Vesicle transport protein USE1 (USE1)

The protein contains 259 amino acids for an estimated molecular weight of 29371 Da.

 

SNARE that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. (updated: March 4, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

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 annotated as membranous in Gene Ontology, is predicted to be membranous by TOPCONS.


Interpro domains
Total structural coverage: 22%
Model score: 45

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VariantDescription
dbSNP:rs414528

The reference OMIM entry for this protein is 610675

Hematopoietic stem/progenitor cell protein mds032
Mds032

CLONING

Using fluorescence localization-based, retrovirus-mediated expression cloning with a signal sequence trap, Okumura et al. (2006) identified a mouse clone, D12, with expression in endoplasmic reticulum (ER) and cytoplasm. The authors subsequently isolated full-length D12 from a mouse bone marrow mast cell cDNA library, and noted that EST sequence variants of D12 exist, some containing a CAG insertion encoding an additional ser residue. D12 contains 2 predicted coiled-coil domains, a C-terminal transmembrane domain, a region weakly similar to the syntaxin N-terminal domain, and a region weakly similar to the t-SNARE motif. D12 shows weak homology to yeast Use1p/Slt1p, and 84.9% identity to the human protein MDS032. MDS032 does not contain the first 11 amino acids of D12, and shows lower homology within an internal region (D12 residues 139-164). Fluorescence analysis and cell fractionation assays showed that D12 localizes to the ER and to ER-Golgi intermediate compartments.

GENE FUNCTION

Using immunoprecipitation assays, Okumura et al. (2006) showed that D12 is a SNARE protein that binds to syntaxin-18 (606046), Sec22b (604029), alpha-SNAP (603215), and VAMP7, thus showing that D12 interacts with SNARES involved in the early and the post-Golgi secretory apparatus and with endosome-lysosome transport. Immunofluorescence and siRNA assays showed that neither overexpression nor knockdown of D12 affected ER, Golgi, or ER-Golgi intermediate compartment structures, suggesting that D12 does not regulate membrane trafficking in the early secretory pathway. However, D12 knockdown did induce apoptosis, as measured by condensed nuclear chromatin, caspase-3 (600636) activation, and BAX (600040) conformational change. In addition, D12 downregulation caused rapid appearance of lipofuscin granules, suggesting impaired degradation of mitochondria by lysosomal degradative enzymes. Consistent with this, confocal microscopy and fractionation of D12-deficient cells showed impaired post-Golgi trafficking and maturation of the lysosomal proteinase cathepsin-D (116840). ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 610675 was added.

Feb. 25, 2016: Protein entry updated
Automatic update: model status changed

Feb. 24, 2016: Protein entry updated
Automatic update: model status changed

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed