LDL-receptor-related protein-associated protein

LDL-receptor-related protein-associated protein

Low density lipoprotein receptor-related protein associated protein 1
PDB rendering based on 1lre.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; A2MRAP; A2RAP; HBP44; MRAP; MYP23; RAP; alpha-2-MRAP
External IDs GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search
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
Alpha-2-MRAP_C
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]

Contents

  • Function 1
  • Interactions 2
  • References 3
  • Further reading 4
  • External links 5

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

  1. ^ Striekland DK, Ashcom JD, Williams S, Battey F, Behre E, McTigue K, Battey JF, Argraves WS (July 1991). "Primary structure of alpha 2-macroglobulin receptor-associated protein. Human homologue of a Heymann nephritis antigen". J. Biol. Chem. 266 (20): 13364–9.  
  2. ^ Korenberg JR, Argraves KM, Chen XN, Tran H, Strickland DK, Argraves WS (July 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.  
  3. ^ "Entrez Gene: LRPAP1 low density lipoprotein receptor-related protein associated protein 1". 
  4. ^ Nielsen PR, Ellgaard L, Etzerodt M, Thogersen HC, Poulsen FM (July 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.  
  5. ^ Lou, Xiaojing; McQuistan Tammie; Orlando Robert A; Farquhar Marilyn Gist (April 2002). "GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function". J. Am. Soc. Nephrol. (United States) 13 (4): 918–27.  
  6. ^ Orlando, R A; Farquhar M G (April 1994). "Functional domains of the receptor-associated protein (RAP)".  

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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Orlando RA, Farquhar MG (1994). "Functional domains of the receptor-associated protein (RAP).". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 3161–5.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  

External links

  • LDL-Receptor Related Protein-Associated Protein at the US National Library of Medicine Medical Subject Headings (MeSH)

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