LDL-receptor-related protein-associated protein

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Low density lipoprotein receptor-related protein associated protein 1
Protein LRPAP1 PDB 1lre.png
PDB rendering based on 1lre.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols LRPAP1 ; A2MRAP; A2RAP; HBP44; MRAP; MYP23; RAP; alpha-2-MRAP
External IDs OMIM104225 MGI96829 HomoloGene37612 GeneCards: LRPAP1 Gene
RNA expression pattern
PBB GE LRPAP1 201186 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 4043 16976
Ensembl ENSG00000163956 ENSMUSG00000029103
UniProt P30533 P55302
RefSeq (mRNA) NM_002337 NM_013587
RefSeq (protein) NP_002328 NP_038615
Location (UCSC) Chr 4:
3.51 – 3.53 Mb
Chr 5:
35.09 – 35.11 Mb
PubMed search [1] [2]
Alpha-2-MRAP_N
PDB 2fyl EBI.jpg
haddock model of the complex between double module of lrp, cr56, and first domain of receptor associated protein, rap-d1.
Identifiers
Symbol Alpha-2-MRAP_N
Pfam PF06400
InterPro IPR009066
SCOP 1lre
SUPERFAMILY 1lre
Alpha-2-MRAP_C
PDB 2ftu EBI.jpg
solution structure of domain 3 of rap
Identifiers
Symbol Alpha-2-MRAP_C
Pfam PF06401
InterPro IPR010483

Low density lipoprotein receptor-related protein-associated protein 1 also known as LRPAP1 or RAP is a chaperone protein which in humans is encoded by the LRPAP1 gene.[1][2]

Function

LRPAP1 is involved with trafficking of certain members of the LDL receptor family including LRP1 and LRP2.[3] It is a glycoprotein that binds to the alpha-2-macroglobulin receptor, as well as to other members of the low density lipoprotein receptor family. It acts to inhibit the binding of all known ligands for these receptors, and may prevent receptor aggregation and degradation in the endoplasmic reticulum, thereby acting as a molecular chaperone.[4] It may be under the regulatory control of calmodulin, since it is able to bind calmodulin and be phosphorylated by calmodulin-dependent kinase II.

Interactions

LDL-receptor-related protein-associated protein has been shown to interact with LRP2.[5][6]

References

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Further reading

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External links

This article incorporates text from the public domain Pfam and InterPro IPR010483


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