Summary: Alpha-2-macroglobulin RAP, N-terminal domain
This is the Wikipedia entry entitled "LDL-receptor-related protein associated protein". More...
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LDL-receptor-related protein associated protein Edit Wikipedia article
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Alpha-2-macroglobulin RAP, N-terminal domain Provide feedback
The alpha-2-macroglobulin receptor-associated protein (RAP) is a intracellular glycoprotein that binds to the 2-macroglobulin receptor and other members of the low density lipoprotein receptor family. The protein inhibits binding of all currently known ligands of these receptors . The N-terminal domain is predominately alpha helical . Two different studies have provided conflicted domain boundaries [2,3].
Nielsen PR, Ellgaard L, Etzerodt M, Thogersen HC, Poulsen FM; , Proc Natl Acad Sci U S A 1997;94:7521-7525.: The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein. PUBMED:9207124 EPMC:9207124
Ellgaard L, Holtet TL, Nielsen PR, Etzerodt M, Gliemann J, Thogersen HC; , Eur J Biochem 1997;244:544-551.: Dissection of the domain architecture of the alpha2macroglobulin-receptor-associated protein. PUBMED:9119022 EPMC:9119022
Warshawsky I, Bu G, Schwartz AL; , J Biol Chem 1993;268:22046-22054.: Identification of domains on the 39-kDa protein that inhibit the binding of ligands to the low density lipoprotein receptor-related protein. PUBMED:7691821 EPMC:7691821
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR009066
The alpha-2-macroglobulin receptor-associated protein (RAP) is a glycoprotein that binds to the alpha-2-macroglobulin receptor, as well as to other members of the low density lipoprotein receptor family (INTERPRO). RAP acts to inhibit the binding of all know ligands for these receptors, and may prevent receptor aggregation and degradation in the endoplasmic reticulum, thereby acting as a molecular chaperone [PUBMED:9207124]. RAP may be under the regulatory control of calmodulin, since it is able to bind calmodulin and be phosphorylated by calmodulin-dependent kinase II (INTERPRO).
RAP is comprised of three domains. Both domains 1 and 3 are involved in binding to the alpha-2-macroglobulin receptor, while domain 1 is also involved in inhibiting the binding of activated alpha-2-macroglobulin (INTERPRO). Structural studies have revealed the RAP domain 1 to be comprised of a partly opened bundle of three helices, the first one being shorter than the other two.
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_44514 (release 9.0)|
|Number in seed:||10|
|Number in full:||108|
|Average length of the domain:||113.90 aa|
|Average identity of full alignment:||50 %|
|Average coverage of the sequence by the domain:||33.65 %|
|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:||6|
|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 Alpha-2-MRAP_N domain has been found. There are 7 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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