LDL-receptor-related protein associated protein

Low density lipoprotein receptor-related protein associated protein 1
PDB rendering based on 1lre.
Available structures PDB 1LRE, 1NRE, 1OP1, 1OV2, 2FCW, 2FTU, 2FYL, 2P01, 2P03
Identifiers
Symbols	LRPAP1; A2MRAP; A2RAP; HBP44; MRAP; RAP
External IDs	OMIM: 104225 MGI: 96829 HomoloGene: 37612 GeneCards: LRPAP1 Gene
Gene Ontology Molecular function • asialoglycoprotein receptor activity • heparin binding • lipase binding • receptor antagonist activity • low-density lipoprotein particle receptor binding • unfolded protein binding • very-low-density lipoprotein particle receptor binding Cellular component • cytoplasm • endoplasmic reticulum • plasma membrane • cell surface • integral to membrane • vesicle • rough endoplasmic reticulum lumen Biological process • protein folding • negative regulation of signal transduction • negative regulation of very-low-density lipoprotein particle clearance • vesicle-mediated transport • negative regulation of protein binding Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4043	16976
Ensembl	ENSG00000163956	ENSMUSG00000029103
UniProt	P30533	P55302
RefSeq (mRNA)	NM_002337.3	NM_013587.2
RefSeq (protein)	NP_002328.1	NP_038615.2
Location (UCSC)	Chr 4: 3.51 – 3.53 Mb	Chr 5: 35.43 – 35.45 Mb
PubMed search	[1]	[2]

Alpha-2-MRAP_N

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
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

Alpha-2-MRAP_C

solution structure of domain 3 of rap
Identifiers
Symbol	Alpha-2-MRAP_C
Pfam	PF06401
InterPro	IPR010483
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

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.

Function

LRPAP1 is involved with trafficking of certain members of the LDL receptor family including LRP1 and LRP2. 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 know ligands for these receptors, and may prevent receptor aggregation and degradation in the endoplasmic reticulum, thereby acting as a molecular chaperone. 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.

Further reading

• Williams SE, Ashcom JD, Argraves WS, Strickland DK (1992). "A novel mechanism for controlling the activity of alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein. Multiple regulatory sites for 39-kDa receptor-associated protein.". J. Biol. Chem. 267 (13): 9035–40. PMID 1374383. 
• Kounnas MZ, Argraves WS, Strickland DK (1992). "The 39-kDa receptor-associated protein interacts with two members of the low density lipoprotein receptor family, alpha 2-macroglobulin receptor and glycoprotein 330.". J. Biol. Chem. 267 (29): 21162–6. PMID 1400426. 
• Striekland DK, Ashcom JD, Williams S, et al. (1991). "Primary structure of alpha 2-macroglobulin receptor-associated protein. Human homologue of a Heymann nephritis antigen.". J. Biol. Chem. 266 (20): 13364–9. PMID 1712782. 
• Herz J, Goldstein JL, Strickland DK, et al. (1991). "39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor.". J. Biol. Chem. 266 (31): 21232–8. PMID 1718973. 
• Furukawa T, Ozawa M, Huang RP, Muramatsu T (1990). "A heparin binding protein whose expression increases during differentiation of embryonal carcinoma cells to parietal endoderm cells: cDNA cloning and sequence analysis.". J. Biochem. 108 (2): 297–302. PMID 2229028. 
• Herz J, Hamann U, Rogne S, et al. (1989). "Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor.". EMBO J. 7 (13): 4119–27. PMC 455121. PMID 3266596. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=455121. 
• Zheng G, Bachinsky DR, Stamenkovic I, et al. (1994). "Organ distribution in rats of two members of the low-density lipoprotein receptor gene family, gp330 and LRP/alpha 2MR, and the receptor-associated protein (RAP).". J. Histochem. Cytochem. 42 (4): 531–42. PMID 7510321. 
• Orlando RA, Farquhar MG (1994). "Functional domains of the receptor-associated protein (RAP).". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 3161–5. doi:10.1073/pnas.91.8.3161. PMC 43535. PMID 7512726. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=43535. 
• Jou YS, Goold RD, Myers RM (1995). "Localization of the alpha 2-macroglobulin receptor-associated protein 1 gene (LRPAP1) and other gene fragments to human chromosome 4p16.3 by direct cDNA selection.". Genomics 24 (2): 410–3. doi:10.1006/geno.1994.1643. PMID 7535288. 
• Argraves KM, Battey FD, MacCalman CD, et al. (1995). "The very low density lipoprotein receptor mediates the cellular catabolism of lipoprotein lipase and urokinase-plasminogen activator inhibitor type I complexes.". J. Biol. Chem. 270 (44): 26550–7. doi:10.1074/jbc.270.44.26550. PMID 7592875. 
• Bu G, Geuze HJ, Strous GJ, Schwartz AL (1995). "39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein.". EMBO J. 14 (10): 2269–80. PMC 398334. PMID 7774585. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=398334. 
• Van Leuven F, Hilliker C, Serneels L, et al. (1995). "Cloning, characterization, and chromosomal localization to 4p16 of the human gene (LRPAP1) coding for the alpha 2-macroglobulin receptor-associated protein and structural comparison with the murine gene coding for the 44-kDa heparin-binding protein.". Genomics 25 (2): 492–500. doi:10.1016/0888-7543(95)80050-V. PMID 7789983. 
• Medh JD, Fry GL, Bowen SL, et al. (1995). "The 39-kDa receptor-associated protein modulates lipoprotein catabolism by binding to LDL receptors.". J. Biol. Chem. 270 (2): 536–40. doi:10.1074/jbc.270.2.536. PMID 7822276. 
• Korenberg JR, Argraves KM, Chen XN, et al. (1994). "Chromosomal localization of human genes for the LDL receptor family member glycoprotein 330 (LRP2) and its associated protein RAP (LRPAP1).". Genomics 22 (1): 88–93. doi:10.1006/geno.1994.1348. PMID 7959795. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Willnow TE, Rohlmann A, Horton J, et al. (1996). "RAP, a specialized chaperone, prevents ligand-induced ER retention and degradation of LDL receptor-related endocytic receptors.". EMBO J. 15 (11): 2632–9. PMC 450198. PMID 8654360. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=450198. 
• Jacobsen L, Madsen P, Moestrup SK, et al. (1997). "Molecular characterization of a novel human hybrid-type receptor that binds the alpha2-macroglobulin receptor-associated protein.". J. Biol. Chem. 271 (49): 31379–83. doi:10.1074/jbc.271.49.31379. PMID 8940146. 
• Bu G, Rennke S, Geuze HJ (1997). "ERD2 proteins mediate ER retention of the HNEL signal of LRP's receptor-associated protein (RAP).". J. Cell. Sci.. 110 ( Pt 1): 65–73. PMID 9010785. 
• Petersen CM, Nielsen MS, Nykjaer A, et al. (1997). "Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography.". J. Biol. Chem. 272 (6): 3599–605. doi:10.1074/jbc.272.6.3599. PMID 9013611. 
• Nielsen PR, Ellgaard L, Etzerodt M, et al. (1997). "The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein.". Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7521–5. doi:10.1073/pnas.94.14.7521. PMC 23854. PMID 9207124. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23854. 

External links

• MeSH LDL-Receptor+Related+Protein-Associated+Protein

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