Vitamin K epoxide reductase complex subunit 1-like protein 1 (VKORC1L1)
The protein contains 176 amino acids for an estimated molecular weight of 19836 Da.
Involved in vitamin K metabolism. Can reduce inactive vitamin K 2,3-epoxide to active vitamin K (in vitro), and may contribute to vitamin K-mediated protection against oxidative stress. Plays a role in vitamin K-dependent gamma-carboxylation of Glu residues in target proteins. (updated: Oct. 10, 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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No binding partner found
Biological Process
Cellular response to oxidative stress
Peptidyl-glutamic acid carboxylation
Vitamin K metabolic process
Cellular Component
Endoplasmic reticulum
Endoplasmic reticulum membrane
Integral component of membrane
The reference OMIM entry for this protein is 608838
Vitamin k epoxide reductase complex, subunit 1-like 1; vkorc1l1
CLONING
By database searching with the sequence of VKORC1 (608547) as query, Rost et al. (2004) identified VKORC1L1. The deduced 176-amino acid protein shares 50% identity with VKORC1 and approximately 97% identity with mouse and rat Vkorc1l1. Rost et al. (2004) also identified a VKORC1L1 pseudogene.GENE FUNCTION
Vitamin K is required for the gamma-carboxylation of glutamate residues in several vitamin K-dependent proteins, usually within Gla domains. These proteins are involved in blood coagulation, bone metabolism, and other functions. Vitamin K is regenerated through the vitamin K 2,3-epoxide reductase (VKOR) activity of VKORC1 (608547). Hammed et al. (2013) showed that a related gene, VKORC1L1, has similar activity but is 50-fold less sensitive to vitamin K antagonists such as warfarin. In mice, VKORC1L1 was expressed in all tissues studied. Hammed et al. (2013) argued that the expression of VKORC1L1 in extrahepatic tissues explains VKOR activity outside of the liver and why these tissues are not affected by VKOR antagonists. ... More on the omim web site
July 1, 2020: Protein entry updated
Automatic update: OMIM entry 608838 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).