The domain within your query sequence starts at position 20 and ends at position 137; the E-value for the Alpha-2-MRAP_N domain shown below is 7.7e-45.

LLLPLMLVPQPIAGHGGKYSREKNEPEMAAKRESGEEFRMEKLNQLWEKAKRLHLSPVRL
AELHSDLKIQERDELNWKKLKVEGLDKDGEKEAKLIHNLNVILARYGLDGRKDAQMVH

Alpha-2-MRAP_N

• PFAM accession number: PF06400
• Interpro abstract (IPR009066):

  The alpha-2-macroglobulin receptor-associated protein (RAP) is a glycoprotein that binds to the alpha-2-macroglobulin receptor, as well as to other members of the low density lipoprotein receptor family ( IPR002172 ). RAP 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 [ (PUBMED:9207124) ]. RAP may be under the regulatory control of calmodulin, since it is able to bind calmodulin and be phosphorylated by calmodulin-dependent kinase II ( IPR002048 ).

  RAP is comprised of three domains. Both domains 1 and 3 are involved in binding to the alpha-2-macroglobulin receptor, while domain 1 is also involved in inhibiting the binding of activated alpha-2-macroglobulin ( IPR001599 ). Structural studies have revealed the RAP domain 1 to be comprised of a partly opened bundle of three helices, the first one being shorter than the other two.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Alpha-2-MRAP_N