Transmembrane protein 165 (TMEM165)
The protein contains 324 amino acids for an estimated molecular weight of 34906 Da.
May function as a calcium/proton transporter involved in calcium and in lysosomal pH homeostasis. Therefore, it may play an indirect role in protein glycosylation. (updated: March 1, 2001)
Protein identification was indicated in the following studies:
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.
Biological Process
Calcium ion transmembrane transport
Cellular calcium ion homeostasis
Golgi calcium ion homeostasis
Golgi calcium ion transport
Manganese ion transmembrane transport
Protein N-linked glycosylation
Regulation of lysosomal lumen pH
The reference OMIM entry for this protein is 614726
Transmembrane protein 165; tmem165
Ft27
CLONING
Akagi et al. (1988) cloned mouse Tmem165, which they designated Ft27. The deduced 323-amino acid protein contains an N-terminal signal sequence and 6 predicted transmembrane domains. Northern blot analysis of undifferentiated F9 mouse teratocarcinoma cells detected a transcript of about 2.0 kb.GENE FUNCTION
Akagi et al. (1988) found that expression of mouse Tmem165 was rapidly downregulated in F9 cells upon 12-O-tetradecanoylphorbol-13-acetate (TPA)- or retinoic acid- and dibutyryl cAMP-induced differentiation. Foulquier et al. (2012) found that TMEM165 has a perinuclear Golgi-like distribution and is present mainly in the late Golgi region.MAPPING
Hartz (2012) mapped the TMEM165 gene to chromosome 4q12 based on an alignment of the TMEM165 sequence (GenBank GENBANK AF220188) with the genomic sequence (GRCh37).MOLECULAR GENETICS
In 5 patients from 4 families with congenital disorder of glycosylation type 2k (CDG2K; 614727), Foulquier et al. (2012) identified 4 homozygous or compound heterozygous mutations in the TMEM165 gene (614726.0001-614726.0004). The mutations were found by autozygosity mapping followed by gene expression profiling. The phenotype was variable, but all patients had psychomotor retardation and growth retardation, and most had short stature. Other features included dysmorphism, hypotonia, eye abnormalities, acquired microcephaly, hepatomegaly, and skeletal dysplasia. Serum transferrin analysis showed a CDG type II pattern, and patient cells showed an N-glycosylation defect and abnormal Golgi morphology. Silencing of the TMEM165 gene in HEK cells resulted in disturbed N-glycosylation in the terminal Golgi. The findings suggested an important role for TMEM165 in Golgi glycosylation and Golgi morphology maintenance. ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 614726 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).