SNTA1_HUMAN
ID SNTA1_HUMAN Reviewed; 505 AA.
AC Q13424; A8K7H9; B4DX40; E1P5N1; Q16438;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Alpha-1-syntrophin;
DE AltName: Full=59 kDa dystrophin-associated protein A1 acidic component 1;
DE AltName: Full=Pro-TGF-alpha cytoplasmic domain-interacting protein 1;
DE Short=TACIP1;
DE AltName: Full=Syntrophin-1;
GN Name=SNTA1; Synonyms=SNT1;
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 [MRNA] (ISOFORM 1), AND INTERACTION WITH DMD; DTNA AND
RP UTRN.
RC TISSUE=Muscle;
RX PubMed=8576247; DOI=10.1074/jbc.271.5.2724;
RA Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.;
RT "The three human syntrophin genes are expressed in diverse tissues, have
RT distinct chromosomal locations, and each bind to dystrophin and its
RT relatives.";
RL J. Biol. Chem. 271:2724-2730(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH DMD.
RC TISSUE=Heart;
RX PubMed=8612778; DOI=10.1016/0014-5793(96)00214-1;
RA Castello A., Brocheriou V., Chafey P., Kahn A., Gilgenkrantz H.;
RT "Characterization of the dystrophin-syntrophin interaction using the two-
RT hybrid system in yeast.";
RL FEBS Lett. 383:124-128(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH MAPK12.
RX PubMed=10212242; DOI=10.1074/jbc.274.18.12626;
RA Hasegawa M., Cuenda A., Spillantini M.G., Thomas G.M., Buee-Scherrer V.,
RA Cohen P., Goedert M.;
RT "Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-
RT syntrophin. A mechanism for specific substrate recognition.";
RL J. Biol. Chem. 274:12626-12631(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Small intestine, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
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 [8]
RP INTERACTION WITH TGFA.
RX PubMed=10230395; DOI=10.1016/s1097-2765(00)80470-0;
RA Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J., Arribas J.;
RT "A role for a PDZ protein in the early secretory pathway for the targeting
RT of proTGF-alpha to the cell surface.";
RL Mol. Cell 3:423-433(1999).
RN [9]
RP INTERACTION WITH GA.
RX PubMed=11163757; DOI=10.1016/s0014-5793(00)02373-5;
RA Olalla L., Aledo J.C., Bannenberg G., Marquez J.;
RT "The C-terminus of human glutaminase L mediates association with PDZ
RT domain-containing proteins.";
RL FEBS Lett. 488:116-122(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP VARIANT LQT12 GLY-257, AND CHARACTERIZATION OF VARIANT LQT12 GLY-257.
RX PubMed=19684871; DOI=10.1161/circep.108.769224;
RA Wu G., Ai T., Kim J.J., Mohapatra B., Xi Y., Li Z., Abbasi S., Purevjav E.,
RA Samani K., Ackerman M.J., Qi M., Moss A.J., Shimizu W., Towbin J.A.,
RA Cheng J., Vatta M.;
RT "alpha-1-syntrophin mutation and the long-QT syndrome: a disease of sodium
RT channel disruption.";
RL Circ. Arrhythm. Electrophysiol. 1:193-201(2008).
RN [17]
RP VARIANT LQT12 VAL-390, AND CHARACTERIZATION OF VARIANT LQT12 VAL-390.
RX PubMed=18591664; DOI=10.1073/pnas.0801294105;
RA Ueda K., Valdivia C., Medeiros-Domingo A., Tester D.J., Vatta M.,
RA Farrugia G., Ackerman M.J., Makielski J.C.;
RT "Syntrophin mutation associated with long QT syndrome through activation of
RT the nNOS-SCN5A macromolecular complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9355-9360(2008).
CC -!- FUNCTION: Adapter protein that binds to and probably organizes the
CC subcellular localization of a variety of membrane proteins. May link
CC various receptors to the actin cytoskeleton and the extracellular
CC matrix via the dystrophin glycoprotein complex. Plays an important role
CC in synapse formation and in the organization of UTRN and acetylcholine
CC receptors at the neuromuscular synapse. Binds to phosphatidylinositol
CC 4,5-bisphosphate (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with the other members of the
CC syntrophin family SNTB1 and SNTB2; SGCG and SGCA of the dystrophin
CC glycoprotein complex; NOS1; GRB2; the sodium channel proteins SCN4A and
CC SCN5A; F-actin and calmodulin (By similarity). Interacts with
CC dystrophin protein DMD and related proteins DTNA and UTRN and with
CC MAPK12, TGFA and GA. Interacts with MYOC; regulates muscle hypertrophy
CC (By similarity). Interacts with DTNB (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q61234}.
CC -!- INTERACTION:
CC Q13424; O95477: ABCA1; NbExp=2; IntAct=EBI-717191, EBI-784112;
CC Q13424; P25100: ADRA1D; NbExp=11; IntAct=EBI-717191, EBI-489993;
CC Q13424; Q63538: Mapk12; Xeno; NbExp=5; IntAct=EBI-717191, EBI-783937;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=In skeletal muscle, it localizes at the cytoplasmic
CC side of the sarcolemmal membrane and at neuromuscular junctions.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13424-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13424-2; Sequence=VSP_056827;
CC -!- TISSUE SPECIFICITY: High expression in skeletal muscle and heart. Low
CC expression in brain, pancreas, liver, kidney and lung. Not detected in
CC placenta.
CC -!- DOMAIN: The PH 1 domain mediates the oligomerization in a calcium
CC dependent manner, and the association with the phosphatidylinositol
CC 4,5-bisphosphate. {ECO:0000250}.
CC -!- DOMAIN: The PDZ domain binds to the last three or four amino acids of
CC ion channels and receptor proteins. The association with dystrophin or
CC related proteins probably leaves the PDZ domain available to recruit
CC proteins to the membrane (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The SU domain binds calmodulin in a calcium-dependent manner.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the
CC interaction with DMD (By similarity). {ECO:0000250}.
CC -!- DISEASE: Long QT syndrome 12 (LQT12) [MIM:612955]: A heart disorder
CC characterized by a prolonged QT interval on the ECG and polymorphic
CC ventricular arrhythmias. They cause syncope and sudden death in
CC response to exercise or emotional stress, and can present with a
CC sentinel event of sudden cardiac death in infancy.
CC {ECO:0000269|PubMed:18591664, ECO:0000269|PubMed:19684871}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}.
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DR EMBL; U40571; AAC50448.1; -; mRNA.
DR EMBL; S81737; AAB36398.1; -; mRNA.
DR EMBL; AL355392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK291994; BAF84683.1; -; mRNA.
DR EMBL; AK301800; BAG63252.1; -; mRNA.
DR EMBL; CH471077; EAW76316.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76317.1; -; Genomic_DNA.
DR EMBL; BC026215; AAH26215.1; -; mRNA.
DR CCDS; CCDS13220.1; -. [Q13424-1]
DR PIR; S62894; S62894.
DR RefSeq; NP_003089.1; NM_003098.2. [Q13424-1]
DR AlphaFoldDB; Q13424; -.
DR BMRB; Q13424; -.
DR SMR; Q13424; -.
DR BioGRID; 112523; 95.
DR DIP; DIP-966N; -.
DR IntAct; Q13424; 36.
DR MINT; Q13424; -.
DR STRING; 9606.ENSP00000217381; -.
DR iPTMnet; Q13424; -.
DR PhosphoSitePlus; Q13424; -.
DR BioMuta; SNTA1; -.
DR DMDM; 23822157; -.
DR EPD; Q13424; -.
DR jPOST; Q13424; -.
DR MassIVE; Q13424; -.
DR MaxQB; Q13424; -.
DR PaxDb; Q13424; -.
DR PeptideAtlas; Q13424; -.
DR PRIDE; Q13424; -.
DR ProteomicsDB; 59409; -. [Q13424-1]
DR Antibodypedia; 10673; 451 antibodies from 34 providers.
DR DNASU; 6640; -.
DR Ensembl; ENST00000217381.3; ENSP00000217381.2; ENSG00000101400.6. [Q13424-1]
DR GeneID; 6640; -.
DR KEGG; hsa:6640; -.
DR MANE-Select; ENST00000217381.3; ENSP00000217381.2; NM_003098.3; NP_003089.1.
DR UCSC; uc002wzd.2; human. [Q13424-1]
DR CTD; 6640; -.
DR DisGeNET; 6640; -.
DR GeneCards; SNTA1; -.
DR GeneReviews; SNTA1; -.
DR HGNC; HGNC:11167; SNTA1.
DR HPA; ENSG00000101400; Tissue enhanced (brain, skeletal muscle, tongue).
DR MalaCards; SNTA1; -.
DR MIM; 601017; gene.
DR MIM; 612955; phenotype.
DR neXtProt; NX_Q13424; -.
DR OpenTargets; ENSG00000101400; -.
DR Orphanet; 101016; Romano-Ward syndrome.
DR PharmGKB; PA36007; -.
DR VEuPathDB; HostDB:ENSG00000101400; -.
DR eggNOG; KOG3551; Eukaryota.
DR GeneTree; ENSGT00950000182863; -.
DR HOGENOM; CLU_026406_3_1_1; -.
DR InParanoid; Q13424; -.
DR OMA; DIKHIGW; -.
DR OrthoDB; 1261897at2759; -.
DR PhylomeDB; Q13424; -.
DR TreeFam; TF317932; -.
DR PathwayCommons; Q13424; -.
DR SignaLink; Q13424; -.
DR SIGNOR; Q13424; -.
DR BioGRID-ORCS; 6640; 33 hits in 1082 CRISPR screens.
DR ChiTaRS; SNTA1; human.
DR GeneWiki; Syntrophin,_alpha_1; -.
DR GenomeRNAi; 6640; -.
DR Pharos; Q13424; Tbio.
DR PRO; PR:Q13424; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q13424; protein.
DR Bgee; ENSG00000101400; Expressed in apex of heart and 184 other tissues.
DR Genevisible; Q13424; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IDA:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0016013; C:syntrophin complex; TAS:BHF-UCL.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0017080; F:sodium channel regulator activity; IMP:BHF-UCL.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; IMP:BHF-UCL.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0003117; P:regulation of vasoconstriction by circulating norepinephrine; IEA:Ensembl.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
DR CDD; cd01258; PHsplit_syntrophin; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR041428; PHsplit_syntrophin.
DR InterPro; IPR028552; SNTA1.
DR InterPro; IPR015482; Syntrophin.
DR PANTHER; PTHR10554; PTHR10554; 1.
DR PANTHER; PTHR10554:SF6; PTHR10554:SF6; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF18012; PH_17; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calcium; Calmodulin-binding;
KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Disease variant;
KW Long QT syndrome; Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..505
FT /note="Alpha-1-syntrophin"
FT /id="PRO_0000184006"
FT DOMAIN 6..269
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 87..170
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 293..401
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 449..505
FT /note="SU"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..505
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 180..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61234"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61234"
FT VAR_SEQ 254..328
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056827"
FT VARIANT 257
FT /note="A -> G (in LQT12; leads to a gain of function of the
FT voltage dependent sodium channel; dbSNP:rs56157422)"
FT /evidence="ECO:0000269|PubMed:19684871"
FT /id="VAR_062399"
FT VARIANT 364
FT /note="L -> F (in dbSNP:rs1046815)"
FT /id="VAR_014075"
FT VARIANT 390
FT /note="A -> V (in LQT12; results in released inhibition of
FT nNOS, S-nitrosylation of SCN5A and increased late sodium
FT current; dbSNP:rs121434500)"
FT /evidence="ECO:0000269|PubMed:18591664"
FT /id="VAR_062400"
FT CONFLICT 6
FT /note="R -> P (in Ref. 2; AAB36398)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="G -> A (in Ref. 2; AAB36398)"
FT /evidence="ECO:0000305"
FT CONFLICT 32..33
FT /note="LL -> PV (in Ref. 2; AAB36398)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="G -> D (in Ref. 2; AAB36398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 53895 MW; C07DA5F21C775CF8 CRC64;
MASGRRAPRT GLLELRAGAG SGAGGERWQR VLLSLAEDVL TVSPADGDPG PEPGAPREQE
PAQLNGAAEP GAGPPQLPEA LLLQRRRVTV RKADAGGLGI SIKGGRENKM PILISKIFKG
LAADQTEALF VGDAILSVNG EDLSSATHDE AVQVLKKTGK EVVLEVKYMK DVSPYFKNST
GGTSVGWDSP PASPLQRQPS SPGPTPRNFS EAKHMSLKMA YVSKRCTPND PEPRYLEICS
ADGQDTLFLR AKDEASARSW ATAIQAQVNT LTPRVKDELQ ALLAATSTAG SQDIKQIGWL
TEQLPSGGTA PTLALLTEKE LLLYLSLPET REALSRPART APLIATRLVH SGPSKGSVPY
DAELSFALRT GTRHGVDTHL FSVESPQELA AWTRQLVDGC HRAAEGVQEV STACTWNGRP
CSLSVHIDKG FTLWAAEPGA ARAVLLRQPF EKLQMSSDDG ASLLFLDFGG AEGEIQLDLH
SCPKTIVFII HSFLSAKVTR LGLLA
