Summary: PLAT/LH2 domain
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This is the Wikipedia entry entitled "PLAT domain". More...
PLAT domain Edit Wikipedia article
PLAT/LH2 domain | |||||||||
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![]() Structure of the lipase-procolipase complex.[1] | |||||||||
Identifiers | |||||||||
Symbol | PLAT | ||||||||
Pfam | PF01477 | ||||||||
InterPro | IPR001024 | ||||||||
SMART | SM00308 | ||||||||
PROSITE | PDOC50095 | ||||||||
SCOPe | 1lpa / SUPFAM | ||||||||
OPM superfamily | 221 | ||||||||
OPM protein | 3swz | ||||||||
CDD | cd00113 | ||||||||
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In molecular biology the PLAT domain is a protein domain that is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain[2] or LH2 (Lipoxygenase homology) domain.[3] The known structure of pancreatic lipase shows this domain binds to procolipase Pfam PF01114, which mediates membrane association.
This domain is found in a variety of membrane or lipid associated proteins. It forms a beta-sandwich composed of two β-sheets of four β-strands each.[2][4][5]
Human proteins containing this domain
ALOX12; ALOX12B; ALOX12P2; ALOX15; ALOX15B; ALOX5; ALOXE3; LIPC; LIPG; LOXHD1; LPL; PKD1; PKD1L1; PKD1L2; PKD1L3; PKDREJ; PNLIP; PNLIPRP1; PNLIPRP2; PNLIPRP3; RAB6IP1;
References
- ^ van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C (April 1993). "Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography". Nature. 362 (6423): 814–20. doi:10.1038/362814a0. PMID 8479519.
- ^ a b Bateman A, Sandford R (1999). "The PLAT domain: a new piece in the PKD1 puzzle". Curr. Biol. 9 (16): R588–90. doi:10.1016/S0960-9822(99)80380-7. PMID 10469604.
- ^ Ponting CP, Hofmann K, Bork P (August 1999). "A latrophilin/CL-1-like GPS domain in polycystin-1". Curr. Biol. 9 (16): R585–8. doi:10.1016/S0960-9822(99)80379-0. PMID 10469603.
- ^ Delrieu I, Waller CC, Mota MM, Grainger M, Langhorne J, Holder AA (2002). "PSLAP, a protein with multiple adhesive motifs, is expressed in Plasmodium falciparum gametocytes". Mol. Biochem. Parasitol. 121 (1): 11–20. doi:10.1016/S0166-6851(02)00016-6. PMID 11985859.
- ^ Minor W, Tomchick DR, Phan P, Cymborowski M, Holman TR (2001). "Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1". Biochemistry. 40 (25): 7509–7517. doi:10.1021/bi002893d. PMID 11412104.
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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.
PLAT/LH2 domain Provide feedback
This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase PF01114 which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.
Internal database links
SCOOP: | ATS3 |
Similarity to PfamA using HHSearch: | ATS3 |
External database links
HOMSTRAD: | lipase lipoxygenase |
PROSITE profile: | PS50095 |
SCOP: | 1lpa |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001024
This entry represents a domain found in a variety of membrane or lipid associated proteins. It is known as the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain, is found in a variety of membrane or lipid associated proteins. Structurally, this domain forms a beta-sandwich composed of two sheets of four strands each [PUBMED:10469604, PUBMED:11985859, PUBMED:11412104]. The most highly conserved regions coincide with the beta-strands, with most of the highly conserved residues being buried within the protein. An exception to this is a surface lysine or arginine that occurs on the surface of the fifth beta-strand of the eukaryotic domains. In pancreatic lipase, the lysine in this position forms a salt bridge with the procolipase protein. The conservation of a charged surface residue may indicate the location of a conserved ligand-binding site. It is thought that this domain may mediate membrane attachment via other protein binding partners.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | protein binding (GO:0005515) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (84) |
Full (12687) |
Representative proteomes | UniProt (18985) |
NCBI (32513) |
Meta (15) |
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RP15 (2293) |
RP35 (5005) |
RP55 (9098) |
RP75 (12835) |
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HTML | |||||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (84) |
Full (12687) |
Representative proteomes | UniProt (18985) |
NCBI (32513) |
Meta (15) |
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RP15 (2293) |
RP35 (5005) |
RP55 (9098) |
RP75 (12835) |
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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.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Bateman A |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 84 |
Number in full: | 12687 |
Average length of the domain: | 110.40 aa |
Average identity of full alignment: | 22 % |
Average coverage of the sequence by the domain: | 18.56 % |
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: | 117 | ||||||||||||
Family (HMM) version: | 24 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
There are 14 interactions for this family. More...
Lipoxygenase Colipase PLAT Colipase_C Zn_dep_PLPC Colipase Lipase Lipase RUN Colipase_C Catalase Lipoxygenase Catalase Zn_dep_PLPCStructures
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 PLAT domain has been found. There are 124 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 sequence.
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