBS Lett. 422:279-283(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
Tissue: Prostate.
[8]"Truncated isoforms inhibit [3H]prazosin binding and cellular trafficking of native human alpha1A-adrenoceptors."
Coge F., Guenin S.P., Renouard-Try A., Rique H., Ouvry C., Fabry N., Beauverger P., Nicolas J.P., Galizzi J.-P., Boutin J.A., Canet E.
Biochem. J. 343:231-239(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7; 8 AND 9).
Tissue: Liver.
[9]"RT-PCR cloning and sequence analysis of adrenergic receptor subtype-alpha-1a cDNA from human prostrate cell-line DU-145."
Banerjee A.G.N., Aarti A.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[10]"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes."
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]"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 (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[12]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cerebellum.
[13]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[14]"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] (ISOFORM 1), VARIANT ARG-347.
[15]"Identification of alpha 1-adrenoceptor subtypes present in the human prostate."
Faure C., Pimoule C., Vallancien G., Langer S.Z., Graham D.
Life Sci. 54:1595-1605(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-400 (ISOFORMS 1/2/3/4), TISSUE SPECIFICITY, VARIANT ARG-347.
Tissue: Prostate.
[16]"Nuclear alpha1-adrenergic receptors signal activated ERK localization to caveolae in adult cardiac myocytes."
Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S., O'Connell T.D.
Circ. Res. 103:992-1000(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[17]"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, SUBUNIT, FUNCTION, MUTAGENESIS OF LYS-334; LYS-335; ARG-342; ARG-348 AND LYS-349.
[18]"Alpha 1a-adrenoceptor polymorphism: pharmacological characterization and association with benign prostatic hypertrophy."
Shibata K., Hirasawa A., Moriyama N., Kawabe K., Ogawa S., Tsujimoto G.
Br. J. Pharmacol. 118:1403-1408(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-347.
[19]"Alpha 1A-adrenergic receptor polymorphism and vascular response."
Sofowora G.G., Dishy V., Landau R., Xie H.G., Prasad H.C., Byrne D.W., Smiley R.M., Kim R.B., Wood A.J., Stein C.M.
Clin. Pharmacol. Ther. 75:539-545(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-347.
[20]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-40.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D25235 mRNA. Translation: BAA04960.1.
U03866 Genomic DNA. Translation: AAB60353.1.
U02569 mRNA. Translation: AAA93114.1.
D32201 mRNA. Translation: BAA06900.1.
D32202 mRNA. Translation: BAA06901.1. Frameshift.
L31774 mRNA. Translation: AAB59486.1.
AF013261 mRNA. Translation: AAC06138.1.
AY491775 mRNA. Translation: AAR84644.1.
AY491776 mRNA. Translation: AAR84645.1.
AY491777 mRNA. Translation: AAR84646.1.
AY491778 mRNA. Translation: AAR84647.1.
AY491779 mRNA. Translation: AAR84648.1.
AY491780 mRNA. Translation: AAR84649.1.
AY491781 mRNA. Translation: AAR84650.1.
AF395806 mRNA. Translation: AAK77197.1.
AB065703 Genomic DNA. Translation: BAC05926.1.
AY389505 Genomic DNA. Translation: AAQ91331.1.
AK289548 mRNA. Translation: BAF82237.1.
EU326301 Genomic DNA. Translation: ACA05899.1.
EU326301 Genomic DNA. Translation: ACA05900.1. Sequence problems.
EU326301 Genomic DNA. Translation: ACA05902.1.
EU326301 Genomic DNA. Translation: ACA05903.1.
EU326301 Genomic DNA. Translation: ACA05904.1.
EU326301 Genomic DNA. Translation: ACA05905.1.
EU326301 Genomic DNA. Translation: ACA05906.1.
EU326301 Genomic DNA. Translation: ACA05907.1.
BC095512 mRNA. Translation: AAH95512.1.
PIRJN0765.
S65656.
S65657.
RefSeqNP_000671.2. NM_000680.2.
NP_150645.2. NM_033302.2.
NP_150646.3. NM_033303.3.
NP_150647.2. NM_033304.2.
XP_005273471.1. XM_005273414.1.
XP_005273472.1. XM_005273415.1.
UniGeneHs.709175.

3D structure databases

ProteinModelPortalP35348.
SMRP35348. Positions 29-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-33401N.
IntActP35348. 3 interactions.

Chemistry

BindingDBP35348.
ChEMBLCHEMBL2096676.
DrugBankDB00346. Alfuzosin.
DB01118. Amiodarone.
DB00182. Amphetamine.
DB00865. Benzphetamine.
DB00217. Bethanidine.
DB01136. Carvedilol.
DB00298. Dapiprazole.
DB04840. Debrisoquin.
DB01576. Dextroamphetamine.
DB00590. Doxazosin.
DB00751. Epinastine.
DB00668. Epinephrine.
DB00696. Ergotamine.
DB00875. Flupenthixol.
DB00226. Guanadrel Sulfate.
DB01170. Guanethidine.
DB00598. Labetalol.
DB01255. Lisdexamfetamine.
DB00934. Maprotiline.
DB01365. Mephentermine.
DB00610. Metaraminol.
DB01577. Methamphetamine.
DB01403. Methotrimeprazine.
DB00723. Methoxamine.
DB00211. Midodrine.
DB01149. Nefazodone.
DB00699. Nicergoline.
DB00665. Nilutamide.
DB00368. Norepinephrine.
DB00506. Norgestrel.
DB00935. Oxymetazoline.
DB00850. Perphenazine.
DB01579. Phendimetrazine.
DB00925. Phenoxybenzamine.
DB00388. Phenylephrine.
DB00397. Phenylpropanolamine.
DB00457. Prazosin.
DB00420. Promazine.
DB01069. Promethazine.
DB01608. Propericiazine.
DB00777. Propiomazine.
DB00852. Pseudoephedrine.
DB00734. Risperidone.
DB06144. Sertindole.
DB00706. Tamsulosin.
DB01162. Terazosin.
DB00679. Thioridazine.
DB00797. Tolazoline.
DB00656. Trazodone.
DB00831. Trifluoperazine.
DB00246. Ziprasidone.
GuidetoPHARMACOLOGY22.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP35348.

Polymorphism databases

DMDM1168246.

Proteomic databases

PaxDbP35348.
PRIDEP35348.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276393; ENSP00000276393; ENSG00000120907. [P35348-1]
ENST00000354550; ENSP00000346557; ENSG00000120907. [P35348-4]
ENST00000358857; ENSP00000351725; ENSG00000120907. [P35348-7]
ENST00000380572; ENSP00000369946; ENSG00000120907. [P35348-6]
ENST00000380573; ENSP00000369947; ENSG00000120907. [P35348-1]
ENST00000380581; ENSP00000369955; ENSG00000120907. [P35348-9]
ENST00000380582; ENSP00000369956; ENSG00000120907. [P35348-3]
ENST00000380586; ENSP00000369960; ENSG00000120907. [P35348-2]
ENST00000380587; ENSP00000369961; ENSG00000120907. [P35348-8]
ENST00000519096; ENSP00000431073; ENSG00000120907. [P35348-7]
ENST00000521711; ENSP00000430414; ENSG00000120907. [P35348-7]
GeneID148.
KEGGhsa:148.
UCSCuc003xfe.1. human. [P35348-3]
uc003xfg.1. human. [P35348-4]
uc003xfh.1. human. [P35348-1]
uc010lul.1. human. [P35348-8]
uc010lum.1. human. [P35348-9]
uc022atd.1. human. [P35348-5]

Organism-specific databases

CTD148.
GeneCardsGC08M026605.
HGNCHGNC:277. ADRA1A.
HPAHPA029678.
MIM104221. gene.
neXtProtNX_P35348.
PharmGKBPA34.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253615.
HOVERGENHBG106962.
KOK04135.
OMACTTARVR.
OrthoDBEOG7H4DTB.
TreeFamTF331895.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP35348.

Gene expression databases

ArrayExpressP35348.
BgeeP35348.
CleanExHS_ADRA1A.
GenevestigatorP35348.

Family and domain databases

InterProIPR002233. ADR_fam.
IPR001004. ADRA1A_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24248. PTHR24248. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01103. ADRENERGICR.
PR00557. ADRENRGCA1AR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAlpha-1A_adrenergic_receptor.
GenomeRNAi148.
NextBio585.
PROP35348.
SOURCESearch...

Entry information

Entry nameADA1A_HUMAN
AccessionPrimary (citable) accession number: P35348
Secondary accession number(s): A8K0I3 expand/collapse secondary AC list , B0ZBD1, B0ZBD2, B0ZBD4, B0ZBD5, B0ZBD6, B0ZBD8, B0ZBD9, O60451, Q13675, Q13729, Q4VBM7, Q6RUJ4, Q6RUJ5, Q6RUJ7, Q6RUJ8, Q6RUJ9, Q96RE8, Q9UD63, Q9UD67
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries