Secretory carrier-associated membrane protein 2 (SCAMP2)
The protein contains 329 amino acids for an estimated molecular weight of 36649 Da.
Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
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.
This protein is predicted to be membranous by TOPCONS.
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Cellular Component
Extracellular exosome
Golgi apparatus
Golgi membrane
Integral component of membrane
Intracellular membrane-bounded organelle
Nucleoplasm
Recycling endosome membrane
Trans-Golgi network membrane
Transport vesicle
Molecular Function
The reference OMIM entry for this protein is 606912
Secretory carrier membrane protein 2; scamp2
CLONING
Singleton et al. (1997) amplified SCAMP2 by PCR using primers designed from SCAMP1 (606911). They cloned the full-length SCAMP2 cDNA from a HeLa cell cDNA library. They also identified SCAMP3 (606913) as another paralog in the HeLa cell library. SCAMP2 encodes a deduced 329-amino acid protein with a calculated molecular mass of 36.6 kD. The protein shares structural features with SCAMP1 and SCAMP3, including a leucine zipper-like segment, a proline-rich element, an extended central core that includes 4 putative transmembrane domains, a polar segment, and an alanine-rich C terminus. SCAMP2 shares 54% and 56% overall sequence identity with SCAMP1 and SCAMP3, respectively, and 94% identity with the mouse homolog. The most divergent regions are in the N terminus. Northern blot analysis detected a 1.3-kb SCAMP2 transcript, with highest expression in heart, placenta, and skeletal muscle, intermediate expression in lung, pancreas, and liver, and low expression in brain and kidney. Immunofluorescent localization in HeLa cells showed punctate staining with some perinuclear and peripheral enrichment, and partial colocalization with SCAMP1 and SCAMP3.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SCAMP2 gene to chromosome 15 (TMAP sts-W74766). ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 606912 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