Cald1
entrez
25687
canonical
uniprot
Q62736
canonical
ensembl
ENSRNOG00000010233
resolver
ensp
ENSRNOP00000043767
resolver
ensp
ENSRNOP00000085217
resolver
ensp
ENSRNOP00000087934
resolver
ensp
ENSRNOP00000093810
resolver
enst
ENSRNOT00000115634
resolver
genesymbol
Cald1
resolver
uniprot
A0A8I6GCL3
resolver
uniprot_entry
A0A8I6GCL3_RAT
resolver
uniprot_entry
CALD1_RAT
resolver
amino_acid_sequence
MLSRSGSQGRRCLATLSQIAYQRNDDDEEEAARERRRRARQERLRQKQEEESLGQVTDQVEAHVQNSAPDEESKPATANAQVEGDEEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSVPSRRMQNNSAENETAEGEEKGESRSGRYEMEETEVVITSYQKNSYQDAEDKKKEEKEEEEEEEKLKGGNLGENQIKDEKIKKDKEPKEEVKNFLDRKKGFTEVKAQNGEFMTHKLKQTENAFSPSRSGGRASGDKEAEGAPQVEAGKRLEELRRRRGETESEEFEKLKQKQQEAALELEELKKKREERRKVLEEEEQRRKQEEADRKAREEEEKRRLKEEIERRRAEAAEKRQKMPEDGLSEDKKPFKCFTPKGSSLKIEERAEFLNKSVQKSGVKSTHQAAVVSKIDSRLEQYTNAIEGTKASKPMKPAASDLPVPAEGVRNIKSMWEKGSVFSSPSASGTPNKETAGLKVGVSSRINEWLTKSPDGNKSPAPKPSDLRPGDVSGKRNLWEKQSVDKVTSPTKV
uniprot
proteins
function
FUNCTION: Actin- 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 plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration. {ECO:0000269|PubMed:17200138}.
uniprot
proteins
mass_dalton
60584
uniprot
proteins
mutagenesis
MUTAGEN 249; /note="S->A: Decreases strongly phosphorylation-dependent actin binding."; /evidence="ECO:0000269|PubMed:7876150"; MUTAGEN 462; /note="S->A: Decreases phosphorylation-dependent actin binding."; /evidence="ECO:0000269|PubMed:7876150"; MUTAGEN 468; /note="T->A: Decreases phosphorylation-dependent actin binding."; /evidence="ECO:0000269|PubMed:7876150"; MUTAGEN 491; /note="S->A: Decreases phosphorylation-dependent actin binding."; /evidence="ECO:0000269|PubMed:7876150"; MUTAGEN 497; /note="S->A: Decreases phosphorylation-dependent actin binding."; /evidence="ECO:0000269|PubMed:7876150"; MUTAGEN 527; /note="S->A: Does not decrease phosphorylation-dependent actin binding."; /evidence="ECO:0000269|PubMed:7876150
uniprot
proteins
post_translational_modification
PTM: In 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. {ECO:0000269|PubMed:17200138, ECO:0000269|PubMed:1986309, ECO:0000269|PubMed:7876150}.
uniprot
proteins
protein_family
Caldesmon family
uniprot
proteins
pubmed
17200138
uniprot
proteins
pubmed
1986309
uniprot
proteins
pubmed
7876150
uniprot
proteins
sequence_length
531
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P13505}. Cytoplasm, myofibril {ECO:0000250|UniProtKB:P13505}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:P13505}. Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle). {ECO:0000250|UniProtKB:P13505}.
uniprot
proteins