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InterPro: IPR002557 Chitin binding protein, peritrophin-A

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2301 proteins

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Architectures
Accession List
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Accession

IPR002557 Chitin-bd_peritrophin-A

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01607	CBM_14	1991
PROSITE profile	PS50940	CHIT_BIND_II	2165
SMART	SM00494	ChtBD2	1992
SuperFamily	SSF57625	Chitin_bind_PerA	2097
Signatures in BioMart

InterPro Relationships Help

Found in

IPR012111 Hemolectin/hemocytin

GO Term annotation Help

Process

GO:0006030 chitin metabolic process

Function

GO:0008061 chitin binding

Component

GO:0005576 extracellular region

InterPro annotation

Entry Details in BioMart

Abstract

The Peritrophin-A domain is found in chitin binding proteins, particularly the peritrophic matrix proteins of insects and animal chitinases [1, 2, 3]. Copies of the domain are also found in some baculoviruses. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains [1].

Structural links Help

PDB - click here

SCOP: g.31.1.1 , g.31.1.2

CATH: 2.170.140.10

Database links Help

PROSITE doc: PDOC50940

PANDIT: PF01607

Blocks: IPB002557

Pfam Clan: CL0155.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002557

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O10336 Capsid-associated protein Vp91

P34504 Uncharacterized protein K04H4.2

Q13231 Chitotriosidase-1

Q91XA9 Acidic mammalian chitinase

Q9W5U2 Probable chitinase 3

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR007026	Domian of unknown function, DUF-CC
IPR001579	Glycoside hydrolase, chitinase active site
IPR006150	Cysteine-rich repeat
IPR013682	Viral capsid protein 91 N-terminal
IPR017853	Glycoside hydrolase, catalytic core
IPR002557	Chitin binding protein, peritrophin-A
IPR011583	Chitinase II
IPR001223	Glycoside hydrolase, family 18, catalytic domain
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Shen Z, Jacobs-Lorena M. A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression, and characterization. J. Biol. Chem. 273 17665-70 1998 [PubMed: 9651363] http://dx.doi.org/10.1074/jbc.273.28.17665
2.	Elvin CM, Vuocolo T, Pearson RD, East IJ, Riding GA, Eisemann CH, Tellam RL. Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina. cDNA and deduced amino acid sequences. J. Biol. Chem. 271 8925-35 1996 [PubMed: 8621536] http://dx.doi.org/10.1074/jbc.271.15.8925
3.	Casu R, Eisemann C, Pearson R, Riding G, East I, Donaldson A, Cadogan L, Tellam R. Antibody-mediated inhibition of the growth of larvae from an insect causing cutaneous myiasis in a mammalian host. Proc. Natl. Acad. Sci. U.S.A. 94 8939-44 1997 [PubMed: 9256413] http://dx.doi.org/10.1073/pnas.94.17.8939

Additional Reading Open in usermanual
	Tjoelker LW, Gosting L, Frey S, Hunter CL, Trong HL, Steiner B, Brammer H, Gray PW. Structural and functional definition of the human chitinase chitin-binding domain. J. Biol. Chem. 275 2000 514-20 [PubMed: 10617646] http://dx.doi.org/10.1074/jbc.275.1.514
	Suetake T, Tsuda S, Kawabata S, Miura K, Iwanaga S, Hikichi K, Nitta K, Kawano K. Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif. J. Biol. Chem. 275 2000 17929-32 [PubMed: 10770921] http://dx.doi.org/10.1074/jbc.C000184200
	Hemmi H, Ishibashi J, Tomie T, Yamakawa M. Structural basis for new pattern of conserved amino acid residues related to chitin-binding in the antifungal peptide from the coconut rhinoceros beetle Oryctes rhinoceros. J. Biol. Chem. 278 2003 22820-7 [PubMed: 12676931] http://dx.doi.org/10.1074/jbc.M301025200
	Gaines PJ, Walmsley SJ, Wisnewski N. Cloning and characterization of five cDNAs encoding peritrophin-A domains from the cat flea, Ctenocephalides felis. Insect Biochem. Mol. Biol. 33 2003 1061-73 [PubMed: 14563358] http://dx.doi.org/10.1016/S0965-1748(03)00096-1

InterPro 23.1