Myozenin-1 (MYOZ1)
The protein contains 299 amino acids for an estimated molecular weight of 31745 Da.
Myozenins may serve as intracellular binding proteins involved in linking Z-disk proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis. (updated: Sept. 12, 2018)
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.
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No binding partner found
Biological Process
Myofibril assembly
Negative regulation of calcineurin-NFAT signaling cascade
Negative regulation of skeletal muscle tissue regeneration
Negative regulation of transcription by RNA polymerase II
Sarcomere organization
Skeletal muscle fiber adaptation
Skeletal muscle tissue development
Wound healing
The reference OMIM entry for this protein is 605603
Myozenin 1; myoz1
Calsarcin 2
CLONING
To identify potential cardiac-specific regulators of calcineurin (see 114105), Frey et al. (2000) conducted a yeast 2-hybrid screen, using the catalytic A subunit of calcineurin as bait. They identified a novel family of striated muscle-specific calcineurin-interacting proteins called calsarcins. Calsarcins interact and colocalize with the Z disc protein alpha-actinin (ACTN1; 102575) in vitro and in vivo and thereby tether calcineurin to the sarcomere of cardiac and skeletal muscle. These properties of calsarcins suggest an important role for these proteins in modulating the function and substrate specificity of calcineurin in striated muscle cells. Frey et al. (2000) cloned and characterized the cDNA of calsarcin-1 (MYOZ2; 605602) and calsarcin-2. Calsarcin-2 encodes a 299-amino acid protein, which shows the highest sequence homology with calsarcin-1 in the N and C termini. Northern blot analysis of human tissues revealed a highly striated muscle-specific expression pattern of both genes. Calsarcins 1 and 2 are expressed in developing cardiac and skeletal muscle during embryogenesis, but calsarcin-1 is expressed specifically in adult cardiac and slow-twitch skeletal muscle as 1.6- and 2.6-kb transcripts, whereas calsarcin-2 is expressed only in adult fast skeletal muscle as a 1.6-kb transcript. By searching a muscle-specific EST database and screening a full-length muscle cDNA library, Faulkner et al. (2000) also cloned MYOZ, which they termed FATZ for FLNC (102565)/ACTN2 (102573)/TCAP (604488)-binding protein of the Z disc. MYOZ shares 90% amino acid identity with the mouse protein and contains a nuclear localization signal as well as 11 potential phosphorylation sites. Northern blot and RT-PCR analysis revealed expression of a 1.5-kb transcript only in skeletal muscle, with weaker signals in heart, prostate, and pancreas. Western blot and immunofluorescence microscopy analysis showed expression of a 34-kD protein mainly in differentiated muscle cells. Immunofluorescence and immunogold electron microscopy demonstrated localization in the Z disc.GENE FUNCTION
By GST pull-down and yeast 2-hybrid analysis, Faulkner et al. (2000) confirmed the interaction of MYOZ with FLNC, ACTN2, and TCAP. Based on its binding partners, the authors suggested a central role for FATZ in myofibrillogenesis. Using the yeast 2-hybrid system, Takada et al. (2001) used sarcomeric isoforms of alpha-actinin and gamma-filamin to screen a human skeletal muscle cDNA library for interacting proteins. The aim was to understand better the structure and function of Z lines. They described the characteristics of myozenin. It is predicted to be a 32-kD globular protein with a central glycine-rich domain flanked by alpha-helical regions with no strong homologies to any known genes. Takada et al. (2001) considered myozenin as a skeletal muscle Z line protein to be a candidate gene for limb-girdle muscular dystrophy or other neuromuscular disorders. By yeast 2-hybrid analysis, Frey and Olson (2002) showed that ZASP (LDB3; 605906) interacted strongly with MYOZ1, MYOZ2, and MYOZ3 (610735). Coimmunoprecipitation studies in COS-7 cells showed that both the longest and shortest ZASP splice variants bind all 3 members of the myozenin family, suggesting that the interaction is not isoform specific.GENE STRUCTURE
The MYOZ gene has 6 exons (Takada et al., 2001).MAPPING
By radiation hybrid analysis, Faulkner et al. (2000) mapped t ... More on the omim web site
Nov. 17, 2018: Protein entry updated
Automatic update: OMIM entry 605603 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).