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

Caldesmon

Gene

CALD1

Organism
Gallus gallus (Chicken)
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.

GO - Molecular functioni

  • actin binding Source: AgBase
  • calmodulin binding Source: CAFA
  • myosin II binding Source: AgBase
  • S100 protein binding Source: AgBase

GO - Biological processi

  • muscle contraction Source: InterPro
  • negative regulation of calcium-dependent ATPase activity Source: AgBase

Keywordsi

Molecular functionActin-binding, Calmodulin-binding, Muscle protein

Enzyme and pathway databases

SABIO-RKiP12957.

Names & Taxonomyi

Protein namesi
Recommended name:
Caldesmon
Short name:
CDM
Gene namesi
Name:CALD1
Synonyms:CAD
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • cell Source: AgBase
  • cytoskeleton Source: UniProtKB-SubCell
  • myofibril Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000892871 – 771CaldesmonAdd BLAST771

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27Phosphotyrosine1 Publication1
Modified residuei597Phosphoserine; by CDK11 Publication1
Modified residuei640Phosphotyrosine1 Publication1
Modified residuei682Phosphoserine; by CDK11 Publication1
Modified residuei688Phosphothreonine; by CDK11 Publication1
Modified residuei711Phosphothreonine; by CDK11 Publication1
Modified residuei717Phosphoserine; by CDK11 Publication1

Post-translational modificationi

Phosphorylated 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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP12957.

PTM databases

iPTMnetiP12957.

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: AgBase
  • calmodulin binding Source: CAFA
  • myosin II binding Source: AgBase
  • S100 protein binding Source: AgBase

Protein-protein interaction databases

STRINGi9031.ENSGALP00000021314.

Structurei

3D structure databases

DisProtiDP00120.
ProteinModelPortaliP12957.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati251 – 2651Add BLAST15
Repeati266 – 2782Add BLAST13
Repeati279 – 2913Add BLAST13
Repeati294 – 3064Add BLAST13
Repeati309 – 3215Add BLAST13
Repeati324 – 3366Add BLAST13
Repeati337 – 3497Add BLAST13
Repeati350 – 3628Add BLAST13
Repeati363 – 3759Add BLAST13
Repeati378 – 39010Add BLAST13

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 199Myosin and calmodulin-bindingAdd BLAST174
Regioni251 – 39010 X 13 AA approximate tandem repeatsAdd BLAST140
Regioni523 – 580Tropomyosin-bindingSequence analysisAdd BLAST58
Regioni612 – 644Strong actin-bindingAdd BLAST33
Regioni622 – 632Tropomyosin-bindingSequence analysisAdd BLAST11
Regioni674 – 680Calmodulin-binding7
Regioni726 – 752Weak actin-bindingAdd BLAST27

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi39 – 46Poly-Arg8
Compositional biasi539 – 542Poly-Glu4
Compositional biasi556 – 559Poly-Glu4

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 muscle forms.

Sequence similaritiesi

Belongs to the caldesmon family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IH1F. Eukaryota.
ENOG410ZMZI. LUCA.
HOGENOMiHOG000013012.
HOVERGENiHBG050785.
InParanoidiP12957.
KOiK12327.
PhylomeDBiP12957.

Family and domain databases

InterProiView protein in InterPro
IPR006017. Caldesmon.
IPR006018. Caldesmon_LSP.
PANTHERiPTHR18949. PTHR18949. 1 hit.
PTHR18949:SF3. PTHR18949:SF3. 1 hit.
PfamiView protein in Pfam
PF02029. Caldesmon. 2 hits.
PRINTSiPR01076. CALDESMON.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Gizzard h-cad (identifier: P12957-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDDFERRREL RRQKREEMRL EAERLSYQRN DDDEEEAARE RRRRARQERL
60 70 80 90 100
RQKEEGDVSG EVTEKSEVNA QNSVAEEETK RSTDDEAALL ERLARREERR
110 120 130 140 150
QKRLQEALER QKEFDPTITD GSLSVPSRRE VNNVEENEIT GKEEKVETRQ
160 170 180 190 200
GRCEIEETET VTKSYQRNNW RQDGEEEGKK EEKDSEEEKP KEVPTEENQV
210 220 230 240 250
DVAVEKSTDK EEVVETKTLA VNAENDTNAM LEGEQSITDA ADKEKEEAEK
260 270 280 290 300
EREKLEAEEK ERLKAEEEKK AAEEKQKAEE EKKAAEERER AKAEEEKRAA
310 320 330 340 350
EERERAKAEE ERKAAEERER AKAEEERKAA EERAKAEEER KAAEERAKAE
360 370 380 390 400
EERKAAEERA KAEKERKAAE ERERAKAEEE KRAAEEKARL EAEKLKEKKK
410 420 430 440 450
MEEKKAQEEK AQANLLRKQE EDKEAKVEAK KESLPEKLQP TSKKDQVKDN
460 470 480 490 500
KDKEKAPKEE MKSVWDRKRG VPEQKAQNGE RELTTPKLKS TENAFGRSNL
510 520 530 540 550
KGAANAEAGS EKLKEKQQEA AVELDELKKR REERRKILEE EEQKKKQEEA
560 570 580 590 600
ERKIREEEEK KRMKEEIERR RAEAAEKRQK VPEDGVSEEK KPFKCFSPKG
610 620 630 640 650
SSLKIEERAE FLNKSAQKSG MKPAHTTAVV SKIDSRLEQY TSAVVGNKAA
660 670 680 690 700
KPAKPAASDL PVPAEGVRNI KSMWEKGNVF SSPGGTGTPN KETAGLKVGV
710 720 730 740 750
SSRINEWLTK TPEGNKSPAP KPSDLRPGDV SGKRNLWEKQ SVEKPAASSS
760 770
KVTATGKKSE TNGLRQFEKE P
Length:771
Mass (Da):88,747
Last modified:November 1, 1997 - v2
Checksum:i518912418DCFC14C
GO
Isoform Brain l-cad (identifier: P12957-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MDDFERRRELRRQKREEMRLEAER → MISRSYCRQNLSSLSK
     200-446: Missing.

Show »
Length:516
Mass (Da):58,804
Checksum:i712F32945E59AEF6
GO
Isoform Gizzard l-cad (identifier: P12957-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     200-446: Missing.

Show »
Length:524
Mass (Da):60,167
Checksum:i956FAE770809A9B5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti318 – 332Missing AA sequence (PubMed:2760048).CuratedAdd BLAST15
Sequence conflicti452D → V in AAA48936 (PubMed:1824698).Curated1
Sequence conflicti762N → NA (PubMed:1824698).Curated1
Sequence conflicti762N → NA (PubMed:8250919).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0041521 – 24MDDFE…LEAER → MISRSYCRQNLSSLSK in isoform Brain l-cad. CuratedAdd BLAST24
Alternative sequenceiVSP_004153200 – 446Missing in isoform Brain l-cad and isoform Gizzard l-cad. 1 PublicationAdd BLAST247

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04968 mRNA. Translation: AAA49067.1.
D17648 Genomic DNA. Translation: BAA04539.1.
M28417 mRNA. Translation: AAA48810.1.
M60620 mRNA. Translation: AAA48936.1.
D17648 Genomic DNA. Translation: BAA04538.1.
D17648 Genomic DNA. Translation: BAA04540.1.
M59762 mRNA. Translation: AAA48649.1.
D17552 Genomic DNA. Translation: BAA04490.1.
M26684 mRNA. Translation: AAA48811.1.
PIRiA33430.
A39038.
RefSeqiNP_989489.1. NM_204158.1.
UniGeneiGga.4988.

Genome annotation databases

GeneIDi373965.
KEGGigga:373965.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04968 mRNA. Translation: AAA49067.1.
D17648 Genomic DNA. Translation: BAA04539.1.
M28417 mRNA. Translation: AAA48810.1.
M60620 mRNA. Translation: AAA48936.1.
D17648 Genomic DNA. Translation: BAA04538.1.
D17648 Genomic DNA. Translation: BAA04540.1.
M59762 mRNA. Translation: AAA48649.1.
D17552 Genomic DNA. Translation: BAA04490.1.
M26684 mRNA. Translation: AAA48811.1.
PIRiA33430.
A39038.
RefSeqiNP_989489.1. NM_204158.1.
UniGeneiGga.4988.

3D structure databases

DisProtiDP00120.
ProteinModelPortaliP12957.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000021314.

PTM databases

iPTMnetiP12957.

Proteomic databases

PaxDbiP12957.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi373965.
KEGGigga:373965.

Organism-specific databases

CTDi800.

Phylogenomic databases

eggNOGiENOG410IH1F. Eukaryota.
ENOG410ZMZI. LUCA.
HOGENOMiHOG000013012.
HOVERGENiHBG050785.
InParanoidiP12957.
KOiK12327.
PhylomeDBiP12957.

Enzyme and pathway databases

SABIO-RKiP12957.

Miscellaneous databases

PROiPR:P12957.

Family and domain databases

InterProiView protein in InterPro
IPR006017. Caldesmon.
IPR006018. Caldesmon_LSP.
PANTHERiPTHR18949. PTHR18949. 1 hit.
PTHR18949:SF3. PTHR18949:SF3. 1 hit.
PfamiView protein in Pfam
PF02029. Caldesmon. 2 hits.
PRINTSiPR01076. CALDESMON.
ProtoNetiSearch...

Entry informationi

Entry nameiCALD1_CHICK
AccessioniPrimary (citable) accession number: P12957
Secondary accession number(s): Q03698
, Q90756, Q90761, Q92018, Q99230
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1997
Last modified: May 10, 2017
This is version 118 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.