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Q61234

- SNTA1_MOUSE

UniProt

Q61234 - SNTA1_MOUSE

Protein

Alpha-1-syntrophin

Gene

Snta1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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. protein binding Source: UniProtKB

    GO - Biological processi

    1. neuromuscular junction development Source: MGI
    2. regulation of vasoconstriction by circulating norepinephrine Source: MGI

    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-SubCell
    2. cytoplasm Source: UniProtKB-KW
    3. cytoskeleton Source: UniProtKB-SubCell
    4. postsynaptic membrane Source: MGI
    5. protein complex Source: MGI
    6. sarcolemma Source: MGI

    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 – 1831Phosphoserine2 Publications
    Modified residuei187 – 1871Phosphoserine2 Publications

    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

    ArrayExpressiQ61234.
    BgeeiQ61234.
    CleanExiMM_SNTA1.
    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

    Protein-protein interaction databases

    DIPiDIP-32898N.
    IntActiQ61234. 4 interactions.
    MINTiMINT-99385.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MASGRRAPRT GLLELRCGAG SGAGGERWQR VLLSLAEDAL TVSPADGEPG    50
    PEPEPAQLNG AAEPGAAPPQ LPEALLLQRR RVTVRKADAG GLGISIKGGR 100
    ENKMPILISK IFKGLAADQT EALFVGDAIL SVNGEDLSSA THDEAVQALK 150
    KTGKEVVLEV KYMKEVSPYF KNSAGGTSVG WDSPPASPLQ RQPSSPGPQP 200
    RNLSEAKHVS LKMAYVSRRC TPTDPEPRYL EICAADGQDA VFLRAKDEAS 250
    ARSWAGAIQA QIGTFIPWVK DELQALLTAT GTAGSQDIKQ IGWLTEQLPS 300
    GGTAPTLALL TEKELLFYCS LPQSREALSR PTRTAPLIAT SSAHRLVHSG 350
    PSKGSVPYDA ELSFALRTGT RHGVDTHLFS VESPQELAAW TRQLVDGCHR 400
    AAEGIQEVST ACTWNGRPCS LSVHIDKGFT LWAAEPGAAR AMLLRQPFEK 450
    LQMSSDDGTS LLFLDFGGAE GEIQLDLHSC PKTMVFIIHS FLSAKVTRLG 500
    LLA 503
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00677 mRNA. Translation: AAC52119.1 .
    BC018546 mRNA. Translation: AAH18546.1 .
    PIRi I84771.
    UniGenei Mm.1541.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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. 4 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

    ArrayExpressi Q61234.
    Bgeei Q61234.
    CleanExi MM_SNTA1.
    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

    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: October 1, 2014
    This is version 134 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