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ADA1A_HUMAN
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   03-AUG-2022, entry version 211.
DE   RecName: Full=Alpha-1A adrenergic receptor;
DE   AltName: Full=Alpha-1A adrenoreceptor;
DE            Short=Alpha-1A adrenoceptor;
DE   AltName: Full=Alpha-1C adrenergic receptor;
DE   AltName: Full=Alpha-adrenergic receptor 1c;
GN   Name=ADRA1A; 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), AND VARIANT ARG-347.
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).
RC   TISSUE=Hippocampus, and Lymphocyte;
RX   PubMed=8183249;
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), AND VARIANT ARG-347.
RX   PubMed=7815325;
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, 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]
RP   VARIANT ARG-347.
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   [20]
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   [21]
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: This alpha-adrenergic receptor mediates its action by
CC       association with G proteins that activate a phosphatidylinositol-
CC       calcium second messenger system. Its effect is mediated by G(q) and
CC       G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate
CC       phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes.
CC       {ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526}.
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; Multi-pass membrane protein.
CC       Cell membrane {ECO:0000269|PubMed:24567387}; Multi-pass membrane
CC       protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:24567387}.
CC       Membrane, caveola {ECO:0000269|PubMed:24567387}. Note=Location at the
CC       nuclear membrane facilitates heterooligomerization and regulates ERK-
CC       mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as
CC       well as LAP2 at the nuclear membrane of cardiac myocytes.
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};
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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_000680.3. [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_006716293.3. [P35348-3]
DR   RefSeq; XP_011542713.1; XM_011544411.2. [P35348-7]
DR   AlphaFoldDB; P35348; -.
DR   SMR; P35348; -.
DR   BioGRID; 106658; 26.
DR   CORUM; P35348; -.
DR   DIP; DIP-33401N; -.
DR   IntAct; P35348; 33.
DR   MINT; P35348; -.
DR   STRING; 9606.ENSP00000369960; -.
DR   BindingDB; P35348; -.
DR   ChEMBL; CHEMBL229; -.
DR   DrugBank; DB01472; 4-Methoxyamphetamine.
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; DB01295; Bevantolol.
DR   DrugBank; DB01200; Bromocriptine.
DR   DrugBank; DB00490; Buspirone.
DR   DrugBank; DB00248; Cabergoline.
DR   DrugBank; DB01136; Carvedilol.
DR   DrugBank; DB00477; Chlorpromazine.
DR   DrugBank; DB09202; Cirazoline.
DR   DrugBank; DB00575; Clonidine.
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; 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; DB04948; Lofexidine.
DR   DrugBank; DB09195; Lorpiprazole.
DR   DrugBank; DB00408; Loxapine.
DR   DrugBank; DB00934; Maprotiline.
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; DB00370; Mirtazapine.
DR   DrugBank; DB09205; Moxisylyte.
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; DB09203; Synephrine.
DR   DrugBank; DB00706; Tamsulosin.
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; DB00661; Verapamil.
DR   DrugBank; DB06694; Xylometazoline.
DR   DrugBank; DB00246; Ziprasidone.
DR   DrugBank; DB01624; Zuclopenthixol.
DR   DrugCentral; P35348; -.
DR   GuidetoPHARMACOLOGY; 22; -.
DR   GlyGen; P35348; 3 sites.
DR   iPTMnet; P35348; -.
DR   PhosphoSitePlus; P35348; -.
DR   BioMuta; ADRA1A; -.
DR   DMDM; 1168246; -.
DR   MassIVE; P35348; -.
DR   PaxDb; P35348; -.
DR   PeptideAtlas; P35348; -.
DR   PRIDE; P35348; -.
DR   ProteomicsDB; 55030; -. [P35348-5]
DR   ProteomicsDB; 55032; -. [P35348-7]
DR   ProteomicsDB; 55033; -. [P35348-8]
DR   Antibodypedia; 10062; 375 antibodies from 38 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   CTD; 148; -.
DR   DisGeNET; 148; -.
DR   GeneCards; ADRA1A; -.
DR   HGNC; HGNC:277; ADRA1A.
DR   HPA; ENSG00000120907; Tissue enhanced (adipose tissue, brain, liver).
DR   MIM; 104221; gene.
DR   neXtProt; NX_P35348; -.
DR   OpenTargets; ENSG00000120907; -.
DR   PharmGKB; PA34; -.
DR   VEuPathDB; HostDB:ENSG00000120907; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000159105; -.
DR   HOGENOM; CLU_009579_11_6_1; -.
DR   InParanoid; P35348; -.
DR   OMA; KHHFSVR; -.
DR   OrthoDB; 1095345at2759; -.
DR   PhylomeDB; P35348; -.
DR   TreeFam; TF331895; -.
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   BioGRID-ORCS; 148; 6 hits in 1074 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 108 other tissues.
DR   ExpressionAtlas; P35348; baseline and differential.
DR   Genevisible; P35348; HS.
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:0098691; C:dopaminergic synapse; IEA:Ensembl.
DR   GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0004937; F:alpha1-adrenergic receptor activity; ISS:BHF-UCL.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0007202; P:activation of phospholipase C activity; ISS:BHF-UCL.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007512; P:adult heart development; IEA:Ensembl.
DR   GO; GO:0007568; P:aging; ISS:BHF-UCL.
DR   GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR   GO; GO:0060402; P:calcium ion transport into cytosol; ISS:BHF-UCL.
DR   GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IEA:Ensembl.
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:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0060073; P:micturition; IEA:Ensembl.
DR   GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR   GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0001985; P:negative regulation of heart rate involved in baroreceptor response to increased systemic arterial blood pressure; IEA:Ensembl.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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; IEA:Ensembl.
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:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IBA:GO_Central.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR   GO; GO:1903997; P:positive regulation of non-membrane spanning protein tyrosine kinase activity; IEA:Ensembl.
DR   GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISS:BHF-UCL.
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:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Ensembl.
DR   GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; IEA:Ensembl.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; ISS:BHF-UCL.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
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   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR001004; ADRA1A_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Nucleus;
KW   Palmitate; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW   Transmembrane; 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   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   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   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
 
 
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