Abstract
HSP47/SERPINH1 is key-regulator for collagen biosynthesis and its structural assembly. To date, there is no comprehensive study on the phylogenetic history of HSP47. Herein we illustrate the evolutionary history of HSP47/SERPINH1 along with sequence, structural and syntenic traits for HSP47/SERPINH1. We have identified ancestral HSP47/SERPINH1 locus in Japanese lamprey (Lethenteron japonicum). This gene remains on the same or similar locus for ~500 million years (MY), but chromosomal duplication was observed in ray-finned fishes, leading into three sets of three sets (I-III) of HSP47/SERPINH1. Two novel introns were inserted at the positions 36b and 102b in the first exon of only HSP47_1 gene from the selected ray-finned fishes. On the evolutionary time scale, the events of HSP47 duplications took placed between 416–360 MY ago (MYA) while intron insertion dates back to 231–190 MYA after early divergence of ray-finned fishes.
Highlights
Heat shock protein 47 (HSP47/SERPINH1) operates as a client-specific chaperone for collagen and plays a vital role in collagen maturation and the consequent embryonic development
HSP47/SERPINH1 is a critical regulator of the collagen maturation and associated embryonic development
The current study provides an updated repository of the HSP47/SERPINH1 gene from 61 vertebrate species (Table S1) and summarizes major concepts revolving around sequence, structure and phylogeny of HSP47/SERPINH1 across vertebrate genomes
Summary
Heat shock protein 47 (HSP47/SERPINH1) operates as a client-specific chaperone for collagen and plays a vital role in collagen maturation and the consequent embryonic development. It is a non-inhibitory serpin, which belongs to the clade H and group V6 based on the clade and indel based group-wise classification systems of vertebrate serpins, respectively[1]. This serpin is an ER-resident, collagen-specific chaperone and plays a key role in collagen biosynthesis and its structural assembly[2]. We elucidated the detailed molecular phylogeny of HSP47/SERPINH1 genes by combining protein sequence, gene structures and genomic organization from 61 vertebrate genomes
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