Vesicle-trafficking protein SEC22b (SEC22B)

The protein contains 215 amino acids for an estimated molecular weight of 24593 Da.

 

SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as 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. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. 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.
  4. 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.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. 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: 91%
Model score: 26
MODL_MODELLER-9.18
MODL_I-TASSER-3.0

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VariantDescription
dbSNP:rs2596331
dbSNP:rs2794053
dbSNP:rs2655551
dbSNP:rs2590131
dbSNP:rs2655557
dbSNP:rs7534444

The reference OMIM entry for this protein is 604029

Secretion deficient 22, s. cerevisiae, homolog-like 1; sec22l1
Sec22b

CLONING

Hay et al. (1997) isolated mouse Sec22b cDNAs and determined that the Sec22b protein is distinct from the previously identified rat SEC22A protein (612442). Sequence analysis revealed that mouse Sec22b is a cytoplasmically oriented, C-terminally anchored integral membrane protein. Mao et al. (1998) identified an umbilical cord blood CD34-positive cell cDNA encoding the human homolog of Sec22b. The predicted human protein contains 215 amino acids.

MAPPING

By analysis of radiation hybrids, Mao et al. (1998) mapped the human SEC22B gene to chromosome 1q21.2-q21.3.

GENE FUNCTION

In S. cerevisiae, the vesicle trafficking protein complexes directing transport between the endoplasmic reticulum (ER) and Golgi appear to include Sed5 (see syntaxin-5; 603189), proposed to be a cis-Golgi receptor protein, and Sec22 and Bet1 (605456), potential Sed5 docking partners localized on ER-derived vesicles. The Sly1 protein may bind to and regulate the activity of Sed5 for docking with ER-derived vesicle proteins. See membrin (GOSR2; 604027). Hay et al. (1997) isolated a rat liver protein complex representing an intermediate in ER-to-Golgi transfer reactions. The complex contained syntaxin-5, GOS28 (604026), the rat homologs of Bet1 and Sly1, and 2 novel proteins, rat SEC22B and membrin. By immunofluorescence of mammalian cells expressing epitope-tagged mouse Sec22b, Hay et al. (1997) found that Sec22b and membrin accumulated primarily at the ER. Other members of the complex localized to Golgi membranes, indicating that the complex recapitulates vesicle docking between distinct organelles in the ER/Golgi transport cycle. Expression of recombinant membrin and Sec22b disrupted normal trafficking, demonstrating that these proteins regulate ER-to-Golgi trafficking. 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, and Bet1 each are 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. ... 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

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 604029 was added.

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