Myotilin

MYOT
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2KDG, 2KKQ
Identifiers
Aliases	MYOT, LGMD1, LGMD1A, MFM3, TTID, TTOD, myotilin
External IDs	MGI: 1889800 HomoloGene: 4942 GeneCards: MYOT
Gene location (Human) Chr. Chromosome 5 (human) Band 5q31.2 Start 137,867,791 bp End 137,887,851 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 B3 Start 44,334,074 bp End 44,355,724 bp
RNA expression pattern More reference expression data
Gene ontology Molecular function • actin binding • structural constituent of muscle • protein binding • alpha-actinin binding Cellular component • cytoplasm • sarcolemma • plasma membrane • Z disc • cytoskeleton • membrane • actin cytoskeleton Biological process • muscle contraction Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9499	58916
Ensembl	ENSG00000120729	ENSMUSG00000024471
UniProt	Q9UBF9	Q9JIF9
RefSeq (mRNA)	NM_006790 NM_001135940 NM_001300911	NM_001033621
RefSeq (protein)	NP_001129412 NP_001287840 NP_006781	NP_001028793
Location (UCSC)	Chr 5: 137.87 – 137.89 Mb	Chr 5: 44.33 – 44.36 Mb
PubMed search

2KDG, 2KKQ

9499

58916

ENSG00000120729

ENSMUSG00000024471

Q9UBF9

Q9JIF9

NM_006790
NM_001135940
NM_001300911

NM_001033621

NP_001129412
NP_001287840
NP_006781

NP_001028793

Myotilin is a protein that in humans is encoded by the MYOT gene. Myotilin (myofibrillar titin-like protein) also known as TTID (TiTin Immunoglobulin Domain) is a muscle protein that is found within the Z-disc of sarcomeres.

Myotilin is a 55.3 kDa protein composed of 496 amino acids. Myotilin was originally identified as a novel alpha-actinin binding partner with two Ig-like domains, that localized to the Z-disc. The C2-type Ig-like domains reside at the C-terminal half, and are most homologous to Ig domains 2-3 of palladin and Ig domains 4-5 of myopalladin and more distantly related to Z-disc Ig domains 7 and 8 of titin. The C-terminal region hosts the binding sites for Z-band proteins, and 2 Ig domains are the site of homodimerization for myotilin. By contrast, the N-terminal part of myotilin is unique, consisting of a serine-rich region with no homology to known proteins. Several disease-associated mutations involve serine residues within the serine-rich domain. Myotilin expression in human tissues is mainly restricted to striated muscles and nerves. In muscles, myotilin is predominantly found within the Z-discs. Myotilin forms homodimers and binds alpha-actinin, actin,Filamin C,FATZ-1,FATZ-2 and ZASP.

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