ID ADA1A_HUMAN Reviewed; 466 AA. AC P35348; A8K0I3; B0ZBD1; B0ZBD2; B0ZBD4; B0ZBD5; B0ZBD6; B0ZBD8; B0ZBD9; AC O60451; Q13675; Q13729; Q4VBM7; Q6RUJ4; Q6RUJ5; Q6RUJ7; Q6RUJ8; Q6RUJ9; AC Q96RE8; Q9UD63; Q9UD67; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 04-NOV-2026, entry version 231. DE RecName: Full=Alpha-1A adrenergic receptor {ECO:0000303|PubMed:37563160}; DE AltName: Full=Alpha-1A adrenoreceptor; DE Short=Alpha-1A adrenoceptor {ECO:0000250|UniProtKB:Q9WU25}; DE AltName: Full=Alpha-1C adrenergic receptor {ECO:0000303|PubMed:8396931}; DE AltName: Full=Alpha-adrenergic receptor 1c; GN Name=ADRA1A {ECO:0000312|HGNC:HGNC:277}; Synonyms=ADRA1C; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT ARG-347. RC TISSUE=Prostate; RX PubMed=8396931; DOI=10.1006/bbrc.1993.2130; RA Hirasawa A., Horie K., Tanaka T., Takagaki K., Murai M., Yano J., RA Tsujimoto G.; RT "Cloning, functional expression and tissue distribution of human cDNA for RT the alpha 1C-adrenergic receptor."; RL Biochem. Biophys. Res. Commun. 195:902-909(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-347, AND FUNCTION. RC TISSUE=Heart; RX PubMed=8024574; DOI=10.1006/bbrc.1994.1845; RA Weinberg D.H., Trivedi P., Tan C.P., Mitra S., Perkins-Barrow A., RA Borkowski D., Strader C.D., Bayne M.; RT "Cloning, expression and characterization of human alpha adrenergic RT receptors alpha 1a, alpha 1b and alpha 1c."; RL Biochem. Biophys. Res. Commun. 201:1296-1304(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND FUNCTION. RC TISSUE=Hippocampus, and Lymphocyte; RX PubMed=8183249; DOI=10.1016/s0026-895x(25)10156-9; RA Forray C., Bard J.A., Wetzel J.M., Chiu G., Shapiro E., Tang R., Lepor H., RA Hartig P.R., Weinshank R.L., Branchek T.A., Gluchowski C.; RT "The alpha 1-adrenergic receptor that mediates smooth muscle contraction in RT human prostate has the pharmacological properties of the cloned human alpha RT 1c subtype."; RL Mol. Pharmacol. 45:703-708(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-347. RX PubMed=8564208; DOI=10.1111/j.1476-5381.1995.tb16640.x; RA Tseng-Crank J., Kost T., Goetz A., Hazum S., Roberson K.M., Haizlip J., RA Godinot N., Robertson C.N., Saussy D.; RT "The alpha 1C-adrenoceptor in human prostate: cloning, functional RT expression, and localization to specific prostatic cell types."; RL Br. J. Pharmacol. 115:1475-1485(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANT ARG-347, AND TISSUE RP SPECIFICITY. RC TISSUE=Prostate; RX PubMed=7737411; DOI=10.1016/0014-5793(95)00330-c; RA Hirasawa A., Shibata K., Horie K., Takei Y., Obika K., Tanaka T., RA Muramoto N., Takagaki K., Yano J., Tsujimoto G.; RT "Cloning, functional expression and tissue distribution of human alpha 1c- RT adrenoceptor splice variants."; RL FEBS Lett. 363:256-260(1995). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-347, AND FUNCTION. RX PubMed=7815325; DOI=10.1016/s0022-3565(25)24297-5; RA Schwinn D.A., Johnston G.I., Page S.O., Mosley M.J., Wilson K.H., RA Worman N.P., Campbell S., Fidock M.D., Furness L.M., Parry-Smith D.J., RA Peter B., Bailey D.S.; RT "Cloning and pharmacological characterization of human alpha-1 adrenergic RT receptors: sequence corrections and direct comparison with other species RT homologues."; RL J. Pharmacol. Exp. Ther. 272:134-142(1995). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY. RC TISSUE=Prostate; RX PubMed=9490024; DOI=10.1016/s0014-5793(98)00024-6; RA Chang D.J., Chang T.K., Yamanishi S.S., Salazar F.H.R., Kosaka A.H., RA Khare R., Bhakta S., Jasper J.R., Shieh I.-S., Lesnick J.D., Ford A.P.D.W., RA Daniels D.V., Clarke D.E., Bach C.T., Chan H.W.; RT "Molecular cloning, genomic characterization and expression of novel human RT alpha1A-adrenoceptor isoforms."; RL FEBS Lett. 422:279-283(1998). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7; 8 AND 9). RC TISSUE=Liver; RX PubMed=10493934; DOI=10.1042/bj3430231; RA Coge F., Guenin S.P., Renouard-Try A., Rique H., Ouvry C., Fabry N., RA Beauverger P., Nicolas J.P., Galizzi J.-P., Boutin J.A., Canet E.; RT "Truncated isoforms inhibit [3H]prazosin binding and cellular trafficking RT of native human alpha1A-adrenoceptors."; RL Biochem. J. 343:231-239(1999). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Banerjee A.G.N., Aarti A.; RT "RT-PCR cloning and sequence analysis of adrenergic receptor subtype-alpha- RT 1a cDNA from human prostrate cell-line DU-145."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.; RT "Genome-wide discovery and analysis of human seven transmembrane helix RT receptor genes."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kopatz S.A., Aronstam R.S., Sharma S.V.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-347. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-400 (ISOFORMS 1/2/3/4), TISSUE RP SPECIFICITY, AND VARIANT ARG-347. RC TISSUE=Prostate; RX PubMed=8196478; DOI=10.1016/0024-3205(94)90031-0; RA Faure C., Pimoule C., Vallancien G., Langer S.Z., Graham D.; RT "Identification of alpha 1-adrenoceptor subtypes present in the human RT prostate."; RL Life Sci. 54:1595-1605(1994). RN [16] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=18802028; DOI=10.1161/circresaha.108.176024; RA Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S., RA O'Connell T.D.; RT "Nuclear alpha1-adrenergic receptors signal activated ERK localization to RT caveolae in adult cardiac myocytes."; RL Circ. Res. 103:992-1000(2008). RN [17] RP SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, AND MUTAGENESIS OF LYS-334; RP LYS-335; ARG-342; ARG-348 AND LYS-349. RX PubMed=22120526; DOI=10.1016/j.cellsig.2011.11.014; RA Wright C.D., Wu S.C., Dahl E.F., Sazama A.J., O'Connell T.D.; RT "Nuclear localization drives alpha1-adrenergic receptor oligomerization and RT signaling in cardiac myocytes."; RL Cell. Signal. 24:794-802(2012). RN [18] RP INTERACTION WITH CAVIN4, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24567387; DOI=10.1073/pnas.1315359111; RA Ogata T., Naito D., Nakanishi N., Hayashi Y.K., Taniguchi T., Miyagawa K., RA Hamaoka T., Maruyama N., Matoba S., Ikeda K., Yamada H., Oh H., Ueyama T.; RT "MURC/Cavin-4 facilitates recruitment of ERK to caveolae and concentric RT cardiac hypertrophy induced by alpha1-adrenergic receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 111:3811-3816(2014). RN [19] {ECO:0007744|PDB:8THK, ECO:0007744|PDB:8THL} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH G PROTEIN AND ADRENALINE, RP DISULFIDE BONDS, AND FUNCTION. RX PubMed=37563160; DOI=10.1038/s41467-023-40524-2; RA Su M., Wang J., Xiang G., Do H.N., Levitz J., Miao Y., Huang X.Y.; RT "Structural basis of agonist specificity of alpha1A-adrenergic receptor."; RL Nat. Commun. 14:4819-4819(2023). RN [20] RP VARIANT ARG-347, AND FUNCTION. RX PubMed=8832064; DOI=10.1111/j.1476-5381.1996.tb15552.x; RA Shibata K., Hirasawa A., Moriyama N., Kawabe K., Ogawa S., Tsujimoto G.; RT "Alpha 1a-adrenoceptor polymorphism: pharmacological characterization and RT association with benign prostatic hypertrophy."; RL Br. J. Pharmacol. 118:1403-1408(1996). RN [21] RP VARIANT ARG-347. RX PubMed=15179408; DOI=10.1016/j.clpt.2004.02.006; RA Sofowora G.G., Dishy V., Landau R., Xie H.G., Prasad H.C., Byrne D.W., RA Smiley R.M., Kim R.B., Wood A.J., Stein C.M.; RT "Alpha 1A-adrenergic receptor polymorphism and vascular response."; RL Clin. Pharmacol. Ther. 75:539-545(2004). RN [22] RP VARIANT [LARGE SCALE ANALYSIS] TRP-40. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Alpha-1 adrenergic receptors are G protein-coupled receptors CC for catecholamines that signal through the G(q) family of G proteins, CC including G(q) and G(11). Upon activation, they stimulate the CC phosphatidylinositol-calcium second messenger pathway, leading to CC calcium release from intracellular stores and activation of protein CC kinase C (PubMed:37563160). ADRA1A binds the catecholamine ligands CC norepinephrine and epinephrine (PubMed:18802028, PubMed:37563160, CC PubMed:7815325, PubMed:8024574, PubMed:8183249, PubMed:8832064). Can CC also couple to G(14) protein (By similarity). Nuclear ADRA1A forms CC heterooligomers with ADRA1B to regulate phenylephrine(PE)-stimulated CC ERK signaling in cardiac myocytes (PubMed:18802028, PubMed:22120526). CC At the plasma membrane, ADRA1A interacts with CAVIN4/MURC to regulates CC ERK activation in cardiomyocytes, contributing to the regulation of CC cardiac hypertrophy (PubMed:24567387). Additionally, functions as a CC vasopressor in resistance arteries and plays a role in maintaining CC normal arterial blood pressure (By similarity). CC {ECO:0000250|UniProtKB:P18130, ECO:0000250|UniProtKB:P97718, CC ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526, CC ECO:0000269|PubMed:24567387, ECO:0000269|PubMed:37563160, CC ECO:0000269|PubMed:7815325, ECO:0000269|PubMed:8024574, CC ECO:0000269|PubMed:8183249, ECO:0000269|PubMed:8832064}. CC -!- SUBUNIT: Homo- and heterooligomer. Heterooligomerizes with ADRA1B CC homooligomers in cardiac myocytes (PubMed:22120526). Interacts with CC CAVIN4 (PubMed:24567387). {ECO:0000269|PubMed:22120526, CC ECO:0000269|PubMed:24567387}. CC -!- INTERACTION: CC P35348-1; Q96HD1: CRELD1; NbExp=3; IntAct=EBI-21288891, EBI-713009; CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:18802028, CC ECO:0000269|PubMed:22120526}; Multi-pass membrane protein. Cell CC membrane {ECO:0000269|PubMed:24567387}; Multi-pass membrane protein CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:24567387}. Membrane, CC caveola {ECO:0000269|PubMed:24567387}. Note=Location at the nuclear CC membrane facilitates heterooligomerization and regulates ERK-mediated CC signaling in cardiac myocytes (PubMed:18802028, PubMed:22120526). CC Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of CC cardiac myocytes (PubMed:18802028, PubMed:22120526). Colocalizes with CC CAVIN4 and CAV3 at the plasma membrane and partly within the cytoplasm CC in cardiomyocytes (PubMed:24567387). {ECO:0000269|PubMed:18802028, CC ECO:0000269|PubMed:22120526, ECO:0000269|PubMed:24567387}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; Synonyms=Alpha 1c-1, Alpha(1A-1); CC IsoId=P35348-1; Sequence=Displayed; CC Name=2; Synonyms=Alpha 1c-2, Alpha(1A-2); CC IsoId=P35348-2; Sequence=VSP_011055; CC Name=3; Synonyms=Alpha 1c-3, Alpha(1A-3); CC IsoId=P35348-3; Sequence=VSP_011044, VSP_011045; CC Name=4; Synonyms=Alpha(1A-4); CC IsoId=P35348-4; Sequence=VSP_011050; CC Name=5; CC IsoId=P35348-5; Sequence=VSP_011051, VSP_011052; CC Name=6; CC IsoId=P35348-6; Sequence=VSP_011053, VSP_011054; CC Name=7; Synonyms=2b/3b; CC IsoId=P35348-7; Sequence=VSP_011047, VSP_011048; CC Name=8; Synonyms=2c; CC IsoId=P35348-8; Sequence=VSP_011046; CC Name=9; Synonyms=3c; CC IsoId=P35348-9; Sequence=VSP_011049; CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver and prostate, but CC not in kidney, lung, adrenal, aorta and pituitary. Within the prostate, CC expressed in the apex, base, periurethral and lateral lobe. Isoform 4 CC is the most abundant isoform expressed in the prostate with high levels CC also detected in liver and heart. {ECO:0000269|PubMed:7737411, CC ECO:0000269|PubMed:8196478, ECO:0000269|PubMed:9490024}. CC -!- PTM: C-terminal Ser or Thr residues may be phosphorylated. CC {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 7]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. CC Adrenergic receptor subfamily. ADRA1A sub-subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- SEQUENCE CAUTION: [Isoform 2]: CC Sequence=ACA05900.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAA06901.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D25235; BAA04960.1; -; mRNA. DR EMBL; U03866; AAB60353.1; -; Genomic_DNA. DR EMBL; U02569; AAA93114.1; -; mRNA. DR EMBL; D32201; BAA06900.1; -; mRNA. DR EMBL; D32202; BAA06901.1; ALT_FRAME; mRNA. DR EMBL; L31774; AAB59486.1; -; mRNA. DR EMBL; AF013261; AAC06138.1; -; mRNA. DR EMBL; AY491775; AAR84644.1; -; mRNA. DR EMBL; AY491776; AAR84645.1; -; mRNA. DR EMBL; AY491777; AAR84646.1; -; mRNA. DR EMBL; AY491778; AAR84647.1; -; mRNA. DR EMBL; AY491779; AAR84648.1; -; mRNA. DR EMBL; AY491780; AAR84649.1; -; mRNA. DR EMBL; AY491781; AAR84650.1; -; mRNA. DR EMBL; AF395806; AAK77197.1; -; mRNA. DR EMBL; AB065703; BAC05926.1; -; Genomic_DNA. DR EMBL; AY389505; AAQ91331.1; -; Genomic_DNA. DR EMBL; AK289548; BAF82237.1; -; mRNA. DR EMBL; EU326301; ACA05899.1; -; Genomic_DNA. DR EMBL; EU326301; ACA05900.1; ALT_SEQ; Genomic_DNA. DR EMBL; EU326301; ACA05902.1; -; Genomic_DNA. DR EMBL; EU326301; ACA05903.1; -; Genomic_DNA. DR EMBL; EU326301; ACA05904.1; -; Genomic_DNA. DR EMBL; EU326301; ACA05905.1; -; Genomic_DNA. DR EMBL; EU326301; ACA05906.1; -; Genomic_DNA. DR EMBL; EU326301; ACA05907.1; -; Genomic_DNA. DR EMBL; BC095512; AAH95512.1; -; mRNA. DR CCDS; CCDS34869.1; -. [P35348-2] DR CCDS; CCDS6052.1; -. [P35348-3] DR CCDS; CCDS6053.1; -. [P35348-4] DR CCDS; CCDS6054.1; -. [P35348-1] DR CCDS; CCDS83269.1; -. [P35348-6] DR PIR; JN0765; JN0765. DR PIR; S65656; S65656. DR PIR; S65657; S65657. DR RefSeq; NP_000671.2; NM_000680.4. [P35348-1] DR RefSeq; NP_001309431.1; NM_001322502.1. [P35348-9] DR RefSeq; NP_001309432.1; NM_001322503.1. [P35348-8] DR RefSeq; NP_001309433.1; NM_001322504.1. [P35348-6] DR RefSeq; NP_150645.2; NM_033302.3. [P35348-3] DR RefSeq; NP_150646.3; NM_033303.4. [P35348-2] DR RefSeq; NP_150647.2; NM_033304.3. [P35348-4] DR RefSeq; XP_006716356.1; XM_006716293.5. [P35348-3] DR RefSeq; XP_016868583.1; XM_017013094.2. [P35348-2] DR RefSeq; XP_016868584.1; XM_017013095.2. [P35348-2] DR PDB; 7YM8; EM; 2.92 A; A=1-227, A=262-371. DR PDB; 7YMH; EM; 3.52 A; A=1-227, A=262-371. DR PDB; 7YMJ; EM; 3.35 A; A=1-234, A=276-371. DR PDB; 8HN1; EM; 2.90 A; A=1-371. DR PDB; 8THK; EM; 2.60 A; R=15-350. DR PDB; 8THL; EM; 3.10 A; R=15-350. DR PDB; 9IQV; EM; 3.30 A; B=5-341. DR PDB; 9M4Q; EM; 2.99 A; A=19-341. DR PDB; 9M4T; EM; 3.19 A; A=19-341. DR AlphaFoldDB; P35348; -. DR EMDB; EMD-33924; -. DR EMDB; EMD-33928; -. DR EMDB; EMD-33930; -. DR EMDB; EMD-34906; -. DR EMDB; EMD-41267; -. DR EMDB; EMD-41268; -. DR EMDB; EMD-60796; -. DR EMDB; EMD-63628; -. DR EMDB; EMD-63629; -. DR SMR; P35348; -. DR BioGRID; 106658; 28. DR CORUM; P35348; -. DR DIP; DIP-33401N; -. DR FunCoup; P35348; 2841. DR IntAct; P35348; 33. DR NDEx; IQUERY-CP-ADRA1A; 8 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000369960; -. DR BindingDB; P35348; -. DR ChEMBL; CHEMBL229; -. DR DrugBank; DB01472; 4-Methoxyamphetamine. DR DrugBank; DB20666; Abanoquil. DR DrugBank; DB01614; Acepromazine. DR DrugBank; DB00346; Alfuzosin. DR DrugBank; DB00321; Amitriptyline. DR DrugBank; DB00543; Amoxapine. DR DrugBank; DB00182; Amphetamine. DR DrugBank; DB00964; Apraclonidine. DR DrugBank; DB09229; Aranidipine. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB14185; Aripiprazole lauroxil. DR DrugBank; DB09204; Arotinolol. DR DrugBank; DB06216; Asenapine. DR DrugBank; DB00865; Benzphetamine. DR DrugBank; DB20389; Besipirdine. DR DrugBank; DB01295; Bevantolol. DR DrugBank; DB09128; Brexpiprazole. DR DrugBank; DB01200; Bromocriptine. DR DrugBank; DB00490; Buspirone. DR DrugBank; DB00248; Cabergoline. DR DrugBank; DB06016; Cariprazine. DR DrugBank; DB01136; Carvedilol. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB09202; Cirazoline. DR DrugBank; DB00575; Clonidine. DR DrugBank; DB15971; Clorotepine. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB00298; Dapiprazole. DR DrugBank; DB01151; Desipramine. DR DrugBank; DB01576; Dextroamphetamine. DR DrugBank; DB11273; Dihydroergocornine. DR DrugBank; DB13345; Dihydroergocristine. DR DrugBank; DB00320; Dihydroergotamine. DR DrugBank; DB00449; Dipivefrin. DR DrugBank; DB11278; DL-Methylephedrine. DR DrugBank; DB00841; Dobutamine. DR DrugBank; DB09167; Dosulepin. DR DrugBank; DB00590; Doxazosin. DR DrugBank; DB01142; Doxepin. DR DrugBank; DB04855; Dronedarone. DR DrugBank; DB00450; Droperidol. DR DrugBank; DB06262; Droxidopa. DR DrugBank; DB01364; Ephedrine. DR DrugBank; DB05492; Epicept NP-1. DR DrugBank; DB00751; Epinastine. DR DrugBank; DB00668; Epinephrine. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB01253; Ergometrine. DR DrugBank; DB00696; Ergotamine. DR DrugBank; DB01175; Escitalopram. DR DrugBank; DB09194; Etoperidone. DR DrugBank; DB00800; Fenoldopam. DR DrugBank; DB13665; Fluanisone. DR DrugBank; DB00875; Flupentixol. DR DrugBank; DB00502; Haloperidol. DR DrugBank; DB04946; Iloperidone. DR DrugBank; DB00458; Imipramine. DR DrugBank; DB11577; Indigotindisulfonic acid. DR DrugBank; DB08950; Indoramin. DR DrugBank; DB06706; Isometheptene. DR DrugBank; DB00598; Labetalol. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB06707; Levonordefrin. DR DrugBank; DB04948; Lofexidine. DR DrugBank; DB09195; Lorpiprazole. DR DrugBank; DB00408; Loxapine. DR DrugBank; DB00934; Maprotiline. DR DrugBank; DB20960; Mazapertine. DR DrugBank; DB11428; Medetomidine. DR DrugBank; DB01365; Mephentermine. DR DrugBank; DB00610; Metaraminol. DR DrugBank; DB01403; Methotrimeprazine. DR DrugBank; DB00723; Methoxamine. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB00211; Midodrine. DR DrugBank; DB24348; Milsaperidone. DR DrugBank; DB00370; Mirtazapine. DR DrugBank; DB09205; Moxisylyte. DR DrugBank; DB12092; Naftopidil. DR DrugBank; DB06711; Naphazoline. DR DrugBank; DB01149; Nefazodone. DR DrugBank; DB00622; Nicardipine. DR DrugBank; DB00699; Nicergoline. DR DrugBank; DB09239; Niguldipine. DR DrugBank; DB00368; Norepinephrine. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB06229; Ocaperidone. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB00935; Oxymetazoline. DR DrugBank; DB01267; Paliperidone. DR DrugBank; DB00715; Paroxetine. DR DrugBank; DB01186; Pergolide. DR DrugBank; DB08922; Perospirone. DR DrugBank; DB01579; Phendimetrazine. DR DrugBank; DB00925; Phenoxybenzamine. DR DrugBank; DB00692; Phentolamine. DR DrugBank; DB00388; Phenylephrine. DR DrugBank; DB09286; Pipamperone. DR DrugBank; DB06153; Pizotifen. DR DrugBank; DB00457; Prazosin. DR DrugBank; DB00433; Prochlorperazine. DR DrugBank; DB00420; Promazine. DR DrugBank; DB01069; Promethazine. DR DrugBank; DB00777; Propiomazine. DR DrugBank; DB12278; Propiverine. DR DrugBank; DB00852; Pseudoephedrine. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB00908; Quinidine. DR DrugBank; DB05469; R450. DR DrugBank; DB11124; Racepinephrine. DR DrugBank; DB00243; Ranolazine. DR DrugBank; DB00734; Risperidone. DR DrugBank; DB00268; Ropinirole. DR DrugBank; DB06144; Sertindole. DR DrugBank; DB06207; Silodosin. DR DrugBank; DB06555; Siramesine. DR DrugBank; DB17056; Spiperone. DR DrugBank; DB19724; Sunepitron. DR DrugBank; DB09203; Synephrine. DR DrugBank; DB00706; Tamsulosin. DR DrugBank; DB20641; Taprizosin. DR DrugBank; DB01162; Terazosin. DR DrugBank; DB06764; Tetryzoline. DR DrugBank; DB01622; Thioproperazine. DR DrugBank; DB00679; Thioridazine. DR DrugBank; DB13025; Tiapride. DR DrugBank; DB00697; Tizanidine. DR DrugBank; DB00797; Tolazoline. DR DrugBank; DB00656; Trazodone. DR DrugBank; DB00831; Trifluoperazine. DR DrugBank; DB00726; Trimipramine. DR DrugBank; DB21230; Upidosin. DR DrugBank; DB00661; Verapamil. DR DrugBank; DB06694; Xylometazoline. DR DrugBank; DB00246; Ziprasidone. DR DrugBank; DB01624; Zuclopenthixol. DR DrugCentral; P35348; -. DR GuidetoPHARMACOLOGY; 22; -. DR GlyCosmos; P35348; 4 sites, 1 glycan. DR GlyGen; P35348; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; P35348; -. DR PhosphoSitePlus; P35348; -. DR BioMuta; ADRA1A; -. DR DMDM; 1168246; -. DR jPOST; P35348; -. DR MassIVE; P35348; -. DR PaxDb; 9606-ENSP00000369960; -. DR PeptideAtlas; P35348; -. DR ProteomicsDB; 55030; -. [P35348-5] DR ProteomicsDB; 55033; -. [P35348-8] DR Antibodypedia; 10062; 434 antibodies from 42 providers. DR DNASU; 148; -. DR Ensembl; ENST00000276393.8; ENSP00000276393.4; ENSG00000120907.18. [P35348-1] DR Ensembl; ENST00000354550.4; ENSP00000346557.4; ENSG00000120907.18. [P35348-4] DR Ensembl; ENST00000380572.3; ENSP00000369946.3; ENSG00000120907.18. [P35348-6] DR Ensembl; ENST00000380573.4; ENSP00000369947.3; ENSG00000120907.18. [P35348-1] DR Ensembl; ENST00000380582.7; ENSP00000369956.3; ENSG00000120907.18. [P35348-3] DR Ensembl; ENST00000380586.5; ENSP00000369960.1; ENSG00000120907.18. [P35348-2] DR Ensembl; ENST00000519096.5; ENSP00000431073.1; ENSG00000120907.18. [P35348-7] DR Ensembl; ENST00000521711.5; ENSP00000430414.1; ENSG00000120907.18. [P35348-7] DR GeneID; 148; -. DR KEGG; hsa:148; -. DR MANE-Select; ENST00000380573.4; ENSP00000369947.3; NM_000680.4; NP_000671.2. DR UCSC; uc003xfc.1; human. [P35348-1] DR AGR; HGNC:277; -. DR ClinPGx; PA34; -. DR CTD; 148; -. DR DisGeNET; 148; -. DR GeneCards; ADRA1A; -. DR HGNC; HGNC:277; ADRA1A. DR HPA; ENSG00000120907; Tissue enhanced (adipose tissue, liver). DR MIM; 104221; gene. DR OpenTargets; ENSG00000120907; -. DR VEuPathDB; HostDB:ENSG00000120907; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00940000159105; -. DR HOGENOM; CLU_009579_11_6_1; -. DR InParanoid; P35348; -. DR OMA; ACCCIVS; -. DR OrthoDB; 6358729at2759; -. DR PAN-GO; P35348; 7 GO annotations based on evolutionary models. DR PhylomeDB; P35348; -. DR PathwayCommons; P35348; -. DR Reactome; R-HSA-390696; Adrenoceptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-416482; G alpha (12/13) signalling events. DR SignaLink; P35348; -. DR SIGNOR; P35348; -. DR Agora; ENSG00000120907; -. DR BioGRID-ORCS; 148; 7 hits in 1158 CRISPR screens. DR GeneWiki; Alpha-1A_adrenergic_receptor; -. DR GenomeRNAi; 148; -. DR Pharos; P35348; Tclin. DR PRO; PR:P35348; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P35348; protein. DR Bgee; ENSG00000120907; Expressed in right lobe of liver and 109 other cell types or tissues. DR ExpressionAtlas; P35348; baseline and differential. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; IMP:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central. DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0150099; P:neuron-glial cell signaling; ISS:ARUK-UCL. DR GO; GO:0001994; P:norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure; ISS:UniProtKB. DR GO; GO:0071882; P:phospholipase C-activating adrenergic receptor signaling pathway; ISS:BHF-UCL. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:UniProt. DR GO; GO:0097195; P:pilomotor reflex; IEA:Ensembl. DR GO; GO:0045760; P:positive regulation of action potential; ISS:BHF-UCL. DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISS:BHF-UCL. DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IDA:UniProtKB. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB. DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl. DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISS:BHF-UCL. DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISS:BHF-UCL. DR GO; GO:0009725; P:response to hormone; ISS:BHF-UCL. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:BHF-UCL. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0006939; P:smooth muscle contraction; TAS:ProtInc. DR CDD; cd15325; 7tmA_alpha1A_AR; 1. DR FunFam; 1.20.1070.10:FF:000027; alpha-1A adrenergic receptor; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR002233; ADR_fam. DR InterPro; IPR001004; ADRA1A_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR24248:SF16; ALPHA-1A ADRENERGIC RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00557; ADRENRGCA1AR. DR PRINTS; PR00237; GPCRRHODOPSN. DR SMART; SM01381; 7TM_GPCR_Srsx; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; KW Disulfide bond; G protein-coupled receptor; Glycoprotein; Lipoprotein; KW Membrane; Nucleus; Palmitate; Phosphoprotein; Proteomics identification; KW Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..466 FT /note="Alpha-1A adrenergic receptor" FT /id="PRO_0000069063" FT TOPO_DOM 1..27 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 28..51 FT /note="Helical; Name=1" FT /evidence="ECO:0000250" FT TOPO_DOM 52..64 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 65..88 FT /note="Helical; Name=2" FT /evidence="ECO:0000250" FT TOPO_DOM 89..99 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 100..122 FT /note="Helical; Name=3" FT /evidence="ECO:0000250" FT TOPO_DOM 123..143 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 144..167 FT /note="Helical; Name=4" FT /evidence="ECO:0000250" FT TOPO_DOM 168..181 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 182..205 FT /note="Helical; Name=5" FT /evidence="ECO:0000250" FT TOPO_DOM 206..273 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 274..297 FT /note="Helical; Name=6" FT /evidence="ECO:0000250" FT TOPO_DOM 298..305 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 306..329 FT /note="Helical; Name=7" FT /evidence="ECO:0000250" FT TOPO_DOM 330..466 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT MOTIF 334..349 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:22120526" FT BINDING 106 FT /ligand="(R)-adrenaline" FT /ligand_id="ChEBI:CHEBI:71406" FT /evidence="ECO:0000269|PubMed:37563160, FT ECO:0007744|PDB:8THL" FT BINDING 188 FT /ligand="(R)-adrenaline" FT /ligand_id="ChEBI:CHEBI:71406" FT /evidence="ECO:0000269|PubMed:37563160, FT ECO:0007744|PDB:8THL" FT MOD_RES 215 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000255" FT LIPID 345 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000255" FT CARBOHYD 7 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 13 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 22 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 99..176 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521, FT ECO:0000269|PubMed:37563160, ECO:0007744|PDB:8THK, FT ECO:0007744|PDB:8THL" FT VAR_SEQ 295..466 FT /note="GSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCL FT CRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPR FT GSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGE FT EV -> DEVSLCHQAGVQWHDLGSLQPPPPGFKRFSCLSLPSSWDYRDVPPGRRHQAQL FT IFVFLVETGFHHVGQDDLDLLTS (in isoform 8)" FT /evidence="ECO:0000303|PubMed:10493934" FT /id="VSP_011046" FT VAR_SEQ 295..342 FT /note="GSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLR -> FT DEETEAQEGKNDSPSFKQPVHHAAVLGLEVMEKENLEGVSRKDTCGVW (in FT isoform 6)" FT /evidence="ECO:0000303|PubMed:10493934" FT /id="VSP_011053" FT VAR_SEQ 296..466 FT /note="SFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLC FT RKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRG FT SARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEE FT V -> THTHDMKPASRPRLLSLLPKEGEHETHHWSCDPLSLESTPGAQEPCLTLGFTSL FT SSIHLTKAQIQHVTVTDTGKTVT (in isoform 9)" FT /evidence="ECO:0000303|PubMed:10493934" FT /id="VSP_011049" FT VAR_SEQ 296..324 FT /note="SFFPDFKPSETVFKIVFWLGYLNSCINPI -> TYILKYDVLFWRKGLSVCT FT RLRERKEIKN (in isoform 7)" FT /evidence="ECO:0000303|PubMed:10493934" FT /id="VSP_011047" FT VAR_SEQ 296..297 FT /note="SF -> KS (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10493934" FT /id="VSP_011051" FT VAR_SEQ 298..466 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10493934" FT /id="VSP_011052" FT VAR_SEQ 325..466 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:10493934" FT /id="VSP_011048" FT VAR_SEQ 343..466 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:10493934" FT /id="VSP_011054" FT VAR_SEQ 424..466 FT /note="VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV -> TKSRS FT VTRLECSGMILAHCNLRLPGSRDSPASASQAAGTTGMCHQADATRPS (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:7737411" FT /id="VSP_011055" FT VAR_SEQ 424..466 FT /note="VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV -> RGMDC FT RYFTKNCREHIKHVNFMMPPWRKGSEC (in isoform 4)" FT /evidence="ECO:0000303|PubMed:9490024" FT /id="VSP_011050" FT VAR_SEQ 424..429 FT /note="VRSKSF -> GHTPMT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:7737411" FT /id="VSP_011044" FT VAR_SEQ 430..466 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:7737411" FT /id="VSP_011045" FT VARIANT 40 FT /note="G -> W (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035756" FT VARIANT 200 FT /note="I -> S (in dbSNP:rs2229125)" FT /id="VAR_049370" FT VARIANT 347 FT /note="C -> R (in dbSNP:rs1048101)" FT /evidence="ECO:0000269|PubMed:15179408, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7737411, FT ECO:0000269|PubMed:7815325, ECO:0000269|PubMed:8024574, FT ECO:0000269|PubMed:8196478, ECO:0000269|PubMed:8396931, FT ECO:0000269|PubMed:8564208, ECO:0000269|PubMed:8832064" FT /id="VAR_019509" FT VARIANT 414 FT /note="K -> R (in dbSNP:rs3730247)" FT /id="VAR_049371" FT VARIANT 465 FT /note="E -> D (in dbSNP:rs2229126)" FT /id="VAR_049372" FT MUTAGEN 334 FT /note="K->A: Abolishes targeting to the nuclear membrane of FT cardiac myocytes; when associated with A-335; A-342; A-348 FT and A-349." FT /evidence="ECO:0000269|PubMed:22120526" FT MUTAGEN 335 FT /note="K->A: Abolishes targeting to the nuclear membrane of FT cardiac myocytes; when associated with A-334; A-342; A-348 FT and A-349." FT /evidence="ECO:0000269|PubMed:22120526" FT MUTAGEN 342 FT /note="R->A: Abolishes targeting to the nuclear membrane of FT cardiac myocytes; when associated with A-334; A-335; A-348 FT and A-349." FT /evidence="ECO:0000269|PubMed:22120526" FT MUTAGEN 348 FT /note="R->A: Abolishes targeting to the nuclear membrane of FT cardiac myocytes; when associated with A-334; A-335; A-342 FT and A-349." FT /evidence="ECO:0000269|PubMed:22120526" FT MUTAGEN 349 FT /note="K->A: Abolishes targeting to the nuclear membrane of FT cardiac myocytes; when associated with A-334; A-335; A-342 FT and A-348." FT /evidence="ECO:0000269|PubMed:22120526" FT CONFLICT 43 FT /note="G -> C (in Ref. 4; AAA93114)" FT /evidence="ECO:0000305" FT CONFLICT 129 FT /note="S -> T (in Ref. 4; AAA93114)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="Y -> H (in Ref. 9; AAK77197)" FT /evidence="ECO:0000305" FT CONFLICT 185 FT /note="V -> A (in Ref. 14; AAH95512)" FT /evidence="ECO:0000305" FT CONFLICT 338 FT /note="Q -> C (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 359 FT /note="T -> P (in Ref. 4; AAA93114)" FT /evidence="ECO:0000305" FT CONFLICT 384 FT /note="T -> A (in Ref. 9; AAK77197)" FT /evidence="ECO:0000305" FT CONFLICT 387 FT /note="R -> G (in Ref. 9; AAK77197)" FT /evidence="ECO:0000305" FT CONFLICT 390 FT /note="K -> R (in Ref. 9; AAK77197)" FT /evidence="ECO:0000305" FT CONFLICT 431 FT /note="Q -> E (in Ref. 1; BAA04960)" FT /evidence="ECO:0000305" FT CONFLICT 437 FT /note="G -> E (in Ref. 9; AAK77197)" FT /evidence="ECO:0000305" FT CONFLICT 442 FT /note="S -> C (in Ref. 4; AAA93114)" FT /evidence="ECO:0000305" FT HELIX 34..53 FT /evidence="ECO:0007829|PDB:8THK" FT TURN 55..58 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 60..74 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 75..79 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 80..89 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 96..100 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 102..129 FT /evidence="ECO:0007829|PDB:8THK" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:8HN1" FT HELIX 134..137 FT /evidence="ECO:0007829|PDB:8THK" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 143..158 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:8THK" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:8HN1" FT HELIX 182..189 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 190..194 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 195..214 FT /evidence="ECO:0007829|PDB:8THK" FT STRAND 260..264 FT /evidence="ECO:0007829|PDB:8HN1" FT HELIX 269..297 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 299..301 FT /evidence="ECO:0007829|PDB:8THK" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:9M4Q" FT HELIX 305..325 FT /evidence="ECO:0007829|PDB:8THK" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:7YM8" FT HELIX 332..342 FT /evidence="ECO:0007829|PDB:8HN1" FT CONFLICT P35348-4:453 FT /note="S -> L (in Ref. 7; AAC06138)" FT /evidence="ECO:0000305" FT CONFLICT P35348-6:302 FT /note="E -> Q (in Ref. 8; AAR84650)" FT /evidence="ECO:0000305" SQ SEQUENCE 466 AA; 51487 MW; 1A50487531DECDF0 CRC64; MVFLSGNASD SSNCTQPPAP VNISKAILLG VILGGLILFG VLGNILVILS VACHRHLHSV THYYIVNLAV ADLLLTSTVL PFSAIFEVLG YWAFGRVFCN IWAAVDVLCC TASIMGLCII SIDRYIGVSY PLRYPTIVTQ RRGLMALLCV WALSLVISIG PLFGWRQPAP EDETICQINE EPGYVLFSAL GSFYLPLAII LVMYCRVYVV AKRESRGLKS GLKTDKSDSE QVTLRIHRKN APAGGSGMAS AKTKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIGSFFPD FKPSETVFKI VFWLGYLNSC INPIIYPCSS QEFKKAFQNV LRIQCLCRKQ SSKHALGYTL HPPSQAVEGQ HKDMVRIPVG SRETFYRISK TDGVCEWKFF SSMPRGSARI TVSKDQSSCT TARVRSKSFL QVCCCVGPST PSLDKNHQVP TIKVHTISLS ENGEEV //