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; RAP
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[edit]

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 know 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[edit]

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

References[edit]

  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. PMID 1712782. 
  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. 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 (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. doi:10.1073/pnas.94.14.7521. PMC 23854. PMID 9207124. 
  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. ISSN 1046-6673. PMID 11912251. 
  6. ^ Orlando, R A; Farquhar M G (April 1994). "Functional domains of the receptor-associated protein (RAP)". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 91 (8): 3161–5. doi:10.1073/pnas.91.8.3161. ISSN 0027-8424. PMC 43535. PMID 7512726. 

Further reading[edit]

External links[edit]

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