STX1A

Last updated
STX1A
Protein STX1A PDB 1br0.png
Identifiers
Aliases STX1A , HPC-1, P35-1, STX1, SYN1A, syntaxin 1A
External IDs OMIM: 186590 MGI: 109355 HomoloGene: 37941 GeneCards: STX1A
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001165903
NM_004603

NM_016801
NM_001359179

RefSeq (protein)

NP_001159375
NP_004594
NP_004594.1

NP_058081
NP_001346108

Location (UCSC) Chr 7: 73.7 – 73.72 Mb Chr 5: 135.05 – 135.08 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Syntaxin-1A is a protein that in humans is encoded by the STX1A gene. [5]

Contents

Function

Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process.

Syntaxin-1A is a member of the syntaxin superfamily. Syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. Syntaxins possess a single C-terminal transmembrane domain, a SNARE [Soluble NSF (N-ethylmaleimide-sensitive fusion protein)-Attachment protein REceptor] domain (known as H3), and an N-terminal regulatory domain (Habc). Syntaxins bind synaptotagmin in a calcium-dependent fashion and interact with voltage dependent calcium and potassium channels via the C-terminal H3 domain. Syntaxin-1A is a key protein in ion channel regulation and synaptic exocytosis. [6]

Clinical significance

Syntaxins serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces explosive exocytosis. [7]

The expression level of STX1A is directly correlated with intelligence in Williams syndrome. [8]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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Nicotine Activity on Dopaminergic Neurons edit
  1. The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602".

Interactions

STX1A has been shown to interact with:

See also

Related Research Articles

<i>N</i>-ethylmaleimide sensitive fusion protein Protein-coding gene in Homo sapiens

N-ethylmaleimide-sensitive factor, also known as NSF or N-ethylmaleimide sensitive fusion proteins, is an enzyme which in humans is encoded by the NSF gene.

<span class="mw-page-title-main">SNARE protein</span> Protein family

SNARE proteins – "SNAPREceptors" – are a large protein family consisting of at least 24 members in yeasts, more than 60 members in mammalian cells, and some numbers in plants. The primary role of SNARE proteins is to mediate the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments. The best studied SNAREs are those that mediate the release of synaptic vesicles containing neurotransmitters in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria.

<span class="mw-page-title-main">SNAP25</span> Protein-coding gene in the species Homo sapiens

Synaptosomal-Associated Protein, 25kDa (SNAP-25) is a Target Soluble NSF (N-ethylmaleimide-sensitive factor) Attachment Protein Receptor (t-SNARE) protein encoded by the SNAP25 gene found on chromosome 20p12.2 in humans. SNAP-25 is a component of the trans-SNARE complex, which accounts for membrane fusion specificity and directly executes fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together.

<span class="mw-page-title-main">Synaptotagmin</span>

Synaptotagmins (SYTs) constitute a family of membrane-trafficking proteins that are characterized by an N-terminal transmembrane region (TMR), a variable linker, and two C-terminal C2 domains - C2A and C2B. There are 17 isoforms in the mammalian synaptotagmin family. There are several C2-domain containing protein families that are related to synaptotagmins, including transmembrane (Ferlins, Extended-Synaptotagmin (E-Syt) membrane proteins, and MCTPs) and soluble (RIMS1 and RIMS2, UNC13D, synaptotagmin-related proteins and B/K) proteins. The family includes synaptotagmin 1, a Ca2+ sensor in the membrane of the pre-synaptic axon terminal, coded by gene SYT1.

<span class="mw-page-title-main">SNAP23</span> Protein-coding gene in the species Homo sapiens

Synaptosomal-associated protein 23 is a protein that in humans is encoded by the SNAP23 gene. Two alternative transcript variants encoding different protein isoforms have been described for this gene.

<span class="mw-page-title-main">STX4</span> Protein-coding gene in the species Homo sapiens

Syntaxin-4 is a protein that in humans is encoded by the STX4 gene.

<span class="mw-page-title-main">SYT1</span> Protein-coding gene in the species Homo sapiens

Synaptotagmin-1 is a protein that in humans is encoded by the SYT1 gene.

<span class="mw-page-title-main">VAMP2</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 2 (VAMP2) is a protein that in humans is encoded by the VAMP2 gene.

<span class="mw-page-title-main">STXBP1</span> Protein-coding gene in the species Homo sapiens

Syntaxin-binding protein 1 is a protein that in humans is encoded by the STXBP1 gene. This gene encodes a syntaxin-binding protein. The encoded protein appears to play a role in release of neurotransmitters via regulation of syntaxin, a transmembrane attachment protein receptor. Mutations in this gene have been associated with neurological disorders including epilepsy, intellectual disability, and movement disorders.

<span class="mw-page-title-main">STX6</span> Protein-coding gene in the species Homo sapiens

Syntaxin-6 is a protein that in humans is encoded by the STX6 gene.

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

N-ethylmaleimide-sensitive factor Attachment Protein Alpha, also known as SNAP-α, is a SNAP protein that is involved in the intra-cellular trafficking and fusing of vesicles to target membranes in cells.

<span class="mw-page-title-main">VAMP3</span> Protein-coding gene in the species Homo sapiens

Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.

<span class="mw-page-title-main">STX5</span> Protein-coding gene in the species Homo sapiens

Syntaxin-5 is a protein that in humans is encoded by the STX5 gene.

<span class="mw-page-title-main">STX2</span> Protein-coding gene in the species Homo sapiens

Syntaxin-2, also known as epimorphin, is a protein that in humans is encoded by the STX2 gene.

<span class="mw-page-title-main">Syntaxin binding protein 2</span> Protein-coding gene in the species Homo sapiens

Syntaxin-binding protein 2 is a protein that in humans is encoded by the STXBP2 gene.

<span class="mw-page-title-main">DNAJC5</span> Protein-coding gene in the species Homo sapiens

DnaJ homolog subfamily C member 5, also known as cysteine string protein or CSP is a protein, that in humans encoded by the DNAJC5 gene. It was first described in 1990.

<span class="mw-page-title-main">CPLX1</span> Protein-coding gene in humans

Complexin-1 is a protein that in humans is encoded by the CPLX1 gene.

<span class="mw-page-title-main">Syntaxin 3</span> Protein-coding gene in the species Homo sapiens

Syntaxin 3, also known as STX3, is a protein which in humans is encoded by the STX3 gene.

<span class="mw-page-title-main">Syntaxin</span> Group of proteins

Syntaxins are a family of membrane integrated Q-SNARE proteins participating in exocytosis.

Munc-18 proteins are the mammalian homologue of UNC-18 and are a member of the Sec1/Munc18-like (SM) protein family. Munc-18 proteins have been identified as essential components of the synaptic vesicle fusion protein complex and are crucial for the regulated exocytosis of neurons and neuroendocrine cells.

References

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Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.