Alpha-1-syntrophin - Mus musculus (Mouse)

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Q61234 (SNTA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-1-syntrophin

Alternative name(s):
59 kDa dystrophin-associated protein A1 acidic component 1
Syntrophin-1

Gene names

Name:	Snta1
Synonyms:	Snt1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12
Subcellular location	Cell membrane › sarcolemma; Peripheral membrane protein; Cytoplasmic side. Cell junction. Cytoplasm › cytoskeleton. Note: In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions. Ref.7
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. Ref.7
Domain	The PH 1 domain mediates the oligomerization in a calcium dependent manner, and the association with the phosphatidylinositol 4,5-bisphosphate. 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. The SU domain binds calmodulin in a calcium-dependent manner.
Post-translational modification	Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the interaction with DMD. Ref.10
Sequence similarities	Belongs to the syntrophin family. Contains 1 PDZ (DHR) domain. Contains 2 PH domains. Contains 1 SU (syntrophin unique) domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
Domain	Repeat
Ligand	Actin-binding Calcium Calmodulin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	neuromuscular junction development Inferred from mutant phenotype PubMed 10995443. Source: MGI regulation of vasoconstriction by circulating norepinephrine Inferred from mutant phenotype PubMed 12600881. Source: MGI
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from direct assay PubMed 10995443. Source: MGI protein complex Inferred from sequence orthology PubMed 18468998. Source: MGI sarcolemma Inferred from direct assay PubMed 11115849. Source: MGI
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dmd	P11531	2	EBI-295952,EBI-295928

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 503

503

Alpha-1-syntrophin

PRO_0000184007

Regions

Domain

6 – 263

258

PH 1

Domain

81 – 164

PDZ

Domain

287 – 399

113

PH 2

Domain

447 – 503

Region

481 – 503

Calmodulin-binding

Amino acid modifications

Modified residue

183

Phosphoserine Ref.13 Ref.14

Modified residue

187

Phosphoserine Ref.14

Experimental info

Sequence conflict

R → C in AAH18546. Ref.2

Sequence conflict

341 – 344

Missing in AAH18546. Ref.2

Sequence conflict

405

I → V in AAH18546. Ref.2

Secondary structure

503

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q61234 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 161BA76CAF50AE96
Show »

FASTA

503

53,665

        10         20         30         40         50         60 
MASGRRAPRT GLLELRCGAG SGAGGERWQR VLLSLAEDAL TVSPADGEPG PEPEPAQLNG 

        70         80         90        100        110        120 
AAEPGAAPPQ LPEALLLQRR RVTVRKADAG GLGISIKGGR ENKMPILISK IFKGLAADQT 

       130        140        150        160        170        180 
EALFVGDAIL SVNGEDLSSA THDEAVQALK KTGKEVVLEV KYMKEVSPYF KNSAGGTSVG 

       190        200        210        220        230        240 
WDSPPASPLQ RQPSSPGPQP RNLSEAKHVS LKMAYVSRRC TPTDPEPRYL EICAADGQDA 

       250        260        270        280        290        300 
VFLRAKDEAS ARSWAGAIQA QIGTFIPWVK DELQALLTAT GTAGSQDIKQ IGWLTEQLPS 

       310        320        330        340        350        360 
GGTAPTLALL TEKELLFYCS LPQSREALSR PTRTAPLIAT SSAHRLVHSG PSKGSVPYDA 

       370        380        390        400        410        420 
ELSFALRTGT RHGVDTHLFS VESPQELAAW TRQLVDGCHR AAEGIQEVST ACTWNGRPCS 

       430        440        450        460        470        480 
LSVHIDKGFT LWAAEPGAAR AMLLRQPFEK LQMSSDDGTS LLFLDFGGAE GEIQLDLHSC 

       490        500 
PKTMVFIIHS FLSAKVTRLG LLA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two forms of mouse syntrophin, a 58 kDa dystrophin-associated protein, differ in primary structure and tissue distribution." Adams M.E., Butler M.H., Dwyer T.M., Peters M.F., Murnane A.A., Froehner S.C. Neuron 11:531-540(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 155-161; 165-171; 213-228; 247-261 AND 271-307. Tissue: Muscle.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
[3]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 7-16, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[4]	"Interactions between dystrophin glycoprotein complex proteins." Madhavan R., Jarrett H.W. Biochemistry 34:12204-12209(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SNTB1; SNTB2; DMD; SGCA AND SGCG.
[5]	"Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains." 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. Cell 84:757-767(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NOS1.
[6]	"Ca2+-calmodulin binding to mouse alpha1 syntrophin: syntrophin is also a Ca2+-binding protein." Newbell B.J., Anderson J.T., Jarrett H.W. Biochemistry 36:1295-1305(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CALMODULIN.
[7]	"Differential association of syntrophin pairs with the dystrophin complex." Peters M.F., Adams M.E., Froehner S.C. J. Cell Biol. 138:81-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH DMD; DTNA AND UTRN.
[8]	"Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins." Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R., Froehner S.C. J. Neurosci. 18:128-137(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCN4A AND SCN5A.
[9]	"Pleckstrin homology domain 1 of mouse alpha 1-syntrophin binds phosphatidylinositol 4,5-bisphosphate." Chockalingam P.S., Gee S.H., Jarrett H.W. Biochemistry 38:5596-5602(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH PHOSPHATIDYLINOSITOL 4,5-BIPHOSPHATE.
[10]	"Phosphorylation of dystrophin and alpha-syntrophin by Ca(2+)-calmodulin dependent protein kinase II." Madhavan R., Jarrett H.W. Biochim. Biophys. Acta 1434:260-274(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY CAM-KINASE II.
[11]	"Oligomerization of mouse alpha 1-syntrophin and self-association of its pleckstrin homology domain 1 containing sequences." Oak S.A., Jarrett H.W. Biochemistry 39:8870-8877(2000) [PubMed] [Europe PMC] [Abstract] Cited for: OLIGOMERIZATION.
[12]	"Mouse alpha1-syntrophin binding to Grb2: further evidence of a role for syntrophin in cell signaling." Oak S.A., Russo K., Petrucci T.C., Jarrett H.W. Biochemistry 40:11270-11278(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB2.
[13]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, MASS SPECTROMETRY. Tissue: Brain cortex.
[14]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-187, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00677 mRNA. Translation: AAC52119.1.
BC018546 mRNA. Translation: AAH18546.1.

IPI

IPI00267848.

PIR

I84771.

UniGene

Mm.1541.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QAV	X-ray	1.90	A	77-164	[»]
1Z86	NMR	-	A	79-165	[»]
1Z87	NMR	-	A	2-264	[»]
2ADZ	NMR	-	A	2-264	[»]
2PDZ	NMR	-	A	79-164	[»]

ProteinModelPortal

Q61234.

SMR

Q61234. Positions 2-264.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32898N.

IntAct

Q61234. 3 interactions.

MINT

MINT-99385.

PTM databases

PhosphoSite

Q61234.

Proteomic databases

PaxDb

Q61234.

PRIDE

Q61234.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000028991; ENSMUSP00000028991; ENSMUSG00000027488.

Organism-specific databases

MGI

MGI:101772. Snta1.

Phylogenomic databases

eggNOG

NOG318350.

GeneTree

ENSGT00550000074581.

HOGENOM

HOG000231596.

HOVERGEN

HBG054204.

InParanoid

Q61234.

OMA

TGTRHGV.

Gene expression databases

ArrayExpress

Q61234.

Bgee

Q61234.

CleanEx

MM_SNTA1.

Genevestigator

Q61234.

GermOnline

ENSMUSG00000027488. Mus musculus.

Family and domain databases

InterPro

IPR001478. PDZ.
IPR001849. Pleckstrin_homology.
IPR015482. Syntrophin.
[Graphical view]

PANTHER

PTHR10554. PTHR10554. 1 hit.

Pfam

PF00595. PDZ. 1 hit.
[Graphical view]

SMART

SM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]

SUPFAM

SSF50156. PDZ. 1 hit.

PROSITE

PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q61234.

SOURCE

Search...

Entry information

Entry name

SNTA1_MOUSE

Accession

Primary (citable) accession number: Q61234
Secondary accession number(s): Q8VEF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents