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Q61234 (SNTA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1-syntrophin
Alternative name(s):
59 kDa dystrophin-associated protein A1 acidic component 1
Syntrophin-1
Gene names
Name:Snta1
Synonyms:Snt1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Interacts with MYOC; regulates muscle hypertrophy. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.14

Subcellular location

Cell membranesarcolemma; Peripheral membrane protein; Cytoplasmic side. Cell junction. Cytoplasmcytoskeleton. 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DmdP115312EBI-295952,EBI-295928

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Alpha-1-syntrophin
PRO_0000184007

Regions

Domain6 – 263258PH 1
Domain81 – 16484PDZ
Domain287 – 399113PH 2
Domain447 – 50357SU
Region481 – 50323Calmodulin-binding

Amino acid modifications

Modified residue1831Phosphoserine Ref.13
Modified residue1871Phosphoserine Ref.13

Experimental info

Sequence conflict161R → C in AAH18546. Ref.2
Sequence conflict341 – 3444Missing in AAH18546. Ref.2
Sequence conflict4051I → V in AAH18546. Ref.2

Secondary structure

....................................................... 503
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61234 [UniParc].

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

FASTA50353,665
        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' 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, IDENTIFICATION BY 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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[14]"Myocilin interacts with syntrophins and is member of dystrophin-associated protein complex."
Joe M.K., Kee C., Tomarev S.I.
J. Biol. Chem. 287:13216-13227(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYOC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00677 mRNA. Translation: AAC52119.1.
BC018546 mRNA. Translation: AAH18546.1.
PIRI84771.
UniGeneMm.1541.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QAVX-ray1.90A77-164[»]
1Z86NMR-A79-165[»]
1Z87NMR-A2-264[»]
2ADZNMR-A2-264[»]
2PDZNMR-A79-164[»]
4HOPX-ray2.29A/C/E77-162[»]
ProteinModelPortalQ61234.
SMRQ61234. Positions 2-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-32898N.
IntActQ61234. 4 interactions.
MINTMINT-99385.

PTM databases

PhosphoSiteQ61234.

Proteomic databases

MaxQBQ61234.
PaxDbQ61234.
PRIDEQ61234.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028991; ENSMUSP00000028991; ENSMUSG00000027488.

Organism-specific databases

MGIMGI:101772. Snta1.

Phylogenomic databases

eggNOGNOG318350.
GeneTreeENSGT00550000074581.
HOGENOMHOG000231596.
HOVERGENHBG054204.
InParanoidQ61234.
OMATGTRHGV.
PhylomeDBQ61234.
TreeFamTF317932.

Gene expression databases

ArrayExpressQ61234.
BgeeQ61234.
CleanExMM_SNTA1.
GenevestigatorQ61234.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR001478. PDZ.
IPR001849. Pleckstrin_homology.
IPR028552. SNTA1.
IPR015482. Syntrophin.
[Graphical view]
PANTHERPTHR10554. PTHR10554. 1 hit.
PTHR10554:SF6. PTHR10554:SF6. 1 hit.
PfamPF00595. PDZ. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ61234.
PROQ61234.
SOURCESearch...

Entry information

Entry nameSNTA1_MOUSE
AccessionPrimary (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: June 11, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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