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0  structures 56  species 0  interactions 407  sequences 6  architectures

Family: BURP (PF03181)

Summary: BURP domain

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BURP domain Edit Wikipedia article

BURP
Identifiers
Symbol BURP
Pfam PF03181
InterPro IPR004873

In molecular biology, the BURP domain is a ~230-amino acid protein domain, which has been named for the four members of the group initially identified, BNM2, USP, RD22, and PG1beta. It is found in the C-terminal part of a number of plant cell wall proteins, which are defined not only by the BURP domain, but also by the overall similarity in their modular construction. The BURP domain proteins consists of either three or four modules: (i) an N-terminal hydrophobic domain - a presumptive transit peptide, joined to (ii) a short conserved segment or other short segment, (iii) an optional segment consisting of repeated units which is unique to each member, and (iv) the C-terminal BURP domain. Although the BURP domain proteins share primary structural features, their expression patterns and the conditions under which they are expressed differ. The presence of the conserved BURP domain in diverse plant proteins suggests an important and fundamental functional role for this domain.[1] It is possible that the BURP domain represents a general motif for localization of proteins within the cell wall matrix. The other structural domains associated with the BURP domain may specify other target sites for intermolecular interactions.[2]

Some proteins known to contain a BURP domain are listed below:[1][2][3]

  • Field bean USPs, abundant non-storage seed proteins with unknown function.
  • Soybean USP-like proteins ADR6 (or SALI5-4A), an auxin-repressible, aluminium-inducible protein and SALI3-2, a protein that is up-regulated by aluminium.
  • Maize ZRP2, a protein of unknown function in cortex parenchyma.
  • Cereal RAFTIN. It is essential specifically for the maturation phase of pollen development.

References[edit]

  1. ^ a b Hattori J, Boutilier KA, van Lookeren Campagne MM, Miki BL (September 1998). "A conserved BURP domain defines a novel group of plant proteins with unusual primary structures". Mol. Gen. Genet. 259 (4): 424–8. PMID 9790599. 
  2. ^ a b Batchelor AK, Boutilier K, Miller SS, Hattori J, Bowman LA, Hu M, Lantin S, Johnson DA, Miki BL (August 2002). "SCB1, a BURP-domain protein gene, from developing soybean seed coats". Planta 215 (4): 523–32. doi:10.1007/s00425-002-0798-1. PMID 12172833. 
  3. ^ Wang A, Xia Q, Xie W, Datla R, Selvaraj G (November 2003). "The classical Ubisch bodies carry a sporophytically produced structural protein (RAFTIN) that is essential for pollen development". Proc. Natl. Acad. Sci. U.S.A. 100 (24): 14487–92. doi:10.1073/pnas.2231254100. PMC 283618. PMID 14612572. 

This article incorporates text from the public domain Pfam and InterPro IPR004873

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

BURP domain Provide feedback

The BURP domain is found at the C-terminus of several different plant proteins. It was named after the proteins in which it was first identified: the BNM2 clone-derived protein from Brassica napus O65009; USPs and USP-like proteins P21746 P21747 Q06765 O24482; RD22 from Arabidopsis thaliana Q08298; and PG1beta from Lycopersicon esculentum Q40161. This domain is around 230 amino acid residues long. It possesses the following conserved features: two phenylalanine residues at its N-terminus; two cysteine residues; and four repeated cysteine-histidine motifs, arranged as: CH-X(10)-CH-X(25-27)-CH-X(25-26)-CH, where X can be any amino acid [1]. The function of this domain is unknown.

Literature references

  1. Hattori J, Boutilier KA, van Lookeren Campagne MM, Miki BL; , Mol Gen Genet 1998;259:424-428.: A conserved BURP domain defines a novel group of plant proteins with unusual primary structures. PUBMED:9790599 EPMC:9790599


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004873

The BURP domain was named after the proteins in which it was first identified: BNM2, USP, RD22, and PG1beta. It is found in the C terminus of a number of plant cell wall proteins, which are defined not only by the BURP domain, but also by the overall similarity in their modular construction. The BURP domain-containing proteins consists of either three or four modules: (i) an N-terminal hydrophobic domain - a presumptive transit peptide, joined to (ii) a short conserved segment or other short segment, (iii) an optional segment consisting of repeated units which is unique to each member, and (iv) the C-terminal BURP domain. Although the BURP domain proteins share primary structural features, their expression patterns and the conditions under which they are expressed differ. The presence of the conserved BURP domain in diverse plant proteins suggests an important and fundamental functional role for this domain [PUBMED:9790599]. It is possible that the BURP domain represents a general motif for localization of proteins within the cell wall matrix. The other structural domains associated with the BURP domain may specify other target sites for intermolecular interactions [PUBMED:12172833].

Some proteins known to contain a BURP domain are listed below [PUBMED:9790599, PUBMED:12172833, PUBMED:14612572]:

  • Brassica protein BNM2, which is expressed during the induction of microspore embryogenesis.
  • Field bean USPs, abundant non-storage seed proteins with unknown function.
  • Soybean USP-like proteins ADR6 (or SALI5-4A), an auxin-repressible, aluminium-inducible protein and SALI3-2, a protein that is up-regulated by aluminium.
  • Soybean seed coat BURP-domain protein 1 (SCB1). It might play a role in the differentiation of the seed coat parenchyma cells.
  • Arabidopsis RD22 drought induced protein.
  • Maize ZRP2, a protein of unknown function in cortex parenchyma.
  • Tomato PG1beta, the beta-subunit of polygalacturonase isozyme 1 (PG1), which is expressed in ripening fruits.
  • Cereal RAFTIN. It is essential specifically for the maturation phase of pollen development.

Domain organisation

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Meta
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RP35
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RP55
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  Seed
(28)
Full
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Representative proteomes NCBI
(416)
Meta
(0)
RP15
(15)
RP35
(102)
RP55
(151)
RP75
(178)
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Seed source: Pfam-B_1432 (release 6.5)
Previous IDs: none
Type: Family
Author: Mifsud W
Number in seed: 28
Number in full: 407
Average length of the domain: 183.20 aa
Average identity of full alignment: 34 %
Average coverage of the sequence by the domain: 55.05 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 21.0 21.0
Noise cut-off 20.3 20.6
Model length: 216
Family (HMM) version: 10
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