Aliases for TNNT3 Gene
External Ids for TNNT3 Gene
Previous GeneCards Identifiers for TNNT3 Gene
The binding of Ca(2+) to the trimeric troponin complex initiates the process of muscle contraction. Increased Ca(2+) concentrations produce a conformational change in the troponin complex that is transmitted to tropomyosin dimers situated along actin filaments. The altered conformation permits increased interaction between a myosin head and an actin filament which, ultimately, produces a muscle contraction. The troponin complex has protein subunits C, I, and T. Subunit C binds Ca(2+) and subunit I binds to actin and inhibits actin-myosin interaction. Subunit T binds the troponin complex to the tropomyosin complex and is also required for Ca(2+)-mediated activation of actomyosin ATPase activity. There are 3 different troponin T genes that encode tissue-specific isoforms of subunit T for fast skeletal-, slow skeletal-, and cardiac-muscle. This gene encodes fast skeletal troponin T protein; also known as troponin T type 3. Alternative splicing results in multiple transcript variants encoding additional distinct troponin T type 3 isoforms. A developmentally regulated switch between fetal/neonatal and adult troponin T type 3 isoforms occurs. Additional splice variants have been described but their biological validity has not been established. Mutations in this gene may cause distal arthrogryposis multiplex congenita type 2B (DA2B). [provided by RefSeq, Oct 2009]
GeneCards Summary for TNNT3 Gene
TNNT3 (Troponin T Type 3 (Skeletal, Fast)) is a Protein Coding gene. Diseases associated with TNNT3 include tnnt3-related arthrogryposis multiplex congenita, distal, type 2b and arthrogryposis, distal, type 2b. Among its related pathways are Striated Muscle Contraction. GO annotations related to this gene include actin binding and tropomyosin binding. An important paralog of this gene is TNNT1.
UniProtKB/Swiss-Prot for TNNT3 Gene
Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity