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InterPro: IPR008985 Concanavalin A-like lectin/glucanase

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UniProtKB

Matches:

15044 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
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Accession List
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Accession

IPR008985 ConA-like_lec_gl

Type

Domain

Signatures Help

Database	ID	Name	Proteins
SuperFamily	SSF49899	ConA_like_lec_gl	15044
Signatures in BioMart

InterPro Relationships Help

Children

IPR013189 Glycosyl hydrolase family 32, C-terminal
IPR013319 Glycoside hydrolase, family 11/12, catalytic domain
IPR013320 Concanavalin A-like lectin/glucanase, subgroup

Found in

IPR000250 Peptidase G1, eqolisin
IPR001722 Glycoside hydrolase, family 7
IPR017229 Multidomain scavenger receptor-like protein PxSR

Contains

IPR000985 Legume lectin, alpha chain, conserved site
IPR002705 Peptidase C30/C16, subtype
IPR006558 LamG-like jellyroll fold
IPR008263 Glycoside hydrolase, family 16, active site
IPR008740 Peptidase C30, Coronavirus endopeptidase
IPR010713 Xyloglucan endo-transglycosylase, C-terminal
IPR014822 Nsp9 replicase
IPR014827 Papain-like viral protease
IPR014828 Nsp7 replicase
IPR014829 Nsp8 replicase
IPR015344 Vibrio cholerae sialidase, lectin insertion
IPR018124 Calreticulin/calnexin, conserved site
IPR018208 Glycoside hydrolase, family 11, active site
IPR018995 RNA synthesis protein NSP10/peptidase C30/C16B, coronavirus
IPR019825 Legume lectin, beta chain, Mn/Ca-binding site

InterPro annotation

Entry Details in BioMart

Abstract

Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain, which consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse, and include the lectins: legume lectins, cereal lectins, viral lectins, and animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds, the binding of nitrogen-fixing bacteria to root hairs, the inhibition of fungal growth or insect feeding, and in hormonally regulated plant growth [1]. Protein members include concanavalin A (Con A), favin, isolectin I, lectin IV, soybean agglutinin and lentil lectin. Animal lectins include the galectins, which are S-type lactose-binding and IgE-binding proteins such as S-lectin, CLC protein, galectin1, galectin2, galectin3 CRD, and Congerin I [2].

Other members with a Con A-like domain include the glucanases and xylanases. Bacterial and fungal beta-glucanases, such as Bacillus 1-3,1-4-beta-glucanse, carry out the acid catalysis of beta-glucans found in microorganisms and plants [3]. Similarly, kappa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls [4]. Xylanase and cellobiohydrolase I degrade hemicellulose and cellulose, respectively [5, 6].

There are many Con A-like domains found in proteins involved in cell recognition and adhesion. For example, several viral and bacterial toxins carry Con A-like domains. Examples include the Clostridium neurotoxins responsible for the neuroparalytic effects of botulism and tetanus [7]. The Pseudomonas exotoxin A, a virulence factor which is highly toxic to eukaryotic cells, causing the arrest of protein synthesis, contains a Con A-like domain involved in receptor binding [8]. Cholerae neuraminidase can bind to cell surfaces, possibly through their Con A-like domains, where they function as part of a mucinase complex to degrade the mucin layer of the gastrointestinal tract [9]. The rotaviral outer capsid protein, VP4, has a Con A-like sialic acid binding domain, which functions in cell attachment and membrane penetration [10].

Con A-like domains also play a role in cell recognition in eukaryotes. Proteins containing a Con A-like domain include the sex hormone-binding globulins which transport sex steroids in blood and regulate their access to target tissues [11], laminins which are large heterotrimeric glycoproteins involved in basement membrane architecture and function [12], neurexins which are expressed in hundreds of isoforms on the neuronal cell surface, where they may function as cell recognition molecules [13] and sialidases that are found in both microorganisms and animals, and function in cell adhesion and signal transduction [14].

Other proteins containing a Con A-like domain include pentraxins and calnexins. The pentraxin PTX3 is a TNFalpha-induced, secreted protein of adipose cells produced during inflammation [15]. The calnexin family of molecular chaperones is conserved among plants, fungi, and animals. Family members include Calnexin, a type-I integral membrane protein in the endoplasmic reticulum which coordinates the processing of newly synthesized N-linked glycoproteins with their productive folding, calmegin, a type-I membrane protein expressed mainly in the spermatids of the testis, and calreticulin, a soluble ER lumenal paralog [16].

Structural links Help

PDB - click here

SCOP: b.1.1.4 , b.1.2.1 , b.104.1.1 , b.140.1.1 , b.29.1.1 , b.29.1.10 , b.29.1.11 , b.29.1.12 , b.29.1.13 , b.29.1.14 , b.29.1.15 , b.29.1.16 , b.29.1.17 , b.29.1.18 , b.29.1.19 , b.29.1.2 , b.29.1.20 , b.29.1.21 , b.29.1.3 , b.29.1.4 , b.29.1.5 , b.29.1.6 , b.29.1.7 , b.29.1.8 , b.29.1.9 , b.47.1.4 , c.66.1.48 , d.144.1.7 , d.15.14.1 , d.169.1.1 , d.294.1.2 , g.23.1.1 , g.3.11.1 , g.3.18.1 , g.86.1.1 , h.4.2.1

CATH: 1.10.1840.10 , 1.10.510.10 , 2.10.25.10 , 2.10.250.10 , 2.120.10.10 , 2.40.10.10 , 2.60.120.180 , 2.60.120.200 , 2.60.120.560 , 2.60.40.10 , 2.60.40.30 , 2.70.100.10 , 3.30.200.20 , 3.90.1350.10 , 3.90.290.10 , 4.10.1080.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008985

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00182 Galectin-9

O08573 Galectin-9

P24014 Protein slit

P27798 Calreticulin

P43555 Protein EMP47

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001791	Laminin G
IPR006210	EGF-like
IPR000483	Cysteine-rich flanking region, C-terminal domain
IPR009169	Calreticulin
IPR001611	Leucine-rich repeat
IPR013032	EGF-like region, conserved site
IPR018097	EGF-like calcium-binding, conserved site
IPR006207	Cystine knot, C-terminal
IPR005052	Legume-like lectin
IPR001881	EGF-like calcium-binding
IPR001079	Galectin, carbohydrate recognition domain
IPR013320	Concanavalin A-like lectin/glucanase, subgroup
IPR012679	Laminin G, subdomain 1
IPR003591	Leucine-rich repeat, typical subtype
IPR018124	Calreticulin/calnexin, conserved site
IPR000372	Leucine-rich repeat-containing N-terminal domain
IPR016710	L-type lectin, fungi
IPR000152	EGF-type aspartate/asparagine hydroxylation site
IPR000742	EGF-like, type 3
IPR001580	Calreticulin/calnexin
IPR008985	Concanavalin A-like lectin/glucanase
IPR006209	EGF
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Sanz-Aparicio J, Hermoso J, Grangeiro TB, Calvete JJ, Cavada BS. The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A. FEBS Lett. 405 114-8 1997 [PubMed: 9094437] http://dx.doi.org/10.1016/S0014-5793(97)00137-3
2.	Ackerman SJ, Liu L, Kwatia MA, Savage MP, Leonidas DD, Swaminathan GJ, Acharya KR. Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion. J. Biol. Chem. 277 14859-68 2002 [PubMed: 11834744] http://dx.doi.org/10.1074/jbc.M200221200
3.	Hahn M, Pons J, Planas A, Querol E, Heinemann U. Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution. FEBS Lett. 374 221-4 1995 [PubMed: 7589539] http://dx.doi.org/10.1016/0014-5793(95)01111-Q
4.	Michel G, Chantalat L, Duee E, Barbeyron T, Henrissat B, Kloareg B, Dideberg O. The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases. Structure 9 513-25 2001 [PubMed: 11435116] http://dx.doi.org/10.1016/S0969-2126(01)00612-8
5.	Ay J, Gotz F, Borriss R, Heinemann U. Structure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain. Proc. Natl. Acad. Sci. U.S.A. 95 6613-8 1998 [PubMed: 9618460] http://dx.doi.org/10.1073/pnas.95.12.6613
6.	Divne C, Stahlberg J, Teeri TT, Jones TA. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei. J. Mol. Biol. 275 309-25 1998 [PubMed: 9466911] http://dx.doi.org/10.1006/jmbi.1997.1437
7.	Swaminathan S, Eswaramoorthy S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 7 693-9 2000 [PubMed: 10932256] http://dx.doi.org/10.1038/78005
8.	Wedekind JE, Trame CB, Dorywalska M, Koehl P, Raschke TM, McKee M, FitzGerald D, Collier RJ, McKay DB. Refined crystallographic structure of Pseudomonas aeruginosa exotoxin A and its implications for the molecular mechanism of toxicity. J. Mol. Biol. 314 823-37 2001 [PubMed: 11734000] http://dx.doi.org/10.1006/jmbi.2001.5195
9.	Crennell S, Garman E, Laver G, Vimr E, Taylor G. Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. Structure 2 535-44 1994 [PubMed: 7922030] http://dx.doi.org/10.1016/S0969-2126(00)00053-8
10.	Dormitzer PR, Sun ZY, Wagner G, Harrison SC. The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. EMBO J. 21 885-97 2002 [PubMed: 11867517] http://dx.doi.org/10.1093/emboj/21.5.885
11.	Grishkovskaya I, Avvakumov GV, Sklenar G, Dales D, Hammond GL, Muller YA. Crystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domain. EMBO J. 19 504-12 2000 [PubMed: 10675319] http://dx.doi.org/10.1093/emboj/19.4.504
12.	Tisi D, Talts JF, Timpl R, Hohenester E. Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin. EMBO J. 19 1432-40 2000 [PubMed: 10747011] http://dx.doi.org/10.1093/emboj/19.7.1432
13.	Rudenko G, Nguyen T, Chelliah Y, Sudhof TC, Deisenhofer J. The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing. Cell 99 93-101 1999 [PubMed: 10520997] http://dx.doi.org/10.1016/S0092-8674(00)80065-3
14.	Buschiazzo A, Amaya MF, Cremona ML, Frasch AC, Alzari PM. The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis. Mol. Cell 10 757-68 2002 [PubMed: 12419220] http://dx.doi.org/10.1016/S1097-2765(02)00680-9
15.	Abderrahim-Ferkoune A, Bezy O, Chiellini C, Maffei M, Grimaldi P, Bonino F, Moustaid-Moussa N, Pasqualini F, Mantovani A, Ailhaud G, Amri EZ. Characterization of the long pentraxin PTX3 as a TNFalpha-induced secreted protein of adipose cells. J. Lipid Res. 44 994-1000 2003 [PubMed: 12611905] http://dx.doi.org/10.1194/jlr.M200382-JLR200
16.	Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M. The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8 633-44 2001 [PubMed: 11583625] http://dx.doi.org/10.1016/S1097-2765(01)00318-5

Additional Reading Open in usermanual
	Bhardwaj K, Palaninathan S, Alcantara JM, Yi LL, Guarino L, Sacchettini JC, Kao CC. Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15. J. Biol. Chem. 283 2008 3655-64 [PubMed: 18045871] http://dx.doi.org/10.1074/jbc.M708375200
	Vandermarliere E, Bourgois TM, Rombouts S, Van Campenhout S, Volckaert G, Strelkov SV, Delcour JA, Rabijns A, Courtin CM. Crystallographic analysis shows substrate binding at the -3 to +1 active-site subsites and at the surface of glycoside hydrolase family 11 endo-1,4-beta-xylanases. Biochem. J. 410 2008 71-9 [PubMed: 17983355] http://dx.doi.org/10.1042/BJ20071128
	Vardakou M, Dumon C, Murray JW, Christakopoulos P, Weiner DP, Juge N, Lewis RJ, Gilbert HJ, Flint JE. Understanding the structural basis for substrate and inhibitor recognition in eukaryotic GH11 xylanases. J. Mol. Biol. 375 2008 1293-305 [PubMed: 18078955] http://dx.doi.org/10.1016/j.jmb.2007.11.007
	Moreno FB, de Oliveira TM, Martil DE, Vicoti MM, Bezerra GA, Abrego JR, Cavada BS, Filgueira de Azevedo W Jr. Identification of a new quaternary association for legume lectins. J. Struct. Biol. 161 2008 133-43 [PubMed: 18068379] http://dx.doi.org/10.1016/j.jsb.2007.10.002
	Kulkarni KA, Katiyar S, Surolia A, Vijayan M, Suguna K. Structure and sugar-specificity of basic winged-bean lectin: structures of new disaccharide complexes and a comparative study with other known disaccharide complexes of the lectin. Acta Crystallogr. D Biol. Crystallogr. D64 2008 730-7 [PubMed: 18566508] http://dx.doi.org/10.1107/S0907444908011323

InterPro 23.1