Summary: Protease inhibitor/seed storage/LTP family
This is the Wikipedia entry entitled "Plant lipid transfer proteins". More...
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Plant lipid transfer proteins Edit Wikipedia article
|Plant lipid transfer protein/seed storage/trypsin-alpha amylase inhibitor|
Plant lipid transfer proteins, also known as plant LTPs or PLTPs, are a group of highly-conserved proteins of about 9kDa found in higher plant tissues. As its name implies, lipid transfer proteins are responsible for the shuttling of phospholipids and other fatty acid groups between cell membranes. LTPs are also able to bind acyl groups.
Plant lipid transfer proteins share the same structural domain with seed storage proteins and trypsin-alpha amylase inhibitors. The domain forms a four-helical bundle in a right-handed superhelix with a folded leaf topology, which is stabilised by disulfide bonds, and which has an internal cavity.
There is no sequence similarity between animal and plant LTPs. In animals, cholesterylester transfer protein (CETP), also called plasma lipid transfer protein, is a plasma protein that facilitates the transport of cholesteryl esters and triglycerides between the lipoproteins.
Role in human health
PLTPs are pan-allergens,   and may be directly responsible for cases of food allergy. Pru p 3, the major allergen from peach, is a 9-kDa allergen belonging to the family of lipid-transfer proteins. 
They are used as antioxidants and prevent diseases.
Role in plant biology
These proteins in plants may be involved in:
- cutin biosynthesis
- surface wax formation
- pathogen defense reactions
- for adaptation of plants to environmental changes
- Bonvin AM, Lyu PC, Samuel D, Cheng CS, Lin KF, Liu YN, Hsu ST (2005). "Characterization and structural analyses of nonspecific lipid transfer protein 1 from mung bean". Biochemistry 44 (15): –. doi:10.1021/bi047608v. PMID 15823028.
- Bruix M, Santoro J, Rico M, Gimenez-Gallego G, Pantoja-Uceda D (2003). "Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis". Biochemistry 42 (47): –. doi:10.1021/bi0352217. PMID 14636051.
- Fukuyama K, Oda Y, Morimoto T, Matsunaga T, Miyazaki T (1997). "Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 A resolution". Biochemistry 36 (44): –. doi:10.1021/bi971307m. PMID 9354618.
- Betzel C, Srinivasan A, Singh TP, Gourinath S, Alam N (2000). "Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution". Acta Crystallogr. D 56: –. doi:10.1107/s0907444999016601. PMID 10713515.
- http://www.food-allergens.de/symposium-2-4/peach/peach-allergens.htm Peach allergy, M.Besler et al.
- "Science Direct".
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Protease inhibitor/seed storage/LTP family Provide feedback
This family is composed of trypsin-alpha amylase inhibitors, seed storage proteins and lipid transfer proteins from plants.
Rico M, Bruix M, Gonzalez C, Monsalve RI, Rodriguez R; , Biochemistry 1996;35:15672-15682.: 1H NMR assignment and global fold of napin BnIb, a representative 2S albumin seed protein. PUBMED:8961930 EPMC:8961930
Internal database links
|Similarity to PfamA using HHSearch:||Gliadin LTP_2 Hydrophob_seed|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry 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].
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
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We make a range of alignments for each Pfam-A family:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Author:||Bateman A, Finn RD, Griffiths-Jones SR|
|Number in seed:||187|
|Number in full:||1632|
|Average length of the domain:||103.10 aa|
|Average identity of full alignment:||21 %|
|Average coverage of the sequence by the domain:||68.27 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Tryp_alpha_amyl domain has been found. There are 52 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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