Calponin homology domain

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

Calponin homology (CH) domain
Solution structure of calponin homology domain of IQGAP1[1]
Identifiers
Symbol	CH
Pfam	PF00307
InterPro	IPR001715
SMART	CH
PROSITE	PDOC00019
SCOP2	1aoa / SCOPe / SUPFAM
CDD	cd00014
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB 1sjjB:33-136 1tjtA:46-149 1wkuA:46-149 1sh5B:186-293 1sh6A:186-293 1mb8A:180-282 1dxxA:16-119 1qagB:32-135 1rt8A:386-495 1pxyB:393-498 1aoa :121-236 1wypA:29-132 1h67A:29-132 1wynA:29-132 1ujoA:25-138 1wymA:25-137 1wyrA:4-111 1p2xA:42-148 1p5sA:42-148 1bkrA:174-278 1aa2 :174-278 1wyqA:178-281 1bhdA:151-254 1wylA:509-612 1wjoA:517-624 1wyoA:15-116 1vkaB:15-116 1uegA:15-116 1pa7A:15-116

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

References

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

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