Summary: Remorin, C-terminal region
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Remorin, C-terminal region Provide feedback
Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.
Literature references
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Reymond P, Kunz B, Paul-Pletzer K, Grimm R, Eckerskorn C, Farmer EE; , Plant Cell 1996;8:2265-2276.: Cloning of a cDNA encoding a plasma membrane-associated, uronide binding phosphoprotein with physical properties similar to viral movement proteins. PUBMED:8989883 EPMC:8989883
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Raffaele S, Bayer E, Lafarge D, Cluzet S, German Retana S, Boubekeur T, Leborgne-Castel N, Carde JP, Lherminier J, Noirot E, Satiat-Jeunemaitre B, Laroche-Traineau J, Moreau P, Ott T, Maule AJ, Reymond P, Simon-Plas F, Farmer EE, Bessoule JJ, Mongrand S;, Plant Cell. 2009;21:1541-1555.: Remorin, a solanaceae protein resident in membrane rafts and plasmodesmata, impairs potato virus X movement. PUBMED:19470590 EPMC:19470590
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Lefebvre B, Timmers T, Mbengue M, Moreau S, Herve C, Toth K, Bittencourt-Silvestre J, Klaus D, Deslandes L, Godiard L, Murray JD, Udvardi MK, Raffaele S, Mongrand S, Cullimore J, Gamas P, Niebel A, Ott T;, Proc Natl Acad Sci U S A. 2010;107:2343-2348.: A remorin protein interacts with symbiotic receptors and regulates bacterial infection. PUBMED:20133878 EPMC:20133878
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Jarsch IK, Ott T;, Mol Plant Microbe Interact. 2011;24:7-12.: Perspectives on remorin proteins, membrane rafts, and their role during plant-microbe interactions. PUBMED:21138374 EPMC:21138374
This tab holds annotation information from the InterPro database.
InterPro entry IPR005516
Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible [PUBMED:8989883].
Domain organisation
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Seed (96) |
Full (2474) |
Representative proteomes | UniProt (3420) |
NCBI (4847) |
Meta (0) |
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RP15 (109) |
RP35 (1241) |
RP55 (1971) |
RP75 (2451) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (96) |
Full (2474) |
Representative proteomes | UniProt (3420) |
NCBI (4847) |
Meta (0) |
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RP15 (109) |
RP35 (1241) |
RP55 (1971) |
RP75 (2451) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Curation and family details
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Curation
Seed source: | Pfam-B_1798 (release 7.0) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Farmer EE |
Number in seed: | 96 |
Number in full: | 2474 |
Average length of the domain: | 101.40 aa |
Average identity of full alignment: | 34 % |
Average coverage of the sequence by the domain: | 28.89 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 107 | ||||||||||||
Family (HMM) version: | 14 | ||||||||||||
Download: | download the raw HMM for this family |
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