| General information | | DisProt: | DP00120 | | Name: | Caldesmon | | Synonym(s): | CALD1_CHICK
CDM
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P12957 | | UniGene: | Gga.4988 | | SwissProt: | CALD1_CHICK | | TrEMBL: | | | NCBI (GI): | 2506984 | | Source organism: | Gallus gallus (Chicken) | | Sequence length: | 771 | | Percent disordered: | 18% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MDDFERRREL RRQKREEMRL EAERLSYQRN DDDEEEAARE RRRRARQERL RQKEEGDVSG - 60
EVTEKSEVNA QNSVAEEETK RSTDDEAALL ERLARREERR QKRLQEALER QKEFDPTITD - 120
GSLSVPSRRE VNNVEENEIT GKEEKVETRQ GRCEIEETET VTKSYQRNNW RQDGEEEGKK - 180
EEKDSEEEKP KEVPTEENQV DVAVEKSTDK EEVVETKTLA VNAENDTNAM LEGEQSITDA - 240
ADKEKEEAEK EREKLEAEEK ERLKAEEEKK AAEEKQKAEE EKKAAEERER AKAEEEKRAA - 300
EERERAKAEE ERKAAEERER AKAEEERKAA EERAKAEEER KAAEERAKAE EERKAAEERA - 360
KAEKERKAAE ERERAKAEEE KRAAEEKARL EAEKLKEKKK MEEKKAQEEK AQANLLRKQE - 420
EDKEAKVEAK KESLPEKLQP TSKKDQVKDN KDKEKAPKEE MKSVWDRKRG VPEQKAQNGE - 480
RELTTPKLKS TENAFGRSNL KGAANAEAGS EKLKEKQQEA AVELDELKKR REERRKILEE - 540
EEQKKKQEEA ERKIREEEEK KRMKEEIERR RAEAAEKRQK VPEDGVSEEK KPFKCFSPKG - 600
SSLKIEERAE FLNKSAQKSG MKPAHTTAVV SKIDSRLEQY TSAVVGNKAA KPAKPAASDL - 660
PVPAEGVRNI KSMWEKGNVF SSPGGTGTPN KETAGLKVGV SSRINEWLTK TPEGNKSPAP - 720
KPSDLRPGDV SGKRNLWEKQ SVEKPAASSS KVTATGKKSE TNGLRQFEKE P
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| Functional narrative |
Caldesmon is an essential for regulation of smooth-muscle contraction. This protein interacts directly with many other proteins including actin, smooth-muscle tropomyosin, non-muscle tropomyosin, calmodulin, myosin, caltropin, and calcyclin. Caldesmon can be found in the thin filaments of smooth muscle.
The disordered region of this protein functions as a multi-partner binding site for a variety of binding partners. Many isoforms of this protein exist - the largest was characterized here.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 636 - 771 | | Length: | 136 | | Region sequence: |
RLEQYTSAVVGNKAAKPAKPAASDLPVPAEGVRNIKSMWEKGNVFSSPGGTGTPNKETAG
LKVGVSSRINEWLTKTPEGNKSPAPKPSDLRPGDVSGKRNLWEKQSVEKPAASSSKVTAT
GKKSETNGLRQFEKEP | | Modification type: | Complex
Engineered
Fragment
Isoform
| | PDB: | | | Structural/functional type: | Function arises via a pre-molten globule to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Phosphorylation
Protein-protein binding
| Detection methods:
- SDS-PAGE gel, Aberrant mobility on (293 K; Calcium; Calmodulin)
- Circular dichroism (CD) spectroscopy, far-UV (293 K; Calcium; Calmodulin)
- Size exclusion/gel filtration chromatography (293 K; Calcium; Calmodulin)
- Small-angle X-ray scattering (SAXS) (293 K; Calcium; Calmodulin)
- Stability at thermal extremes (293 K; Calcium; Calmodulin)
| References:
- Czuryło EA. "Motifs of the caldesmon family." Acta Biochim Pol. 2000; 47(4): 1019-26. PubMed: 11996092
- Hayashi K, Kanda K, Kimizuka F, Kato I, Sobue K. "Primary structure and functional expression of h-caldesmon complementary DNA." Biochem Biophys Res Commun. 1989; 164(1): 503-511. PubMed: 2803315
- Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN. "Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin." Proteins. 2003; 53(4): 855-862. PubMed: 14635127
| Comments:
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| References |
- Haruna M, Hayashi K, Yano H, Takeuchi O, Sobue K. "Common structural and expressional properties of vertebrate caldesmon genes." Biochem Biophys Res Commun. 1993; 197(1): 145-53. PubMed: 8250919
- Lynch WP, Riseman VM, Bretscher A. "Smooth muscle caldesmon is an extended flexible monomeric protein in solution that can readily undergo reversible intra- and intermolecular sulfhydryl cross-linking. A mechanism for caldesmon's F-actin bundling activity." J Biol Chem. 1987; 262(15): 7429-37. PubMed: 3584120
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