VIP36-like protein (LMAN2L)
The protein contains 348 amino acids for an estimated molecular weight of 39711 Da.
May be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. May function as a regulator of ERGIC-53. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- 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.
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 |
|---|---|
| MRT52 |
No binding partner found
Biological Process
Endoplasmic reticulum organization
Endoplasmic reticulum to Golgi vesicle-mediated transport
Golgi organization
Protein folding
Protein transport
The reference OMIM entry for this protein is 609552
Lman2-like protein; lman2l
Vip36-like protein; vipl
CLONING
Nufer et al. (2003) and Neve et al. (2003) independently cloned LMAN2L, which they both called VIPL, by searching databases using sequences conserved in L-type lectins, followed by screening liver carcinoma cell line and fetal brain cDNA libraries, respectively. The deduced 348-amino acid protein contains an N-terminal signal peptide, followed by a lectin-type carbohydrate recognition domain (CARD), a transmembrane domain, and a C-terminal endoplasmic reticulum (ER) retrieval motif. The CRD has conserved cysteines and key residues required for Ca(2+) and sugar binding, as well as an N-glycosylation site. VIPL shares 35% and 58% amino acid identity with ERGIC53 (LMAN1; 601567) and VIP36 (LMAN2; 609551), respectively, with highest identity in the CARDs. EST database analysis by Nufer et al. (2003) suggested that VIPL is ubiquitously expressed. VIPL distributed with the membrane pellet of fractionated transfected human embryonic kidney cells. Confocal immunofluorescence microscopy localized VIPL to the ER of HepG2 and all other human cell lines examined. Endoglycosidase treatment indicated that the N-glycan of VIPL is a high-mannose-type carbohydrate. By Northern blot analysis, Neve et al. (2003) detected a 2.4-kb VIPL transcript in all tissues examined. Expression was highest in skeletal muscle and kidney, intermediate in heart, liver, and placenta, low in brain, thymus, spleen, small intestine, and lung, and very low in colon and peripheral blood lymphocytes. Immunofluorescent microscopy found weak VIPL staining in all cell lines examined. VIPL was expressed in a reticular pattern, including staining of the nuclear rim, suggesting localization to the ER.GENE FUNCTION
Nufer et al. (2003) found that overexpression of VIPL in HepG2 cells led to the redistribution of ERGIC53 from a concentration near the Golgi to the ER. The morphology of the general secretory pathway was unaffected by VIPL overexpression, and mutation analysis indicated that the lectin domain was not required for ERGIC53 redistribution. Retention of VIPL in the ER required a C-terminal RKR motif, and the RKR motif of VIPL was required to redistribute ERGIC53. VIPL lacking the RKR motif localized to the plasma membrane, and its distribution did not overlap with that of ERGIC53. Neve et al. (2003) also found that ERGIC53 redistributed from the perinuclear Golgi to the ER when VIPL was overexpressed in baby hamster kidney cells, and that mutation of the VIPL ER retrieval signal resulted in transport of VIPL to the cell surface. Neve et al. (2003) found that knockdown of VIPL expression in HeLa cells with small interfering RNA resulted in reduced secretion of a select group of proteins, while the overall pattern of protein secretion was unaffected.GENE STRUCTURE
Nufer et al. (2003) determined that the LMAN2L gene contains 8 exons and spans 34.14 kb.MAPPING
By genomic sequence analysis, Nufer et al. (2003) mapped the LMAN2L gene to chromosome 2q11.2. ... More on the omim web site
July 1, 2020: Protein entry updated
Automatic update: OMIM entry 609552 was added.
Feb. 23, 2019: Protein entry updated
Automatic update: comparative model was added.
Feb. 23, 2019: Protein entry updated
Automatic update: model status changed
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).