MGP Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins
MGP000395

UniProt Annotations

Entry Information
Gene Namecaldesmon 1
Protein EntryCALD1_HUMAN
UniProt IDQ05682
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=6; Name=1; Synonyms=H-CAD; IsoId=Q05682-1; Sequence=Displayed; Name=2; Synonyms=WI-38 L-CAD I; IsoId=Q05682-2; Sequence=VSP_004155; Note=Contains a phosphoserine at position 202.; Name=3; Synonyms=HELA L-CAD I; IsoId=Q05682-3; Sequence=VSP_004154, VSP_004155; Note=Contains a phosphoserine at position 196. Contains a phosphoserine at position 12. Contains a phosphotyrosine at position 21.; Name=4; Synonyms=WI-38 L-CAD II, 1-CAD; IsoId=Q05682-4; Sequence=VSP_004156; Note=Contains a phosphoserine at position 202.; Name=5; Synonyms=HELA L-CAD II; IsoId=Q05682-5; Sequence=VSP_004154, VSP_004156; Note=Contains a phosphoserine at position 196. Contains a phosphoserine at position 12. Contains a phosphotyrosine at position 21.; Name=6; IsoId=Q05682-6; Sequence=VSP_004155, VSP_043292; Note=No experimental confirmation available. Contains a phosphoserine at position 202.;
DomainThe N-terminal part seems to be a myosin/calmodulin- binding domain, and the C-terminal a tropomyosin/actin/calmodulin- binding domain. These two domains are separated by a central helical region in the smooth-muscle form.
FunctionActin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). {ECO:0000250}.
PtmIn non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization. CDK1-mediated phosphorylation promotes Schwann cell migration during peripheral nerve regeneration (By similarity). {ECO:0000250}.
SimilarityBelongs to the caldesmon family. {ECO:0000305}.
Subcellular LocationCytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril {ECO:0000250}. Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle). {ECO:0000250}.
Tissue SpecificityHigh-molecular-weight caldesmon (isoform 1) is predominantly expressed in smooth muscles, whereas low-molecular- weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart.
  logo