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Protein

Alpha-1-syntrophin

Gene

Snta1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1-syntrophin
Alternative name(s):
59 kDa dystrophin-associated protein A1 acidic component 1
Syntrophin-1
Gene namesi
Name:Snta1
Synonyms:Snt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:101772. Snta1.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • intracellular Source: MGI
  • postsynaptic membrane Source: MGI
  • protein complex Source: MGI
  • sarcolemma Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001840071 – 503Alpha-1-syntrophinAdd BLAST503

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei95PhosphoserineCombined sources1
Modified residuei178PhosphoserineBy similarity1
Modified residuei183PhosphoserineCombined sources1
Modified residuei187PhosphoserineCombined sources1
Modified residuei194PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the interaction with DMD.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ61234.
PaxDbiQ61234.
PeptideAtlasiQ61234.
PRIDEiQ61234.

PTM databases

iPTMnetiQ61234.
PhosphoSitePlusiQ61234.

Expressioni

Tissue specificityi

High expression in skeletal muscle. Expressed at intermediate level in heart, kidney and brain, and at low level in intestine, liver, lung and testis.1 Publication

Gene expression databases

BgeeiENSMUSG00000027488.
CleanExiMM_SNTA1.
ExpressionAtlasiQ61234. baseline and differential.
GenevisibleiQ61234. MM.

Interactioni

Subunit structurei

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.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DmdP115312EBI-295952,EBI-295928
Grb2Q606313EBI-295952,EBI-1688

GO - Molecular functioni

  • ATPase binding Source: MGI
  • ion channel binding Source: BHF-UCL
  • nitric-oxide synthase binding Source: MGI

Protein-protein interaction databases

DIPiDIP-32898N.
IntActiQ61234. 6 interactors.
MINTiMINT-99385.
STRINGi10090.ENSMUSP00000105350.

Structurei

Secondary structure

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 16Combined sources8
Beta strandi20 – 24Combined sources5
Beta strandi28 – 35Combined sources8
Beta strandi37 – 43Combined sources7
Beta strandi63 – 67Combined sources5
Turni75 – 77Combined sources3
Beta strandi80 – 85Combined sources6
Turni88 – 90Combined sources3
Beta strandi94 – 99Combined sources6
Helixi100 – 102Combined sources3
Beta strandi104 – 111Combined sources8
Beta strandi113 – 115Combined sources3
Helixi116 – 119Combined sources4
Beta strandi127 – 132Combined sources6
Helixi137 – 139Combined sources3
Helixi142 – 150Combined sources9
Beta strandi154 – 162Combined sources9
Beta strandi164 – 167Combined sources4
Beta strandi169 – 171Combined sources3
Beta strandi176 – 178Combined sources3
Beta strandi180 – 182Combined sources3
Beta strandi189 – 193Combined sources5
Beta strandi195 – 197Combined sources3
Beta strandi207 – 219Combined sources13
Beta strandi225 – 227Combined sources3
Beta strandi229 – 234Combined sources6
Turni235 – 238Combined sources4
Beta strandi239 – 244Combined sources6
Helixi248 – 262Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ61234.
SMRiQ61234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61234.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 263PH 1PROSITE-ProRule annotationAdd BLAST258
Domaini81 – 164PDZPROSITE-ProRule annotationAdd BLAST84
Domaini287 – 399PH 2PROSITE-ProRule annotationAdd BLAST113
Domaini447 – 503SUAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni481 – 503Calmodulin-bindingAdd BLAST23

Domaini

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.

Sequence similaritiesi

Belongs to the syntrophin family.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IMRM. Eukaryota.
ENOG410XS4Y. LUCA.
GeneTreeiENSGT00550000074581.
HOGENOMiHOG000231596.
HOVERGENiHBG054204.
InParanoidiQ61234.
OMAiKEMSAFF.
OrthoDBiEOG091G0O31.
PhylomeDBiQ61234.
TreeFamiTF317932.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR028552. SNTA1.
IPR015482. Syntrophin.
[Graphical view]
PANTHERiPTHR10554. PTHR10554. 1 hit.
PTHR10554:SF6. PTHR10554:SF6. 1 hit.
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61234-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGRRAPRT GLLELRCGAG SGAGGERWQR VLLSLAEDAL TVSPADGEPG
60 70 80 90 100
PEPEPAQLNG AAEPGAAPPQ LPEALLLQRR RVTVRKADAG GLGISIKGGR
110 120 130 140 150
ENKMPILISK IFKGLAADQT EALFVGDAIL SVNGEDLSSA THDEAVQALK
160 170 180 190 200
KTGKEVVLEV KYMKEVSPYF KNSAGGTSVG WDSPPASPLQ RQPSSPGPQP
210 220 230 240 250
RNLSEAKHVS LKMAYVSRRC TPTDPEPRYL EICAADGQDA VFLRAKDEAS
260 270 280 290 300
ARSWAGAIQA QIGTFIPWVK DELQALLTAT GTAGSQDIKQ IGWLTEQLPS
310 320 330 340 350
GGTAPTLALL TEKELLFYCS LPQSREALSR PTRTAPLIAT SSAHRLVHSG
360 370 380 390 400
PSKGSVPYDA ELSFALRTGT RHGVDTHLFS VESPQELAAW TRQLVDGCHR
410 420 430 440 450
AAEGIQEVST ACTWNGRPCS LSVHIDKGFT LWAAEPGAAR AMLLRQPFEK
460 470 480 490 500
LQMSSDDGTS LLFLDFGGAE GEIQLDLHSC PKTMVFIIHS FLSAKVTRLG

LLA
Length:503
Mass (Da):53,665
Last modified:November 1, 1996 - v1
Checksum:i161BA76CAF50AE96
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16R → C in AAH18546 (PubMed:15489334).Curated1
Sequence conflicti341 – 344Missing in AAH18546 (PubMed:15489334).Curated4
Sequence conflicti405I → V in AAH18546 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00677 mRNA. Translation: AAC52119.1.
BC018546 mRNA. Translation: AAH18546.1.
PIRiI84771.
UniGeneiMm.1541.

Genome annotation databases

EnsembliENSMUST00000028991; ENSMUSP00000028991; ENSMUSG00000027488.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00677 mRNA. Translation: AAC52119.1.
BC018546 mRNA. Translation: AAH18546.1.
PIRiI84771.
UniGeneiMm.1541.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ61234.
SMRiQ61234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-32898N.
IntActiQ61234. 6 interactors.
MINTiMINT-99385.
STRINGi10090.ENSMUSP00000105350.

PTM databases

iPTMnetiQ61234.
PhosphoSitePlusiQ61234.

Proteomic databases

MaxQBiQ61234.
PaxDbiQ61234.
PeptideAtlasiQ61234.
PRIDEiQ61234.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028991; ENSMUSP00000028991; ENSMUSG00000027488.

Organism-specific databases

MGIiMGI:101772. Snta1.

Phylogenomic databases

eggNOGiENOG410IMRM. Eukaryota.
ENOG410XS4Y. LUCA.
GeneTreeiENSGT00550000074581.
HOGENOMiHOG000231596.
HOVERGENiHBG054204.
InParanoidiQ61234.
OMAiKEMSAFF.
OrthoDBiEOG091G0O31.
PhylomeDBiQ61234.
TreeFamiTF317932.

Miscellaneous databases

EvolutionaryTraceiQ61234.
PROiQ61234.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027488.
CleanExiMM_SNTA1.
ExpressionAtlasiQ61234. baseline and differential.
GenevisibleiQ61234. MM.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR028552. SNTA1.
IPR015482. Syntrophin.
[Graphical view]
PANTHERiPTHR10554. PTHR10554. 1 hit.
PTHR10554:SF6. PTHR10554:SF6. 1 hit.
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSNTA1_MOUSE
AccessioniPrimary (citable) accession number: Q61234
Secondary accession number(s): Q8VEF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.