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Q61234

- SNTA1_MOUSE

UniProt

Q61234 - SNTA1_MOUSE

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Protein

Alpha-1-syntrophin

Gene

Snta1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. ion channel binding Source: BHF-UCL
  2. sodium channel regulator activity Source: Ensembl

GO - Biological processi

  1. negative regulation of peptidyl-cysteine S-nitrosylation Source: Ensembl
  2. neuromuscular junction development Source: MGI
  3. regulation of heart rate Source: Ensembl
  4. regulation of sodium ion transmembrane transport Source: Ensembl
  5. regulation of vasoconstriction by circulating norepinephrine Source: MGI
  6. regulation of ventricular cardiac muscle cell membrane repolarization Source: Ensembl
  7. ventricular cardiac muscle cell action potential Source: Ensembl
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
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:101772. Snta1.

Subcellular locationi

Cell membranesarcolemma 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell junction 1 Publication. Cytoplasmcytoskeleton 1 Publication
Note: In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. neuromuscular junction Source: Ensembl
  5. postsynaptic membrane Source: MGI
  6. protein complex Source: MGI
  7. sarcolemma Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Alpha-1-syntrophinPRO_0000184007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831Phosphoserine1 Publication
Modified residuei187 – 1871Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the interaction with DMD.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ61234.
PaxDbiQ61234.
PRIDEiQ61234.

PTM databases

PhosphoSiteiQ61234.

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

BgeeiQ61234.
CleanExiMM_SNTA1.
ExpressionAtlasiQ61234. baseline and differential.
GenevestigatoriQ61234.

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

Protein-protein interaction databases

DIPiDIP-32898N.
IntActiQ61234. 5 interactions.
MINTiMINT-99385.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 168Combined sources
Beta strandi20 – 245Combined sources
Beta strandi28 – 358Combined sources
Beta strandi37 – 437Combined sources
Beta strandi63 – 675Combined sources
Turni75 – 773Combined sources
Beta strandi80 – 856Combined sources
Turni88 – 903Combined sources
Beta strandi94 – 996Combined sources
Helixi100 – 1023Combined sources
Beta strandi104 – 1118Combined sources
Beta strandi113 – 1153Combined sources
Helixi116 – 1194Combined sources
Beta strandi127 – 1326Combined sources
Helixi137 – 1393Combined sources
Helixi142 – 1509Combined sources
Beta strandi154 – 1629Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi207 – 21913Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi229 – 2346Combined sources
Turni235 – 2384Combined sources
Beta strandi239 – 2446Combined sources
Helixi248 – 26215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-264.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61234.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 263258PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini81 – 16484PDZPROSITE-ProRule annotationAdd
BLAST
Domaini287 – 399113PH 2PROSITE-ProRule annotationAdd
BLAST
Domaini447 – 50357SUAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni481 – 50323Calmodulin-bindingAdd
BLAST

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

eggNOGiNOG318350.
GeneTreeiENSGT00550000074581.
HOGENOMiHOG000231596.
HOVERGENiHBG054204.
InParanoidiQ61234.
OMAiTGTRHGV.
PhylomeDBiQ61234.
TreeFamiTF317932.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001849. PH_domain.
IPR028552. SNTA1.
IPR015482. Syntrophin.
[Graphical view]
PANTHERiPTHR10554. PTHR10554. 1 hit.
PTHR10554:SF6. PTHR10554:SF6. 1 hit.
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161R → C in AAH18546. (PubMed:15489334)Curated
Sequence conflicti341 – 3444Missing in AAH18546. (PubMed:15489334)Curated
Sequence conflicti405 – 4051I → V in AAH18546. (PubMed:15489334)Curated

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 .
PIRi I84771.
UniGenei Mm.1541.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
4HOP X-ray 2.29 A/C/E 77-162 [» ]
ProteinModelPortali Q61234.
SMRi Q61234. Positions 2-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-32898N.
IntActi Q61234. 5 interactions.
MINTi MINT-99385.

PTM databases

PhosphoSitei Q61234.

Proteomic databases

MaxQBi Q61234.
PaxDbi Q61234.
PRIDEi Q61234.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028991 ; ENSMUSP00000028991 ; ENSMUSG00000027488 .

Organism-specific databases

MGIi MGI:101772. Snta1.

Phylogenomic databases

eggNOGi NOG318350.
GeneTreei ENSGT00550000074581.
HOGENOMi HOG000231596.
HOVERGENi HBG054204.
InParanoidi Q61234.
OMAi TGTRHGV.
PhylomeDBi Q61234.
TreeFami TF317932.

Miscellaneous databases

EvolutionaryTracei Q61234.
PROi Q61234.
SOURCEi Search...

Gene expression databases

Bgeei Q61234.
CleanExi MM_SNTA1.
ExpressionAtlasi Q61234. baseline and differential.
Genevestigatori Q61234.

Family and domain databases

Gene3Di 2.30.42.10. 1 hit.
InterProi IPR001478. PDZ.
IPR001849. PH_domain.
IPR028552. SNTA1.
IPR015482. Syntrophin.
[Graphical view ]
PANTHERi PTHR10554. PTHR10554. 1 hit.
PTHR10554:SF6. PTHR10554:SF6. 1 hit.
Pfami PF00595. PDZ. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
PROSITEi PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

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 26, 2014
This is version 136 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

External Data

Dasty 3