Coatomer subunit zeta-1 (COPZ1)

The protein contains 177 amino acids for an estimated molecular weight of 20198 Da.

 

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity). (updated: Nov. 13, 2019)

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.

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: 86%
Model score: 23

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The reference OMIM entry for this protein is 615472

Coatomer protein complex, subunit zeta-1; copz1
Copz

DESCRIPTION

Intracellular cargo transport is mediated by vesicles decorated with protein complexes, such as coat protein complex I (COPI; see 601924). COPI consists of a 7-subunit coatomer subcomplex plus the small G protein ARF1 (103180). COPZ1 and COPZ2 (615526) are paralogous isoforms of the zeta subunit of the coatomer subcomplex (Moelleken et al., 2007).

CLONING

Zhang et al. (2000) cloned COPZ1, which they designated HSPC181, from CD34 (142230)-positive hematopoietic stem/progenitor cells. The deduced 177-amino acid protein contains a clathrin adaptor complex small chain (see 603531) signature. Low to moderate COPZ1 expression was present in all cell lines examined. Orthologs of COPZ1 were detected in mammals, bacteria, nematode, fly, and yeast, but not in plants. Using transfected rat hepatocytes, Futatsumori et al. (2000) found that epitope-tagged human zeta-1 COP colocalized with beta-COP (COPB; 600959) in the paranuclear region, characteristic of Golgi localization.

GENE FUNCTION

Kuge et al. (1993) found that antibodies directed against bovine zeta-COP blocked coatomer binding to Chinese hamster ovary Golgi membranes and prevented assembly of COP-coated vesicles on Golgi cisternae. They concluded that zeta-COP has a dual role in coat assembly in budding and in coupling fusion to budding. Using yeast 2-hybrid analysis, Futatsumori et al. (2000) showed that both human gamma-1 (COPG1; 615525) and gamma-2 COP (COPG2; 604355) interacted directly with both human zeta-1 and zeta-2 COP. None of the gamma or zeta subunits interacted with other COP subunits or with subunits of the AP1 clathrin adaptor complex (see 603531). By immunoprecipitation and immunoelectron microscopy of mouse and rat cells, Moelleken et al. (2007) found a preference for Copg1/Copz1- and Copg1/Copz2-containing coatomer complexes in the early Golgi apparatus and Copg2/Copz1-containing coatomer complexes in the late Golgi apparatus. They concluded that different coatomer isoforms may serve different intracellular transport routes.

MAPPING

Hartz (2013) mapped the COPZ1 gene to chromosome 12q13.13 based on an alignment of the COPZ1 sequence (GenBank GENBANK AF086911) with the genomic sequence (GRCh37). ... More on the omim web site

Subscribe to this protein entry history

Dec. 2, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.

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

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 615472 was added.

Jan. 27, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed