Vesicle transport through interaction with t-SNAREs homolog 1B (VTI1B)

The protein contains 232 amino acids for an estimated molecular weight of 26688 Da.

 

V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. May be concerned with increased secretion of cytokines associated with cellular senescence. (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.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is predicted to be membranous by TOPCONS.

Topcons

Interpro domains
Total structural coverage: 46%
Model score: 24
MODL_I-TASSER-3.0
MODL_I-TASSER-3.0

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The reference OMIM entry for this protein is 603207

Vti1, s. cerevisiae, homolog of, b; vti1b
Vti1
Vti1-like; vti1l

CLONING

Membrane traffic in eukaryotic cells requires the interaction of a vesicle-associated soluble NSF attachment protein receptor (v-SNARE) on transport vesicles with a t-SNARE on the target membrane. See 603215. Vti1 is an S. cerevisiae v-SNARE that is essential for viability. Vti1 participates both in Golgi to prevacuolar transport and in traffic to the cis-Golgi. Using a multicopy suppressor screen to identity human proteins that can functionally complement a yeast vti1 deletion mutant, Fischer von Mollard and Stevens (1998) isolated a glioblastoma cDNA encoding VTI1, a human homolog of yeast Vti1. The deduced 232-amino acid human protein contains a C-terminal transmembrane domain and 2 predicted coiled-coil regions. The yeast and human proteins are 29% identical. Expression of human VTI1 in yeast indicated that VTI1 can replace yeast Vti1 in both Golgi transport reactions. Northern blot analysis detected a 1.2-kb VTI1 mRNA in all human tissues tested. Searches of an EST database identified cDNAs encoding a mouse protein with 93% sequence identity to human VTI1.

BIOCHEMICAL FEATURES

- Crystal Structure Miller et al. (2007) characterized the molecular details governing the sorting of a SNARE into clathrin-coated vesicles, namely, the direct recognition of the 3-helical bundle H(abc) domain of the mouse SNARE Vti1b by the human clathrin adaptor epsinR (EPNR, also known as CLINT1; 607265). Structures of each domain and of their complex showed that this interaction (dissociation constant 22 microM) is mediated by surface patches composed of approximately 15 residues each, the topographies of which are dependent on each domain's overall fold. Disruption of the interface with point mutations abolished the interaction in vitro and caused Vti1b to become relocalized to late endosomes and lysosomes. Miller et al. (2007) stated that this new class of highly specific, surface-surface interaction between the clathrin coat component and the cargo is distinct from the widely observed binding of short, linear cargo motifs by the assembly polypeptide (AP) complex and GGA adaptors and is therefore not vulnerable to competition from standard motif-containing cargoes for incorporation into clathrin-coated vesicles. Miller et al. (2007) proposed that conceptually similar but mechanistically different interactions direct the post-Golgi trafficking of many SNAREs. ... 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 603207 was added.

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