Syntaxin-5 (STX5)

The protein contains 355 amino acids for an estimated molecular weight of 39673 Da.

 

Mediates endoplasmic reticulum to Golgi transport. Together with p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  2. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is predicted to be membranous by TOPCONS.


Interpro domains
Total structural coverage: 19%
Model score: 44

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VariantDescription
dbSNP:rs3802945
dbSNP:rs11231241
a breast cancer sample; somatic mutation
De novo variant found in a patient with childhood apraxia of speech

The reference OMIM entry for this protein is 603189

Syntaxin 5; stx5
Stx5a
Sed5

CLONING

In eukaryotic cells, vesicle docking is thought to be regulated in part by the specific interactions of a vesicle-associated membrane protein (VAMP), or synaptobrevin (e.g., 185880), with the presynaptic plasma membrane proteins syntaxin and SNAP25 (600322). By PCR using oligonucleotides based on the sequence of rat syntaxin-5, Ravichandran and Roche (1997) isolated a partial cDNA encoding human syntaxin-5. They used the partial cDNA to clone a full-length human syntaxin-5 cDNA from an EBV-transformed lymphocyte cell cDNA library. The predicted 301-amino acid human protein is 96% identical to rat syntaxin-5. In vitro, human syntaxin-5 bound efficiently to rat VAMP2 (see SYB2; 185881) but not to human SNAP25.

GENE FUNCTION

To fuse transport vesicles with target membranes, proteins of the SNARE complex must be located on both the vesicle and the target membrane. In yeast, 4 integral membrane proteins, Sed5, Bos1, Sec22 (see 604029), and Bet1 (605456), are each believed to contribute a single helix to form the SNARE complex that is needed for transport from endoplasmic reticulum to Golgi. This generates a 4-helix bundle, which ultimately mediates the actual fusion event. Parlati et al. (2000) explored how the anchoring arrangement of the 4 helices affects their ability to mediate fusion. Parlati et al. (2000) reconstituted 2 populations of phospholipid bilayer vesicles, with the individual SNARE proteins distributed in all possible combinations between them. Of the 8 nonredundant permutations of 4 subunits distributed over 2 vesicle populations, only 1 resulted in membrane fusion. Fusion occurred only when the v-SNARE Bet1 is on 1 membrane and the syntaxin heavy chain Sed5 and its 2 light chains, Bos1 and Sec22, are on the other membrane, where they form a functional t-SNARE. Thus, each SNARE protein is topologically restricted by design to function either as a v-SNARE or as part of a t-SNARE complex.

MAPPING

Gross (2014) mapped the STX5 gene to chromosome 11q12.3 based on an alignment of the STX5 sequence (GenBank GENBANK BC002645) with the genomic sequence (GRCh37). ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 603189 was added.

Dec. 10, 2018: Protein entry updated
Automatic update: model status changed

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).