Secretory carrier-associated membrane protein 4 (SCAMP4)
The protein contains 229 amino acids for an estimated molecular weight of 25728 Da.
Probably involved in membrane protein trafficking. (updated: Jan. 7, 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.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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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| Variant | Description |
|---|---|
| dbSNP:rs45562539 |
No binding partner found
Cellular Component
Golgi apparatus
Golgi membrane
Integral component of membrane
Recycling endosome membrane
Trans-Golgi network membrane
Molecular Function
The reference OMIM entry for this protein is 613764
Secretory carrier membrane protein 4; scamp4
DESCRIPTION
Secretory carrier membrane proteins (SCAMPs) are widely distributed integral membrane proteins implicated in membrane trafficking. Most SCAMPs (e.g., SCAMP1; 606911) have N-terminal cytoplasmic NPF (arg-pro-phe) repeats, 4 central transmembrane regions, and a short C-terminal cytoplasmic tail. These SCAMPs likely have a role in endocytosis that is mediated by their NPF repeats. Other SCAMPs, such as SCAMP4, lack the NPF repeats and are therefore unlikely to function in endocytosis (summary by Fernandez-Chacon and Sudhof, 2000).CLONING
By searching EST databases, Fernandez-Chacon and Sudhof (2000) identified mouse Scamp4. The deduced 230-amino acid mouse protein contains 4 transmembrane domains that are highly conserved among other SCAMPs, with little conservation at the N- and C-terminal ends. Scamp4 lacks the N-terminal NPF repeats found in several other SCAMPs. Northern blot analysis revealed variable expression of Scamp4 in all rat tissues examined, with highest expression in testis and liver. Krebs and Pfaff (2001) cloned rat Scamp4. The deduced protein lacks the calcium-binding, leucine zipper, and NPF motifs found in other SCAMPs, but it has a putative protein kinase C (PKC; see 176960) phosphorylation site. In situ hybridization showed that Scamp4 mRNA was relatively low in female rat forebrain, with highest levels in ventromedial hypothalamus, habenula, and hippocampus.GENE FUNCTION
Using differential display PCR, Krebs and Pfaff (2001) found reduced expression of Scamp4 mRNA in the ventromedial hypothalamus of female rat brains after progesterone treatment, following estrogen priming. In situ hybridization showed that Scamp4 mRNA was less abundant in habenula and ventromedial hypothalamus during proestrus, when circulating levels of estrogen and progesterone are at their peak, than during diestrus-1, when circulating hormone levels are low. Krebs and Pfaff (2001) noted that Scamp4 mRNA levels are high in habenula, a brain area rich in mast cells that may be involved in courtship behavior. They suggested that SCAMP4 may be involved in reproductive behaviors associated with mast cell activity in the central nervous system.MAPPING
Gross (2011) mapped the SCAMP4 gene to chromosome 19p13.3 based on an alignment of the SCAMP4 sequence (GenBank GENBANK BC011747) with the genomic sequence (GRCh37). ... 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 613764 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