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 LRPAP1 ; A2MRAP; A2RAP; HBP44; MRAP; MYP23; RAP; alpha-2-MRAP
External IDs OMIM: 104225 MGI: 96829 HomoloGene: 37612 GeneCards: LRPAP1 Gene
RNA expression pattern
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
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]

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. ↑ Strickland DK, Ashcom JD, Williams S, Battey F, Behre E, McTigue K, Battey JF, Argraves WS (Jul 1991). "Primary structure of alpha 2-macroglobulin receptor-associated protein. Human homologue of a Heymann nephritis antigen". The Journal of Biological Chemistry 266 (20): 13364–9. PMID 1712782.
  2. ↑ Korenberg JR, Argraves KM, Chen XN, Tran H, Strickland DK, Argraves WS (Jul 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.
  3. ↑ "Entrez Gene: LRPAP1 low density lipoprotein receptor-related protein associated protein 1".
  4. ↑ Nielsen PR, Ellgaard L, Etzerodt M, Thogersen HC, Poulsen FM (Jul 1997). "The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein". Proceedings of the National Academy of Sciences of the United States of America 94 (14): 7521–5. doi:10.1073/pnas.94.14.7521. PMC 23854. PMID 9207124.
  5. ↑ Lou X, McQuistan T, Orlando RA, Farquhar MG (Apr 2002). "GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function". Journal of the American Society of Nephrology 13 (4): 918–27. PMID 11912251.
  6. ↑ Orlando RA, Farquhar MG (Apr 1994). "Functional domains of the receptor-associated protein (RAP)". Proceedings of the National Academy of Sciences of the United States of America 91 (8): 3161–5. doi:10.1073/pnas.91.8.3161. PMC 43535. PMID 7512726.

Further reading

  • Williams SE, Ashcom JD, Argraves WS, Strickland DK (May 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". The Journal of Biological Chemistry 267 (13): 9035–40. PMID 1374383. 
  • Kounnas MZ, Argraves WS, Strickland DK (Oct 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". The Journal of Biological Chemistry 267 (29): 21162–6. PMID 1400426. 
  • Strickland DK, Ashcom JD, Williams S, Battey F, Behre E, McTigue K, Battey JF, Argraves WS (Jul 1991). "Primary structure of alpha 2-macroglobulin receptor-associated protein. Human homologue of a Heymann nephritis antigen". The Journal of Biological Chemistry 266 (20): 13364–9. PMID 1712782. 
  • Herz J, Goldstein JL, Strickland DK, Ho YK, Brown MS (Nov 1991). "39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor". The Journal of Biological Chemistry 266 (31): 21232–8. PMID 1718973. 
  • Furukawa T, Ozawa M, Huang RP, Muramatsu T (Aug 1990). "A heparin binding protein whose expression increases during differentiation of embryonal carcinoma cells to parietal endoderm cells: cDNA cloning and sequence analysis". Journal of Biochemistry 108 (2): 297–302. PMID 2229028. 
  • Herz J, Hamann U, Rogne S, Myklebost O, Gausepohl H, Stanley KK (Dec 1988). "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". The EMBO Journal 7 (13): 4119–27. PMC 455121. PMID 3266596. 
  • Zheng G, Bachinsky DR, Stamenkovic I, Strickland DK, Brown D, Andres G, McCluskey RT (Apr 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)". The Journal of Histochemistry and Cytochemistry 42 (4): 531–42. doi:10.1177/42.4.7510321. PMID 7510321. 
  • Orlando RA, Farquhar MG (Apr 1994). "Functional domains of the receptor-associated protein (RAP)". Proceedings of the National Academy of Sciences of the United States of America 91 (8): 3161–5. doi:10.1073/pnas.91.8.3161. PMC 43535. PMID 7512726. 
  • Jou YS, Goold RD, Myers RM (Nov 1994). "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, McCrae KR, Gåfvels M, Kozarsky KF, Chappell DA, Strauss JF, Strickland DK (Nov 1995). "The very low density lipoprotein receptor mediates the cellular catabolism of lipoprotein lipase and urokinase-plasminogen activator inhibitor type I complexes". The Journal of Biological Chemistry 270 (44): 26550–7. doi:10.1074/jbc.270.44.26550. PMID 7592875. 
  • Bu G, Geuze HJ, Strous GJ, Schwartz AL (May 1995). "39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein". The EMBO Journal 14 (10): 2269–80. PMC 398334. PMID 7774585. 
  • Van Leuven F, Hilliker C, Serneels L, Umans L, Overbergh L, De Strooper B, Fryns JP, Van den Berghe H (Jan 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, Pladet MW, Strickland DK, Chappell DA (Jan 1995). "The 39-kDa receptor-associated protein modulates lipoprotein catabolism by binding to LDL receptors". The Journal of Biological Chemistry 270 (2): 536–40. doi:10.1074/jbc.270.2.536. PMID 7822276. 
  • Korenberg JR, Argraves KM, Chen XN, Tran H, Strickland DK, Argraves WS (Jul 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 (Jan 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, Otani H, Braun JR, Hammer RE, Herz J (Jun 1996). "RAP, a specialized chaperone, prevents ligand-induced ER retention and degradation of LDL receptor-related endocytic receptors". The EMBO Journal 15 (11): 2632–9. PMC 450198. PMID 8654360. 
  • Jacobsen L, Madsen P, Moestrup SK, Lund AH, Tommerup N, Nykjaer A, Sottrup-Jensen L, Gliemann J, Petersen CM (Dec 1996). "Molecular characterization of a novel human hybrid-type receptor that binds the alpha2-macroglobulin receptor-associated protein". The Journal of Biological Chemistry 271 (49): 31379–83. doi:10.1074/jbc.271.49.31379. PMID 8940146. 
  • Bu G, Rennke S, Geuze HJ (Jan 1997). "ERD2 proteins mediate ER retention of the HNEL signal of LRP's receptor-associated protein (RAP)". Journal of Cell Science. 110. 110 ( Pt 1): 65–73. PMID 9010785. 
  • Petersen CM, Nielsen MS, Nykjaer A, Jacobsen L, Tommerup N, Rasmussen HH, Roigaard H, Gliemann J, Madsen P, Moestrup SK (Feb 1997). "Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography". The Journal of Biological Chemistry 272 (6): 3599–605. doi:10.1074/jbc.272.6.3599. PMID 9013611. 
  • Nielsen PR, Ellgaard L, Etzerodt M, Thogersen HC, Poulsen FM (Jul 1997). "The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein". Proceedings of the National Academy of Sciences of the United States of America 94 (14): 7521–5. doi:10.1073/pnas.94.14.7521. PMC 23854. PMID 9207124. 

External links

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


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