Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Non-muscle caldesmon

Gene

Cald1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration.1 Publication

GO - Molecular functioni

  • actin binding Source: RGD

GO - Biological processi

  • actin filament bundle assembly Source: RGD
  • female pregnancy Source: RGD
  • muscle contraction Source: InterPro
  • positive regulation of protein binding Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-muscle caldesmon
Short name:
CDM
Alternative name(s):
L-caldesmon
Gene namesi
Name:Cald1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2256. Cald1.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: RGD
  • dendrite Source: RGD
  • dendritic spine Source: RGD
  • myofibril Source: UniProtKB-SubCell
  • neuronal cell body Source: RGD
  • postsynaptic density Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi249 – 2491S → A: Decreases strongly phosphorylation-dependent actin binding. 1 Publication
Mutagenesisi462 – 4621S → A: Decreases phosphorylation-dependent actin binding. 1 Publication
Mutagenesisi468 – 4681T → A: Decreases phosphorylation-dependent actin binding. 1 Publication
Mutagenesisi491 – 4911S → A: Decreases phosphorylation-dependent actin binding. 1 Publication
Mutagenesisi497 – 4971S → A: Decreases phosphorylation-dependent actin binding. 1 Publication
Mutagenesisi527 – 5271S → A: Does not decrease phosphorylation-dependent actin binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 531531Non-muscle caldesmonPRO_0000089290Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei123 – 1231PhosphoserineBy similarity
Modified residuei249 – 2491Phosphoserine; by CDK11 Publication
Modified residuei382 – 3821PhosphoserineBy similarity
Modified residuei395 – 3951PhosphoserineBy similarity
Modified residuei462 – 4621Phosphoserine; by CDK11 Publication
Modified residuei468 – 4681Phosphothreonine; by CDK11 Publication
Modified residuei491 – 4911Phosphoserine; by CDK11 Publication
Modified residuei497 – 4971Phosphoserine; by CDK11 Publication
Modified residuei527 – 5271Phosphoserine; by CDK11 Publication

Post-translational modificationi

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.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ62736.
PRIDEiQ62736.

PTM databases

iPTMnetiQ62736.
PhosphoSiteiQ62736.

Expressioni

Tissue specificityi

High-molecular-weight caldesmon (h-caldesmon) is predominantly expressed in smooth muscles, whereas low-molecular-weight caldesmon (l-caldesmon) is widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart.

Interactioni

GO - Molecular functioni

  • actin binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043767.

Structurei

3D structure databases

ProteinModelPortaliQ62736.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 200181Myosin and calmodulin-bindingBy similarityAdd
BLAST
Regioni303 – 36058Tropomyosin-bindingSequence analysisAdd
BLAST
Regioni392 – 42433Strong actin-bindingBy similarityAdd
BLAST
Regioni402 – 41211Tropomyosin-bindingSequence analysisAdd
BLAST
Regioni454 – 4607Calmodulin-bindingBy similarity
Regioni506 – 53126Weak actin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi33 – 408Poly-Arg
Compositional biasi180 – 18910Poly-Glu
Compositional biasi279 – 2824Poly-Arg
Compositional biasi319 – 3224Poly-Glu
Compositional biasi336 – 3394Poly-Glu

Domaini

The 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.

Sequence similaritiesi

Belongs to the caldesmon family.Curated

Phylogenomic databases

eggNOGiENOG410IH1F. Eukaryota.
ENOG410ZMZI. LUCA.
HOGENOMiHOG000013012.
HOVERGENiHBG050785.
InParanoidiQ62736.
KOiK12327.
PhylomeDBiQ62736.

Family and domain databases

InterProiIPR006017. Caldesmon.
IPR006018. Caldesmon_LSP.
[Graphical view]
PANTHERiPTHR18949. PTHR18949. 1 hit.
PTHR18949:SF0. PTHR18949:SF0. 1 hit.
PfamiPF02029. Caldesmon. 1 hit.
[Graphical view]
PRINTSiPR01076. CALDESMON.

Sequencei

Sequence statusi: Complete.

Q62736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRSGSQGR RCLATLSQIA YQRNDDDEEE AARERRRRAR QERLRQKQEE
60 70 80 90 100
ESLGQVTDQV EAHVQNSAPD EESKPATANA QVEGDEEAAL LERLARREER
110 120 130 140 150
RQKRLQEALE RQKEFDPTIT DGSLSVPSRR MQNNSAENET AEGEEKGESR
160 170 180 190 200
SGRYEMEETE VVITSYQKNS YQDAEDKKKE EKEEEEEEEK LKGGNLGENQ
210 220 230 240 250
IKDEKIKKDK EPKEEVKNFL DRKKGFTEVK AQNGEFMTHK LKQTENAFSP
260 270 280 290 300
SRSGGRASGD KEAEGAPQVE AGKRLEELRR RRGETESEEF EKLKQKQQEA
310 320 330 340 350
ALELEELKKK REERRKVLEE EEQRRKQEEA DRKAREEEEK RRLKEEIERR
360 370 380 390 400
RAEAAEKRQK MPEDGLSEDK KPFKCFTPKG SSLKIEERAE FLNKSVQKSG
410 420 430 440 450
VKSTHQAAVV SKIDSRLEQY TNAIEGTKAS KPMKPAASDL PVPAEGVRNI
460 470 480 490 500
KSMWEKGSVF SSPSASGTPN KETAGLKVGV SSRINEWLTK SPDGNKSPAP
510 520 530
KPSDLRPGDV SGKRNLWEKQ SVDKVTSPTK V
Length:531
Mass (Da):60,584
Last modified:November 1, 1996 - v1
Checksum:iCBBEC50271A23829
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18419 mRNA. Translation: AAA68521.1.
PIRiA55887.
RefSeqiNP_037278.1. NM_013146.2.
UniGeneiRn.204926.

Genome annotation databases

GeneIDi25687.
KEGGirno:25687.
UCSCiRGD:2256. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18419 mRNA. Translation: AAA68521.1.
PIRiA55887.
RefSeqiNP_037278.1. NM_013146.2.
UniGeneiRn.204926.

3D structure databases

ProteinModelPortaliQ62736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043767.

PTM databases

iPTMnetiQ62736.
PhosphoSiteiQ62736.

Proteomic databases

PaxDbiQ62736.
PRIDEiQ62736.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25687.
KEGGirno:25687.
UCSCiRGD:2256. rat.

Organism-specific databases

CTDi800.
RGDi2256. Cald1.

Phylogenomic databases

eggNOGiENOG410IH1F. Eukaryota.
ENOG410ZMZI. LUCA.
HOGENOMiHOG000013012.
HOVERGENiHBG050785.
InParanoidiQ62736.
KOiK12327.
PhylomeDBiQ62736.

Miscellaneous databases

PROiQ62736.

Family and domain databases

InterProiIPR006017. Caldesmon.
IPR006018. Caldesmon_LSP.
[Graphical view]
PANTHERiPTHR18949. PTHR18949. 1 hit.
PTHR18949:SF0. PTHR18949:SF0. 1 hit.
PfamiPF02029. Caldesmon. 1 hit.
[Graphical view]
PRINTSiPR01076. CALDESMON.
ProtoNetiSearch...

Entry informationi

Entry nameiCALD1_RAT
AccessioniPrimary (citable) accession number: Q62736
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.