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Alpha-1-syntrophin (59 kDa dystrophin-associated protein A1 acidic component 1) (Syntrophin-1)

 SNTA1_MOUSE             Reviewed;         503 AA.
Q61234; Q8VEF3;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 168.
RecName: Full=Alpha-1-syntrophin;
AltName: Full=59 kDa dystrophin-associated protein A1 acidic component 1;
AltName: Full=Syntrophin-1;
Name=Snta1; Synonyms=Snt1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 155-161; 165-171;
213-228; 247-261 AND 271-307.
TISSUE=Muscle;
PubMed=7691103; DOI=10.1016/0896-6273(93)90157-M;
Adams M.E., Butler M.H., Dwyer T.M., Peters M.F., Murnane A.A.,
Froehner S.C.;
"Two forms of mouse syntrophin, a 58 kDa dystrophin-associated
protein, differ in primary structure and tissue distribution.";
Neuron 11:531-540(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 7-16, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4]
INTERACTION WITH SNTB1; SNTB2; DMD; SGCA AND SGCG.
PubMed=7547961; DOI=10.1021/bi00038a014;
Madhavan R., Jarrett H.W.;
"Interactions between dystrophin glycoprotein complex proteins.";
Biochemistry 34:12204-12209(1995).
[5]
INTERACTION WITH NOS1.
PubMed=8625413; DOI=10.1016/S0092-8674(00)81053-3;
Brenman J.E., Chao D.S., Gee S.H., McGee A.W., Craven S.E.,
Santillano D.R., Wu Z., Huang F., Xia H., Peters M.F., Froehner S.C.,
Bredt D.S.;
"Interaction of nitric oxide synthase with the postsynaptic density
protein PSD-95 and alpha1-syntrophin mediated by PDZ domains.";
Cell 84:757-767(1996).
[6]
INTERACTION WITH CALMODULIN.
PubMed=9063877; DOI=10.1021/bi962452n;
Newbell B.J., Anderson J.T., Jarrett H.W.;
"Ca2+-calmodulin binding to mouse alpha1 syntrophin: syntrophin is
also a Ca2+-binding protein.";
Biochemistry 36:1295-1305(1997).
[7]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH DMD;
DTNA AND UTRN.
PubMed=9214383; DOI=10.1083/jcb.138.1.81;
Peters M.F., Adams M.E., Froehner S.C.;
"Differential association of syntrophin pairs with the dystrophin
complex.";
J. Cell Biol. 138:81-93(1997).
[8]
INTERACTION WITH SCN4A AND SCN5A.
PubMed=9412493;
Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R.,
Froehner S.C.;
"Interaction of muscle and brain sodium channels with multiple members
of the syntrophin family of dystrophin-associated proteins.";
J. Neurosci. 18:128-137(1998).
[9]
ASSOCIATION WITH PHOSPHATIDYLINOSITOL 4,5-BIPHOSPHATE.
PubMed=10220348; DOI=10.1021/bi982564+;
Chockalingam P.S., Gee S.H., Jarrett H.W.;
"Pleckstrin homology domain 1 of mouse alpha 1-syntrophin binds
phosphatidylinositol 4,5-bisphosphate.";
Biochemistry 38:5596-5602(1999).
[10]
PHOSPHORYLATION BY CAM-KINASE II.
PubMed=10525145; DOI=10.1016/S0167-4838(99)00193-4;
Madhavan R., Jarrett H.W.;
"Phosphorylation of dystrophin and alpha-syntrophin by Ca(2+)-
calmodulin dependent protein kinase II.";
Biochim. Biophys. Acta 1434:260-274(1999).
[11]
OLIGOMERIZATION.
PubMed=10913299; DOI=10.1021/bi0000824;
Oak S.A., Jarrett H.W.;
"Oligomerization of mouse alpha 1-syntrophin and self-association of
its pleckstrin homology domain 1 containing sequences.";
Biochemistry 39:8870-8877(2000).
[12]
INTERACTION WITH GRB2.
PubMed=11551227; DOI=10.1021/bi010490n;
Oak S.A., Russo K., Petrucci T.C., Jarrett H.W.;
"Mouse alpha1-syntrophin binding to Grb2: further evidence of a role
for syntrophin in cell signaling.";
Biochemistry 40:11270-11278(2001).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-187, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-183; SER-187 AND
SER-194, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
INTERACTION WITH MYOC.
PubMed=22371502; DOI=10.1074/jbc.M111.224063;
Joe M.K., Kee C., Tomarev S.I.;
"Myocilin interacts with syntrophins and is member of dystrophin-
associated protein complex.";
J. Biol. Chem. 287:13216-13227(2012).
-!- FUNCTION: Adapter protein that binds to and probably organizes the
subcellular localization of a variety of membrane proteins. May
link various receptors to the actin cytoskeleton and the
extracellular matrix via the dystrophin glycoprotein complex.
Plays an important role in synapse formation and in the
organization of UTRN and acetylcholine receptors at the
neuromuscular synapse. Binds to phosphatidylinositol 4,5-
bisphosphate.
-!- SUBUNIT: Monomer and homodimer. Interacts with MAPK12, TGFA, GA
and F-actin (By similarity). Interacts with the other members of
the syntrophin family: SNTB1 and SNTB2; with dystrophin protein
DMD and related proteins DTNA and UTRN; SGCG and SGCA of the
dystrophin glycoprotein complex; NOS1; GRB2; calmodulin and the
sodium channel proteins SCN4A and SCN5A. Interacts with MYOC;
regulates muscle hypertrophy. {ECO:0000250,
ECO:0000269|PubMed:11551227, ECO:0000269|PubMed:22371502,
ECO:0000269|PubMed:7547961, ECO:0000269|PubMed:8625413,
ECO:0000269|PubMed:9063877, ECO:0000269|PubMed:9214383,
ECO:0000269|PubMed:9412493}.
-!- INTERACTION:
P11531:Dmd; NbExp=3; IntAct=EBI-295952, EBI-295928;
Q60631:Grb2; NbExp=3; IntAct=EBI-295952, EBI-1688;
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000269|PubMed:9214383}; Peripheral membrane protein
{ECO:0000269|PubMed:9214383}; Cytoplasmic side
{ECO:0000269|PubMed:9214383}. Cell junction
{ECO:0000269|PubMed:9214383}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:9214383}. Note=In skeletal muscle, it
localizes at the cytoplasmic side of the sarcolemmal membrane and
at neuromuscular junctions.
-!- TISSUE SPECIFICITY: High expression in skeletal muscle. Expressed
at intermediate level in heart, kidney and brain, and at low level
in intestine, liver, lung and testis.
{ECO:0000269|PubMed:9214383}.
-!- DOMAIN: The PH 1 domain mediates the oligomerization in a calcium
dependent manner, and the association with the
phosphatidylinositol 4,5-bisphosphate.
-!- DOMAIN: The PDZ domain binds to the last three or four amino acids
of ion channels and receptor proteins. The association with
dystrophin or related proteins probably leaves the PDZ domain
available to recruit proteins to the membrane.
-!- DOMAIN: The SU domain binds calmodulin in a calcium-dependent
manner.
-!- PTM: Phosphorylated by CaM-kinase II. Phosphorylation may inhibit
the interaction with DMD. {ECO:0000269|PubMed:10525145}.
-!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U00677; AAC52119.1; -; mRNA.
EMBL; BC018546; AAH18546.1; -; mRNA.
PIR; I84771; I84771.
UniGene; Mm.1541; -.
PDB; 1QAV; X-ray; 1.90 A; A=77-164.
PDB; 1Z86; NMR; -; A=79-165.
PDB; 1Z87; NMR; -; A=2-264.
PDB; 2ADZ; NMR; -; A=2-264.
PDB; 2PDZ; NMR; -; A=79-164.
PDB; 4HOP; X-ray; 2.29 A; A/C/E=77-162.
PDBsum; 1QAV; -.
PDBsum; 1Z86; -.
PDBsum; 1Z87; -.
PDBsum; 2ADZ; -.
PDBsum; 2PDZ; -.
PDBsum; 4HOP; -.
ProteinModelPortal; Q61234; -.
SMR; Q61234; -.
CORUM; Q61234; -.
DIP; DIP-32898N; -.
IntAct; Q61234; 10.
MINT; Q61234; -.
STRING; 10090.ENSMUSP00000105350; -.
iPTMnet; Q61234; -.
PhosphoSitePlus; Q61234; -.
MaxQB; Q61234; -.
PaxDb; Q61234; -.
PeptideAtlas; Q61234; -.
PRIDE; Q61234; -.
Ensembl; ENSMUST00000028991; ENSMUSP00000028991; ENSMUSG00000027488.
MGI; MGI:101772; Snta1.
eggNOG; ENOG410IMRM; Eukaryota.
eggNOG; ENOG410XS4Y; LUCA.
GeneTree; ENSGT00550000074581; -.
HOGENOM; HOG000231596; -.
HOVERGEN; HBG054204; -.
InParanoid; Q61234; -.
OMA; IGWLTEQ; -.
OrthoDB; EOG091G0O31; -.
PhylomeDB; Q61234; -.
TreeFam; TF317932; -.
EvolutionaryTrace; Q61234; -.
PRO; PR:Q61234; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027488; Expressed in 227 organ(s), highest expression level in gastrocnemius.
CleanEx; MM_SNTA1; -.
ExpressionAtlas; Q61234; baseline and differential.
Genevisible; Q61234; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0042383; C:sarcolemma; IDA:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0051117; F:ATPase binding; ISO:MGI.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; ISO:MGI.
GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISO:MGI.
GO; GO:0003117; P:regulation of vasoconstriction by circulating norepinephrine; IMP:MGI.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR028552; SNTA1.
InterPro; IPR015482; Syntrophin.
PANTHER; PTHR10554; PTHR10554; 1.
PANTHER; PTHR10554:SF6; PTHR10554:SF6; 1.
Pfam; PF00595; PDZ; 1.
Pfam; PF00169; PH; 1.
SMART; SM00228; PDZ; 1.
SMART; SM00233; PH; 2.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Calcium; Calmodulin-binding;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 503 Alpha-1-syntrophin.
/FTId=PRO_0000184007.
DOMAIN 6 263 PH 1. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 81 164 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 287 399 PH 2. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 447 503 SU.
REGION 481 503 Calmodulin-binding.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000250|UniProtKB:Q13424}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 16 16 R -> C (in Ref. 2; AAH18546).
{ECO:0000305}.
CONFLICT 341 344 Missing (in Ref. 2; AAH18546).
{ECO:0000305}.
CONFLICT 405 405 I -> V (in Ref. 2; AAH18546).
{ECO:0000305}.
STRAND 9 16 {ECO:0000244|PDB:1Z87}.
STRAND 20 24 {ECO:0000244|PDB:2ADZ}.
STRAND 28 35 {ECO:0000244|PDB:1Z87}.
STRAND 37 43 {ECO:0000244|PDB:1Z87}.
STRAND 63 67 {ECO:0000244|PDB:1Z87}.
TURN 75 77 {ECO:0000244|PDB:2ADZ}.
STRAND 80 85 {ECO:0000244|PDB:1QAV}.
TURN 88 90 {ECO:0000244|PDB:1QAV}.
STRAND 94 99 {ECO:0000244|PDB:1QAV}.
HELIX 100 102 {ECO:0000244|PDB:1QAV}.
STRAND 104 111 {ECO:0000244|PDB:1QAV}.
STRAND 113 115 {ECO:0000244|PDB:1Z86}.
HELIX 116 119 {ECO:0000244|PDB:1QAV}.
STRAND 127 132 {ECO:0000244|PDB:1QAV}.
HELIX 137 139 {ECO:0000244|PDB:1Z86}.
HELIX 142 150 {ECO:0000244|PDB:1QAV}.
STRAND 154 162 {ECO:0000244|PDB:1QAV}.
STRAND 164 167 {ECO:0000244|PDB:1Z87}.
STRAND 169 171 {ECO:0000244|PDB:1Z87}.
STRAND 176 178 {ECO:0000244|PDB:2ADZ}.
STRAND 180 182 {ECO:0000244|PDB:1Z87}.
STRAND 189 193 {ECO:0000244|PDB:1Z87}.
STRAND 195 197 {ECO:0000244|PDB:1Z87}.
STRAND 207 219 {ECO:0000244|PDB:1Z87}.
STRAND 225 227 {ECO:0000244|PDB:1Z87}.
STRAND 229 234 {ECO:0000244|PDB:1Z87}.
TURN 235 238 {ECO:0000244|PDB:1Z87}.
STRAND 239 244 {ECO:0000244|PDB:1Z87}.
HELIX 248 262 {ECO:0000244|PDB:1Z87}.
SEQUENCE 503 AA; 53665 MW; 161BA76CAF50AE96 CRC64;
MASGRRAPRT GLLELRCGAG SGAGGERWQR VLLSLAEDAL TVSPADGEPG PEPEPAQLNG
AAEPGAAPPQ LPEALLLQRR RVTVRKADAG GLGISIKGGR ENKMPILISK IFKGLAADQT
EALFVGDAIL SVNGEDLSSA THDEAVQALK KTGKEVVLEV KYMKEVSPYF KNSAGGTSVG
WDSPPASPLQ RQPSSPGPQP RNLSEAKHVS LKMAYVSRRC TPTDPEPRYL EICAADGQDA
VFLRAKDEAS ARSWAGAIQA QIGTFIPWVK DELQALLTAT GTAGSQDIKQ IGWLTEQLPS
GGTAPTLALL TEKELLFYCS LPQSREALSR PTRTAPLIAT SSAHRLVHSG PSKGSVPYDA
ELSFALRTGT RHGVDTHLFS VESPQELAAW TRQLVDGCHR AAEGIQEVST ACTWNGRPCS
LSVHIDKGFT LWAAEPGAAR AMLLRQPFEK LQMSSDDGTS LLFLDFGGAE GEIQLDLHSC
PKTMVFIIHS FLSAKVTRLG LLA


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