Syntrophin, alpha 1

Last updated
SNTA1
Protein SNTA1 PDB 1qav.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SNTA1 , LQT12, SNT1, TACIP1, dJ1187J4.5, Syntrophin, alpha 1, syntrophin alpha 1
External IDs OMIM: 601017 MGI: 101772 HomoloGene: 2331 GeneCards: SNTA1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003098

NM_009228

RefSeq (protein)

NP_003089

NP_033254

Location (UCSC) Chr 20: 33.41 – 33.44 Mb Chr 2: 154.22 – 154.25 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Alpha-1-syntrophin is a protein that in humans is encoded by the SNTA1 gene. [5] [6] [7] Alpha-1 syntrophin is a signal transducing adaptor protein and serves as a scaffold for various signaling molecules. Alpha-1 syntrophin contains a PDZ domain, two Pleckstrin homology domain and a 'syntrophin unique' domain.

Contents

Function

Dystrophin is a large, rod-like cytoskeletal protein found at the inner surface of muscle fibers. Dystrophin is missing in Duchenne Muscular Dystrophy patients and is present in reduced amounts in Becker Muscular Dystrophy patients. The protein encoded by this gene is a peripheral membrane protein found associated with dystrophin and dystrophin-related proteins. This gene is a member of the syntrophin gene family, which contains at least two other structurally related genes. [7] The PDZ domain of syntrophin-α1(SNTA1), the most abundant isoform in the heart, has been reported to bind to the C-terminal domain of murine cardiac voltage-gated sodium channels (SkM2) causing altering ion channel activity leading to Long QT syndrome. [8] [9]

Interactions

Syntrophin, alpha 1 has been shown to interact with Dystrophin, [5] [10] [11] Nav1.1 [11] and Nav1.5, [11] and Aquaporin 4. [12]

Related Research Articles

<span class="mw-page-title-main">Dystrophin</span> Rod-shaped cytoplasmic protein

Dystrophin is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. This complex is variously known as the costamere or the dystrophin-associated protein complex (DAPC). Many muscle proteins, such as α-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at the costamere. It has a molecular weight of 427 kDa

<span class="mw-page-title-main">Utrophin</span> Mammalian protein found in Homo sapiens

Utrophin is a protein that in humans is encoded by the UTRN gene. The name is a short form for ubiquitous dystrophin.

Dystrobrevin is a protein that binds to dystrophin in the costamere of skeletal muscle cells. In humans, there are at least two isoforms of dystrobrevin, dystrobrevin alpha and dystrobrevin beta.

<span class="mw-page-title-main">DLG4</span> Mammalian protein found in Homo sapiens

PSD-95 also known as SAP-90 is a protein that in humans is encoded by the DLG4 gene.

<span class="mw-page-title-main">DLG2</span> Protein-coding gene in the species Homo sapiens

Disks large homolog 2 (DLG2) also known as channel-associated protein of synapse-110 (chapsyn-110) or postsynaptic density protein 93 (PSD-93) is a protein that in humans is encoded by the DLG2 gene.

<span class="mw-page-title-main">Syntenin-1</span> Protein found in humans

Syntenin-1 is a protein that in humans is encoded by the SDCBP gene.

<span class="mw-page-title-main">Alpha-1B adrenergic receptor</span> Protein-coding gene in the species Homo sapiens

The alpha-1B adrenergic receptor1B-adrenoreceptor), also known as ADRA1B, is an alpha-1 adrenergic receptor, and also denotes the human gene encoding it. The crystal structure of the α1B-adrenergic receptor has been determined in complex with the inverse agonist (+)-cyclazosin.

<span class="mw-page-title-main">Alpha-actinin-1</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.

<span class="mw-page-title-main">Alpha-actinin-4</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.

<span class="mw-page-title-main">GIPC1</span> Protein-coding gene in the species Homo sapiens

GIPC PDZ domain containing family, member 1 (GIPC1) is a protein that in humans is encoded by the GIPC1 gene. GIPC was originally identified as it binds specifically to the C terminus of RGS-GAIP, a protein involved in the regulation of G protein signaling. GIPC is an acronym for "GAIP Interacting Protein C-terminus". RGS proteins are "Regulators of G protein Signaling" and RGS-GAIP is a "GTPase Activator protein for Gαi/Gαq", which are two major subtypes of Gα proteins. The human GIPC1 molecule is 333 amino acids or about 36 kDa in molecular size and consists of a central PDZ domain, a compact protein module which mediates specific protein-protein interactions. The RGS-GAIP protein interacts with this domain and many other proteins interact here or at other parts of the GIPC1 molecule. As a result, GIPC1 was independently discovered by several other groups and has a variety of alternate names, including synectin, C19orf3, RGS19IP1 and others. The GIPC1 gene family in mammals consisting of three members, so the first discovered, originally named GIPC, is now generally called GIPC1, with the other two being named GIPC2 and GIPC3. The three human proteins are about 60% identical in protein sequence. GIPC1 has been shown to interact with a variety of other receptor and cytoskeletal proteins including the GLUT1 receptor, ACTN1, KIF1B, MYO6, PLEKHG5, SDC4/syndecan-4, SEMA4C/semaphorin-4 and HTLV-I Tax. The general function of GIPC family proteins therefore appears to be mediating specific interactions between proteins involved in G protein signaling and membrane translocation.

<span class="mw-page-title-main">KCNJ4</span> Protein-coding gene in the species Homo sapiens

Potassium inwardly-rectifying channel, subfamily J, member 4, also known as KCNJ4 or Kir2.3, is a human gene.

<span class="mw-page-title-main">SNTB2</span> Protein-coding gene in the species Homo sapiens

Beta-2-syntrophin is a protein that in humans is encoded by the SNTB2 gene.

<span class="mw-page-title-main">SNTB1</span> Protein-coding gene in the species Homo sapiens

Beta-1-syntrophin is a protein that in humans is encoded by the SNTB1 gene.

<span class="mw-page-title-main">MAST2</span> Protein-coding gene in the species Homo sapiens

Microtubule-associated serine/threonine-protein kinase 2 is an enzyme that in humans is encoded by the MAST2 gene. The protein encoded by this gene controls TRAF6 and NF-kappaB activity.

<span class="mw-page-title-main">LIN7B</span> Protein-coding gene in humans

Lin-7 homolog B is a protein that in humans is encoded by the LIN7B gene.

<span class="mw-page-title-main">CRIPT</span> Protein-coding gene in the species Homo sapiens

Cysteine-rich PDZ-binding protein is a protein that in humans is encoded by the CRIPT gene.

<span class="mw-page-title-main">SNTG1</span> Protein-coding gene in the species Homo sapiens

Gamma-1-syntrophin is a protein that in humans is encoded by the SNTG1 gene.

<span class="mw-page-title-main">Dystrobrevin alpha</span> Protein found in humans

Dystrobrevin alpha is a protein that in humans is encoded by the DTNA gene.

<span class="mw-page-title-main">Dystrobrevin beta</span> Protein-coding gene in the species Homo sapiens

Dystrobrevin beta is a protein which in humans is encoded by the DTNB gene.

Stanley C. Froehner is an American physiologist and biophysicist currently the UW Medicine Distinguished Professor at University of Washington and an Elected Fellow of the American Association for the Advancement of Science.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000101400 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027488 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 Ahn AH, Freener CA, Gussoni E, Yoshida M, Ozawa E, Kunkel LM (Mar 1996). "The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives". J Biol Chem. 271 (5): 2724–30. doi: 10.1074/jbc.271.5.2724 . PMID   8576247.
  6. Castelló A, Brochériou V, Chafey P, Kahn A, Gilgenkrantz H (Jun 1996). "Characterization of the dystrophin-syntrophin interaction using the two-hybrid system in yeast". FEBS Lett. 383 (1–2): 124–8. doi: 10.1016/0014-5793(96)00214-1 . PMID   8612778. S2CID   27278535.
  7. 1 2 "Entrez Gene: SNTA1 syntrophin, alpha 1 (dystrophin-associated protein A1, 59kDa, acidic component)".
  8. Wu G, Ai T, Kim JJ, Mohapatra B, Xi Y, Li Z, Abbasi S, Purevjav E, Samani K, Ackerman MJ, Qi M, Moss AJ, Shimizu W, Towbin JA, Cheng J, Vatta M (Aug 2008). "Alpha-1-syntrophin mutation and the long-QT syndrome: a disease of sodium channel disruption". Circ Arrhythmia Electrophysiol. 1 (3): 193–201. doi:10.1161/CIRCEP.108.769224. PMC   2726717 . PMID   19684871.
  9. Hedley PL, Jørgensen P, Schlamowitz S, Wangari R, Moolman-Smook J, Brink PA, Kanters JK, Corfield VA, Christiansen M (2009). "The genetic basis of long QT and short QT syndromes: a mutation update". Human Mutation. 30 (11): 1486–511. doi: 10.1002/humu.21106 . PMID   19862833. S2CID   19122696.
  10. Yang B, Jung D, Rafael JA, Chamberlain JS, Campbell KP (Mar 1995). "Identification of alpha-syntrophin binding to syntrophin triplet, dystrophin, and utrophin". J. Biol. Chem. 270 (10): 4975–8. doi: 10.1074/jbc.270.10.4975 . PMID   7890602.
  11. 1 2 3 Gee SH, Madhavan R, Levinson SR, Caldwell JH, Sealock R, Froehner SC (Jan 1998). "Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins". J. Neurosci. 18 (1): 128–37. doi: 10.1523/jneurosci.18-01-00128.1998 . PMC   6793384 . PMID   9412493.
  12. Neely JD, Amiry-Moghaddam M, Ottersen OP, Froehner SC, Agre P, Adams ME (November 2001). "Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein". Proc. Natl. Acad. Sci. U.S.A. 98 (24): 14108–13. Bibcode:2001PNAS...9814108N. doi: 10.1073/pnas.241508198 . PMC   61176 . PMID   11717465.

Further reading