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CALD1

Identifiers

CALD1, CDM, H-CAD, HCAD, L-CAD, LCAD, NAG22, caldesmon 1, h-CD

External IDs

OMIM: 114213; HomoloGene: 137424; GeneCards: CALD1; OMA:CALD1 - orthologs

Gene location (Human)
👁 Chromosome 7 (human)
Chr.	Chromosome 7 (human)^[1]
👁 Chromosome 7 (human) 👁 Genomic location for CALD1 👁 Genomic location for CALD1
Band	7q33	Start	134,744,252 bp^[1]
Band	7q33	End	134,970,729 bp^[1]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

saphenous vein

tail of epididymis

seminal vesicula

tendon of biceps brachii

urethra

superficial temporal artery

visceral pleura

parietal pleura

stromal cell of endometrium

right coronary artery

n/a

More reference expression data

BioGPS

👁 Image 👁 Image 👁 Image
More reference expression data

Gene ontology
Molecular function	myosin binding actin binding tropomyosin binding protein binding calmodulin binding cadherin binding
Cellular component	cytoplasm cytosol plasma membrane myofibril cytoskeleton actin cytoskeleton intracellular membrane-bounded organelle membrane actin cap
Biological process	muscle contraction
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


800


n/a

Ensembl


ENSG00000122786


n/a

UniProt


Q05682


n/a

RefSeq (mRNA)


NM_004342 NM_033138 NM_033139 NM_033140 NM_033157


n/a

RefSeq (protein)


NP_004333 NP_149129 NP_149130 NP_149131 NP_149347


n/a

Location (UCSC)

Chr 7: 134.74 – 134.97 Mb

n/a

PubMed search

^[2]

n/a

Wikidata

View/Edit Human

Caldesmon is a protein that in humans is encoded by the CALD1 gene.^[3]^[4]

Caldesmon is a calmodulin binding protein. Like calponin, caldesmon tonically inhibits the ATPase activity of myosin in smooth muscle.

This gene encodes a calmodulin- and actin-binding protein that plays an essential role in the regulation of smooth muscle and nonmuscle contraction. The conserved domain of this protein possesses the binding activities to 👁 {\displaystyle {\text{Ca}}^{2+}}
-calmodulin, actin, tropomyosin, myosin, and phospholipids. This protein is a potent inhibitor of the actin-tropomyosin activated myosin MgATPase, and serves as a mediating factor for 👁 {\displaystyle {\text{Ca}}^{2+}}
-dependent inhibition of smooth muscle contraction. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms.^[4]

Immunochemistry

[edit]

In diagnostic immunochemistry, caldesmon is a marker for smooth muscle differentiation.

References

[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000122786 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Novy RE, Lin JL, Lin JJ (Oct 1991). "Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells". J Biol Chem. 266 (25): 16917–24. doi:10.1016/S0021-9258(18)55390-4. PMID 1885618.
^ ^a ^b "Entrez Gene: CALD1 caldesmon 1".

Huber PA (1998). "Caldesmon". Int. J. Biochem. Cell Biol. 29 (8–9): 1047–51. doi:10.1016/S1357-2725(97)00004-6. PMID 9415999.
Gusev NB (2002). "Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation". Biochemistry Mosc. 66 (10): 1112–21. doi:10.1023/A:1012480829618. PMID 11736632. S2CID 310781.
Wang CL (2002). "Caldesmon and smooth-muscle regulation". Cell Biochem. Biophys. 35 (3): 275–88. doi:10.1385/CBB:35:3:275. PMID 11894847. S2CID 195271255.
Mani RS, McCubbin WD, Kay CM (1992). "Calcium-dependent regulation of caldesmon by an 11-kDa smooth muscle calcium-binding protein, caltropin". Biochemistry. 31 (47): 11896–901. doi:10.1021/bi00162a031. PMID 1445920.
Hayashi K, Yano H, Hashida T, et al. (1993). "Genomic structure of the human caldesmon gene". Proc. Natl. Acad. Sci. U.S.A. 89 (24): 12122–6. doi:10.1073/pnas.89.24.12122. PMC 50710. PMID 1465449.
Humphrey MB, Herrera-Sosa H, Gonzalez G, et al. (1992). "Cloning of cDNAs encoding human caldesmons". Gene. 112 (2): 197–204. doi:10.1016/0378-1119(92)90376-Z. PMID 1555769.
Adam LP, Gapinski CJ, Hathaway DR (1992). "Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas". FEBS Lett. 302 (3): 223–6. doi:10.1016/0014-5793(92)80446-N. PMID 1601129. S2CID 46129878.
Horiuchi KY, Chacko S (1989). "Interaction between caldesmon and tropomyosin in the presence and absence of smooth muscle actin". Biochemistry. 27 (22): 8388–93. doi:10.1021/bi00422a014. PMID 3242591.
der Terrossian E, Deprette C, Lebbar I, Cassoly R (1994). "Purification and characterization of erythrocyte caldesmon. Hypothesis for an actin-linked regulation of a contractile activity in the red blood cell membrane". Eur. J. Biochem. 219 (1–2): 503–11. doi:10.1111/j.1432-1033.1994.tb19965.x. PMID 8307018.
Surgucheva I, Bryan J (1996). "Over-expression of smooth muscle caldesmon in mouse fibroblasts". Cell Motil. Cytoskeleton. 32 (3): 233–43. doi:10.1002/cm.970320307. PMID 8581978.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Graether SP, Heinonen TY, Raharjo WH, et al. (1997). "Tryptophan residues in caldesmon are major determinants for calmodulin binding". Biochemistry. 36 (2): 364–9. doi:10.1021/bi962008k. PMID 9003189.
Wang Z, Danielsen AJ, Maihle NJ, McManus MJ (1999). "Tyrosine phosphorylation of caldesmon is required for binding to the Shc.Grb2 complex". J. Biol. Chem. 274 (47): 33807–13. doi:10.1074/jbc.274.47.33807. PMID 10559276.
Adam L, Vadlamudi R, Mandal M, et al. (2000). "Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1". J. Biol. Chem. 275 (16): 12041–50. doi:10.1074/jbc.275.16.12041. PMID 10766836.
Hall SM, Hislop AA, Pierce CM, Haworth SG (2000). "Prenatal origins of human intrapulmonary arteries: formation and smooth muscle maturation". Am. J. Respir. Cell Mol. Biol. 23 (2): 194–203. doi:10.1165/ajrcmb.23.2.3975. PMID 10919986.
Nimmrich I, Erdmann S, Melchers U, et al. (2000). "Seven genes that are differentially transcribed in colorectal tumor cell lines". Cancer Lett. 160 (1): 37–43. doi:10.1016/S0304-3835(00)00553-X. PMID 11098082.
Hisaoka M, Wei-Qi S, Jian W, et al. (2003). "Specific but variable expression of h-caldesmon in leiomyosarcomas: an immunohistochemical reassessment of a novel myogenic marker". Appl. Immunohistochem. Mol. Morphol. 9 (4): 302–8. doi:10.1097/00022744-200112000-00003. PMID 11759055. S2CID 25653139.
Sobue K, Muramoto Y, Fujita M, Kakiuchi S (Sep 1981). "Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin". Proc. Natl. Acad. Sci. U.S.A. 78 (9): 5652–5. Bibcode:1981PNAS...78.5652S. doi:10.1073/pnas.78.9.5652. PMC 348816. PMID 6946503.