Golgin subfamily A member 7 (GOLGA7)

The protein contains 137 amino acids for an estimated molecular weight of 15824 Da.

 

May be involved in protein transport from Golgi to cell surface. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS. (updated: Jan. 7, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. 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.
  3. 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.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. 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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 0%
Model score: 32

(right-click above to access to more options from the contextual menu)

No binding partner found

The reference OMIM entry for this protein is 609453

Golgi autoantigen, golgin subfamily a, 7; golga7
Golgi complex-associated protein, 16-kd; gcp16

CLONING

Using an N-terminal domain of GCP170 (GOLGA3; 602581) as bait in a yeast 2-hybrid screen of a HeLa cell cDNA library, Ohta et al. (2003) cloned GOLGA7, which they designated GCP16. The deduced 137-amino acid protein has a calculated molecular mass of 16 kD. GCP16 contains a short coiled-coil domain. Northern blot analysis detected a 2.0-kb transcript in all tissues examined, with abundant expression in testis, ovary, and spleen. A similarity search revealed GCP16 homologs in mouse, nematode, and fly, but not in yeast and plants. Immunoelectron microscopy detected GCP16 associated with the Golgi stack and related structures. SDS-PAGE detected endogenous GCP16 at an apparent molecular mass of 16 kD. By searching databases for homologs of S. pombe Erf4, Swarthout et al. (2005) identified GCP16. Northern blot analysis detected a 1.9-kb transcript in all human tissues examined except colon and thymus. Confocal microscopy of transfected human embryonic kidney cells showed colocalization of epitope-tagged GCP16 with DHHC9 (ZDHHC9; 300646) at the Golgi apparatus

GENE FUNCTION

By coimmunoprecipitation of HeLa cell extracts, Ohta et al. (2003) confirmed that native GCP16 and GCP170 interact. Overexpression of GCP16 in COS-1 cells inhibited protein transport from the Golgi to the cell surface. Swarthout et al. (2005) found that DHHC9 and GCP16 coimmunoprecipitated in transfected human embryonic kidney cells. Following expression in insect cells, the DHHC9/GCP16 complex showed protein acyltransferase activity, leading to incorporation of radioactive palmitate into both DHHC9 and an HRAS (190020) substrate. Both autoacylation of DHHC9 and palmitoylation of HRAS depended upon the presence of GCP16 in the complex, and no activity was observed when the conserved cys169 of the DHHC motif of DHHC9 was mutated to serine. The purified DHHC9/GCP16 complex also showed protein acyltransferase activity with an NRAS (164790) substrate, but not with substrates containing N-terminal palmitoylation motifs. DHHC9 appeared to require GCP16 for protein stability.

BIOCHEMICAL FEATURES

Despite the absence of a hydrophobic domain, Ohta et al. (2003) found that GCP16 behaved as an integral Golgi membrane protein following treatment with brefeldin A. Mutation analysis of GCP16 carrying radiolabeled palmitic acid indicated that GCP16 is acylated at cys69 and cys72, accounting for its tight association with the membrane. Mutant proteins lacking one or the other acylation site retained Golgi membrane targeting, but a mutant lacking both sites dispersed to the cytoplasm, indicating that the acylation anchors GCP16 to Golgi membranes.

MAPPING

The International Radiation Hybrid Mapping Consortium mapped the GOLGA7 gene to chromosome 8 (TMAP RH66402). ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 609453 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. 24, 2016: Protein entry updated
Automatic update: model status changed