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HSPA1L
Heat shock 70 kDa protein 1L is a protein that in humans is encoded by the ''HSPA1L'' gene on chromosome 6.〔(【引用サイトリンク】 url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3305 )〕 As a member of the heat shock protein 70 (Hsp70) family and a chaperone protein, it facilitates the proper folding of newly translated and misfolded proteins, as well as stabilize or degrade mutant proteins.〔 Its functions contribute to biological processes including signal transduction, apoptosis, protein homeostasis, and cell growth and differentiation.〔 It has been associated with an extensive number of cancers, neurodegenerative diseases, cell senescence and aging, and Graft-versus-host disease.〔〔
== Structure ==
This gene encodes a 70kDa heat shock protein and is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which also encode isoforms of the 70kDa heat shock protein.〔 The amino acid sequence of the encoded protein shares a 90% homology to the isoforms HSPA1A and HSPA1B. As a Hsp70 protein, it has a C-terminal protein substrate-binding domain and an N-terminal ATP-binding domain. The substrate-binding domain consists of two subdomains, a two-layered β-sandwich subdomain (SBDβ) and an α-helical subdomain (SBDα), which are connected by the loop Lα,β. SBDβ contains the peptide binding pocket while SBDα serves as a lid to cover the substrate binding cleft. The ATP binding domain consists of four subdomains split into two lobes by a central ATP/ADP binding pocket.〔 The two terminal domains are linked together by a conserved region referred to as loop LL,1, which is critical for allosteric regulation. The unstructured region at the very end of the C-terminal is believed to be the docking site for co-chaperones.〔〔
Since a cDNA clone of this gene contains a 119 bp-region in the 5' UTR, it is likely that ''HSPA1L'' contains one or more introns in its own 5' UTR.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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