AAI

Plant lipid transfer protein / seed storage protein / trypsin-alpha amylase inhibitor domain family

• SMART accession number: SM00499
• Description: -
• Interpro abstract (IPR016140):

  This entry represents a structural domain consisting of 4-helices with a folded leaf topology, and forming a right-handed superhelix. This domain occurs in several proteins, including:

  • Plant lipid-transfer proteins, such as the non-specific lipid-transfer proteins ns-LTP1 and ns-LTP2 [ (PUBMED:10491104) (PUBMED:12011089) ].
  • Proteinase/alpha-amylase inhibitors, such as trypsin/alpha-amylase inhibitor RBI from Eleusine coracana (Indian finger millet) [ (PUBMED:9687373) ] and Hageman factor/amylase inhibitor from Zea mays (Maize) [ (PUBMED:9799488) ].
  • Seed storage proteins, such as napin from Brassica napus (Rape) [ (PUBMED:8961930) ] and 2S albumin from Ricinus communis (Castor bean) [ (PUBMED:14636051) ].

There are 14352 AAI domains in 14113 proteins in SMART's nrdb database.

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Wirtz KW
• Phospholipid transfer proteins.
• Annu Rev Biochem. 1991; 60: 73-99

• Gautier MF, Alary R, Joudrier P
• Cloning and characterization of a cDNA encoding the wheat (Triticum durum Desf.) CM16 protein.
• Plant Mol Biol. 1990; 14: 313-22

A Triticum durum cDNA library prepared from developing endosperm (22 days after flowering (DAF] was screened using synthetic oligonucleotide probes covering part of the CM3 and CM16 N-terminal protein sequences. A full-length cDNA clone (pTd78) encoding the CM16 protein (chloroform/methanol-soluble protein) was isolated and characterized. To our knowledge this is the first characterization of a clone coding for a wheat CM protein. The CM16 protein is synthesized as a preprotein with a signal peptide of 24 residues, the molecular weight of the mature protein being 13,438 Da. As other members of the cereal trypsin/alpha-amylase inhibitor family, the CM16 protein contains 10 cysteine residues, their position being well conserved. In developing endosperm the highest level of CM16 mRNA was detected at mid-maturation.

• Henrissat B, Popineau Y, Kader JC
• Hydrophobic-cluster analysis of plant protein sequences. A domain homology between storage and lipid-transfer proteins.
• Biochem J. 1988; 255: 901-5

Hydrophobic-cluster analysis was used to characterize a conserved domain located near the C-terminal amino acid sequence of wheat (Triticum aestivum) storage proteins. This domain was transformed into a linear template for a global search for similarities in over 5200 protein sequences. In addition to proteins that had already been found to exhibit homology to wheat storage proteins, a previously unreported homology was found with non-specific lipid-transfer proteins from castor bean (Ricinus communis) and from spinach (Spinacia oleracea) leaf. Hydrophobic-cluster analysis of various members of the present protein group clearly shows a typical domain structure where (i) variable and conserved domains are located along the sequence at precise positions, (ii) the conserved domains probably reflect a common ancestor, and (iii) the unique properties of a given protein (chain cut into subunits, repetitive domains, trypsin-inhibitor active site) are associated with the variable domains.

Structure (3D structures containing this domain)

3D Structures of AAI domains in PDB

PDB code	Title
1afh	LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES
1b1u	CRYSTAL STRUCTURE OF THE BIFUNCTIONAL INHIBITOR RAGI
1be2	LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE, NMR, 10 STRUCTURES
1bea	BIFUNCTIONAL HAGEMAN FACTOR/AMYLASE INHIBITOR FROM MAIZE
1bfa	RECOMBINANT BIFUNCTIONAL HAGEMAN FACTOR/AMYLASE INHIBITOR FROM MAIZE
1bip	BIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI (ELEUSINE CORACANA GAERTNERI)
1bv2	LIPID TRANSFER PROTEIN FROM RICE SEEDS, NMR, 14 STRUCTURES
1bwo	THE CRYSTAL STRUCTURE OF WHEAT NON-SPECIFIC TRANSFER PROTEIN COMPLEXED WITH TWO MOLECULES OF PHOSPHOLIPID AT 2.1 A RESOLUTION
1cz2	SOLUTION STRUCTURE OF WHEAT NS-LTP COMPLEXED WITH PROSTAGLANDIN B2.
1fk0	STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH CAPRIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
1fk1	STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH LAURIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
1fk2	STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH MYRISTIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
1fk3	STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH PALMITOLEIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
1fk4	STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH STEARIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
1fk5	STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH OLEIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
1fk6	STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH ALPHA-LINOLENIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
1fk7	STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH RICINOLEIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
1gh1	NMR STRUCTURES OF WHEAT NONSPECIFIC LIPID TRANSFER PROTEIN
1hss	0.19 ALPHA-AMYLASE INHIBITOR FROM WHEAT
1hyp	CRYSTAL STRUCTURE OF HYDROPHOBIC PROTEIN FROM SOYBEAN; A MEMBER OF A NEW CYSTINE-RICH FAMILY
1jtb	LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COENZYME A, NMR, 16 STRUCTURES
1l6h	Solution Structure of Plant nsLTP2 purified from Rice (oryza Sativa)
1lip	BARLEY LIPID TRANSFER PROTEIN (NMR, 4 STRUCTURES)
1mid	Non-specific lipid transfer protein 1 from barley in complex with L-alfa-lysophosphatidylcholine, Laudoyl
1mzl	MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN
1mzm	MAIZE NONSPECIFIC LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE
1n89	Solution structure of a liganded type 2 wheat non-specific Lipid Transfer Protein
1pnb	STRUCTURE OF NAPIN BNIB, NMR, 10 STRUCTURES
1psy	STRUCTURE OF RicC3, NMR, 20 STRUCTURES
1rzl	RICE NONSPECIFIC LIPID TRANSFER PROTEIN
1s6d	Structure in solution of a methionine-rich 2S Albumin protein from Sunflower Seed
1siy	NMR structure of mung bean non-specific lipid transfer protein 1
1sm7	Solution structure of the recombinant pronapin precursor, BnIb.
1t12	Solution Structure of a new LTP1
1tmq	STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR
1tuk	Crystal stucture of liganted type 2 non specific lipid transfer protein from wheat
1uva	Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza sativa
1uvb	Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza sativa
1uvc	Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza sativa
1w2q	allergen arah6 from peanut (Arachis hypogaea)
2alg	Crystal structure of peach Pru p3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens
2b5s	Crystal structure of peach Pru p3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens
2ds2	Crystal structure of mabinlin II
2lvf	Solution structure of the Brazil Nut 2S albumin Ber e 1
2mal	Solution structure of Lipid Transfer Protein from Lentil Lens Culinaris
2n2z	2N2Z
2n81	2N81
2rkn	X-ray structure of the self-defense and signaling protein DIR1 from Arabidopsis taliana
3gsh	Three-dimensional structure of a post translational modified barley LTP1
3ob4	MBP-fusion protein of the major peanut allergen Ara h 2
4cvw	4CVW
4xuw	4XUW
5dom	5DOM

Links (links to other resources describing this domain)

• PROSITE: CEREAL_TRYP_AMYL_INH
• PFAM: tryp_alpha_amyl
• INTERPRO: IPR016140