Calponin homology domain

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1sjj B:33-136 1tjt A:46-149 1wku A:46-149 1sh5 B:186-293 1sh6 A:186-293 1mb8 A:180-282 1dxx A:16-119 1qag B:32-135 1rt8 A:386-495 1pxy B:393-498 1aoa :121-236 1wyp A:29-132 1h67 A:29-132 1wyn A:29-132 1ujo A:25-138 1wym A:25-137 1wyr A:4-111 1p2x A:42-148 1p5s A:42-148 1bkr A:174-278 1aa2 :174-278 1wyq A:178-281 1bhd A:151-254 1wyl A:509-612 1wjo A:517-624 1wyo A:15-116 1vka B:15-116 1ueg A:15-116 1pa7 A:15-116

Calponin homology (CH) domain
Calponin homology (CH) domain
	Solution structure of calponin homology domain of IQGAP1
Identifiers
Symbol	CH
Pfam	PF00307
InterPro	IPR001715
SMART	CH
PROSITE	PDOC00019
SCOP2	1aoa / SCOPe / SUPFAM
CDD	cd00014
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1sjj B:33-136 1tjt A:46-149 1wku A:46-149 1sh5 B:186-293 1sh6 A:186-293 1mb8 A:180-282 1dxx A:16-119 1qag B:32-135 1rt8 A:386-495 1pxy B:393-498 1aoa :121-236 1wyp A:29-132 1h67 A:29-132 1wyn A:29-132 1ujo A:25-138 1wym A:25-137 1wyr A:4-111 1p2x A:42-148 1p5s A:42-148 1bkr A:174-278 1aa2 :174-278 1wyq A:178-281 1bhd A:151-254 1wyl A:509-612 1wjo A:517-624 1wyo A:15-116 1vka B:15-116 1ueg A:15-116 1pa7 A:15-116

Last updated December 04, 2023

Calponin homology domain (or CH domain) is a family of actin binding domains found in both cytoskeletal proteins and signal transduction proteins.^[2] The domain is about 100 amino acids in length and is composed of four alpha helices.^[3] It comprises the following groups of actin-binding domains:

Actinin-type (including spectrin, fimbrin, ABP-280)
Calponin-type

A comprehensive review of proteins containing this type of actin-binding domains is given in.^[4]

The CH domain is involved in actin binding in some members of the family. However, in calponins there is evidence that the CH domain is not involved in its actin binding activity.^[5] Most proteins have two copies of the CH domain, however some proteins such as calponin and the human vav proto-oncogene ( P15498 ) have only a single copy. The structure of an example CH domain has been determined using X-ray crystallography.^[6]

Examples

Human genes encoding calponin homology domain-containing proteins include:

ACTN1, ACTN2, ACTN3, ACTN4, ARHGEF6, ARHGEF7, ASPM,
CLMN, CNN1, CNN2, CNN3,
DIXDC1, DMD, DST,
EHBP1, EHBP1L1,
FLNA, FLNB, FLNC,
GAS2, GAS2L1, GAS2L2, GAS2L3,
IQGAP1, IQGAP2, IQGAP3,
LCP1, LIMCH1, LMO7, LRCH1, LRCH2, LRCH3, LRCH4,
MACF1, MAPRE1, MAPRE2, MAPRE3, MICAL1, MICAL2, MICAL2PV1, MICAL2PV2, MICAL3, MICALL1, MICALL2,
NAV2, NAV3,
PARVA, PARVB, PARVG, PLEC1, PLS1, PLS3, PP14183,
SMTN, SMTNL2, SPECC1, SPECC1L, SPNB4, SPTB, SPTBN1, SPTBN2, SPTBN4, SPTBN5, SYNE1, SYNE2,
TAGLN, TAGLN2, TAGLN3,
UTRN, and
VAV1, VAV2, VAV3

Related Research Articles

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Pleckstrin homology domain or (PHIP) is a protein domain of approximately 120 amino acids that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton.

Utrophin is a protein that in humans is encoded by the UTRN gene. The name is a short form for ubiquitous dystrophin.

<span class="mw-page-title-main">Calponin</span> Calcium binding protein

Calponin is a calcium binding protein. Calponin tonically inhibits the ATPase activity of myosin in smooth muscle. Phosphorylation of calponin by a protein kinase, which is dependent upon calcium binding to calmodulin, releases the calponin's inhibition of the smooth muscle ATPase.

Actinin is a microfilament protein. The functional protein is an anti-parallel dimer, which cross-links the thin filaments in adjacent sarcomeres, and therefore coordinates contractions between sarcomeres in the horizontal axis. Alpha-actinin is a part of the spectrin superfamily. This superfamily is made of spectrin, dystrophin, and their homologous and isoforms. In non-muscle cells, it is found by the actin filaments and at the adhesion sites.The lattice like arrangement provides stability to the muscle contractile apparatus. Specifically, it helps bind actin filaments to the cell membrane. There is a binding site at each end of the rod and with bundles of actin filaments.

Protein 4.1,, is a protein associated with the cytoskeleton that in humans is encoded by the EPB41 gene. Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Protein 4.1 interacts with spectrin and short actin filaments to form the erythrocyte membrane skeleton. Mutations of spectrin and protein 4.1 are associated with elliptocytosis or spherocytosis and anemia of varying severity.

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.

Spectrin alpha chain, erythrocyte is a protein that in humans is encoded by the SPTA1 gene.

Alpha II-spectrin, also known as Spectrin alpha chain, brain is a protein that in humans is encoded by the SPTAN1 gene. Alpha II-spectrin is expressed in a variety of tissues, and is highly expressed in cardiac muscle at Z-disc structures, costameres and at the sarcolemma membrane. Mutations in alpha II-spectrin have been associated with early infantile epileptic encephalopathy-5, and alpha II-spectrin may be a valuable biomarker for Guillain–Barré syndrome and infantile congenital heart disease.

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Ras GTPase-activating-like protein IQGAP1 (IQGAP1) also known as p195 is a ubiquitously expressed protein that in humans is encoded by the IQGAP1 gene. IQGAP1 is a scaffold protein involved in regulating various cellular processes ranging from organization of the actin cytoskeleton, transcription, and cellular adhesion to regulating the cell cycle.

Alpha-actinin-2 is a protein which in humans is encoded by the ACTN2 gene. This gene encodes an alpha-actinin isoform that is expressed in both skeletal and cardiac muscles and functions to anchor myofibrillar actin thin filaments and titin to Z-discs.

Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.

Spectrin beta chain, brain 1 is a protein that in humans is encoded by the SPTBN1 gene.

Alpha-centractin (yeast) or ARP1 is a protein that in humans is encoded by the ACTR1A gene.

Ena/VASP-like protein is a member of the Ena/VASP family of proteins that in humans is encoded by the EVL gene.

TRIO and F-actin-binding protein is a protein that in humans is encoded by the TRIOBP gene.

WH1 domain is an evolutionary conserved protein domain found on WASP proteins, which are often involved in actin polymerization.

Calponin 1 is a basic smooth muscle protein that in humans is encoded by the CNN1 gene.

References

↑ PDB: 2RR8 ; Umemoto R, Nishida N, Ogino S, Shimada I (September 2010). "NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode". J. Biomol. NMR. 48 (1): 59–64. doi:10.1007/s10858-010-9434-8. PMID 20644981. S2CID 25649748.
↑ Saraste M, Castresana J (1995). "Does Vav bind to F-actin through a CH domain?". FEBS Lett. 374 (2): 149–151. doi:10.1016/0014-5793(95)01098-Y. PMID 7589522. S2CID 29667309.
↑ Korenbaum, E.; Rivero, F. (Sep 2002). "Calponin homology domains at a glance". J Cell Sci. 115 (Pt 18): 3543–5. CiteSeerX 10.1.1.608.8653 . doi:10.1242/jcs.00003. PMID 12186940. S2CID 38137068.
↑ Hartwig JH (1995). "Actin-binding proteins. 1: Spectrin super family". Protein Prof. 2 (7): 703–800. PMID 7584474.
↑ Gimona M, Mital R (1998). "The single CH domain of calponin is neither sufficient nor necessary for F-actin binding". J. Cell Sci. 111: 1813–1821. PMID 9625744.
↑ Saraste M, Carugo KD, Banuelos S (1997). "Crystal structure of a calponin homology domain". Nat. Struct. Biol. 4 (3): 175–179. doi:10.1038/nsb0397-175. PMID 9164454. S2CID 1428195.

This article incorporates text from the public domain Pfam and InterPro: IPR001715

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[pmid20644981-1] PDB: 2RR8 ; Umemoto R, Nishida N, Ogino S, Shimada I (September 2010). "NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode". J. Biomol. NMR. 48 (1): 59–64. doi:10.1007/s10858-010-9434-8. PMID 20644981. S2CID 25649748.

[PUB00001696-2] Saraste M, Castresana J (1995). "Does Vav bind to F-actin through a CH domain?". FEBS Lett. 374 (2): 149–151. doi:10.1016/0014-5793(95)01098-Y. PMID 7589522. S2CID 29667309.

[Korenbaum-2002-3] Korenbaum, E.; Rivero, F. (Sep 2002). "Calponin homology domains at a glance". J Cell Sci. 115 (Pt 18): 3543–5. CiteSeerX 10.1.1.608.8653 . doi:10.1242/jcs.00003. PMID 12186940. S2CID 38137068.

[PUB00004975-4] Hartwig JH (1995). "Actin-binding proteins. 1: Spectrin super family". Protein Prof. 2 (7): 703–800. PMID 7584474.

[PUB00003095-5] Gimona M, Mital R (1998). "The single CH domain of calponin is neither sufficient nor necessary for F-actin binding". J. Cell Sci. 111: 1813–1821. PMID 9625744.

[PUB00003938-6] Saraste M, Carugo KD, Banuelos S (1997). "Crystal structure of a calponin homology domain". Nat. Struct. Biol. 4 (3): 175–179. doi:10.1038/nsb0397-175. PMID 9164454. S2CID 1428195.

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