Summary: Myelin proteolipid protein (PLP or lipophilin)
This is the Wikipedia entry entitled "Myelin proteolipid protein". More...
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Myelin proteolipid protein Edit Wikipedia article
|Myelin proteolipid protein (PLP or lipophilin)|
Myelin proteolipid protein (PLP or lipophilin) is the major myelin protein from the central nervous system (CNS). It plays an important role in the formation or maintenance of the multilamellar structure of myelin. The myelin sheath is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the velocity of axonal impulse conduction.
In man point mutations in PLP are the cause of Pelizaeus-Merzbacher disease (PMD), a neurologic disorder of myelin metabolism. In animals dismyelinating diseases such as mouse 'jimpy' or dog 'shaking pup' are also caused by mutations in PLP.
PLP is a highly conserved hydrophobic protein of 276 to 280 amino acids which seems to contain four transmembrane segments, two disulfide bonds and which covalently binds lipids (at least six palmitate groups in mammals). PLP is highly related to GPM6A, a neuronal membrane glycoprotein.
Human proteins containing this domain
- Dautigny A, Popot JL, Pham Dinh D (1991). "Major Myelin proteolipid: the 4-alpha-helix topology". J. Membr. Biol. 120 (3): 233–246. doi:10.1007/BF01868534. PMID 1711121.
- Kitamura K, Sakamoto Y, Yoshimura K, Nishijima T, Uyemura K (1987). "Complete amino acid sequence of PO protein in bovine peripheral nerve myelin". J. Biol. Chem. 262 (9): 4208–4214. PMID 2435734.
- Stoffel W, Schliess F (1991). "Evolution of the myelin integral membrane proteins of the central nervous system". Biol. Chem. Hoppe-Seyler 372 (9): 865–874. doi:10.1515/bchm3.1991.372.2.865. PMID 1722981.
- Weimbs T, Sto ffel W (1992). "Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP". Biochemistry 31 (49): 12289–12296. doi:10.1021/bi00164a002. PMID 1281423.
- Yan Y, Lagenaur C, Narayanan V (1993). "Molecular cloning of M6: identification of a PLP/DM20 gene family". Neuron 11 (3): 423–431. doi:10.1016/0896-6273(93)90147-J. PMID 8398137.
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External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001614
The myelin sheath is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the velocity of axonal impulse conduction [PUBMED:2435734]. Myelin proteolipid protein (PLP or lipophilin) [PUBMED:1711121] is the major myelin protein from the central nervous system (CNS). It probably plays an important role in the formation or maintenance of the multilamellar structure of myelin. In man point mutations in PLP are the cause of Pelizaeus-Merzbacher disease (PMD), a neurologic disorder of myelin metabolism. In animals dismyelinating diseases such as mouse 'jimpy' (jp), rat md, or dog 'shaking pup' are also caused by mutations in PLP.
PLP is a highly conserved [PUBMED:1722981] hydrophobic protein of 276 to 280 amino acids which seems to contain four transmembrane segments, two disulphide bonds and which covalently binds lipids (at least six palmitate groups in mammals) [PUBMED:1281423].
PLP is highly related to M6, a neuronal membran glycoprotein [PUBMED:8398137].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||integral to membrane (GO:0016021)|
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Curation and family details
|Author:||Finn RD, Bateman A|
|Number in seed:||7|
|Number in full:||395|
|Average length of the domain:||203.20 aa|
|Average identity of full alignment:||47 %|
|Average coverage of the sequence by the domain:||86.95 %|
|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:||14|
|Download:||download the raw HMM for this family|
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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 Myelin_PLP domain has been found. There are 1 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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