Proteome analysis of shell matrix proteins in the brachiopod Laqueus rubellus

Yukinobu Isowa, Isao Sarashina, Kenshiro Oshima, Keiji Kito, Masahira Hattori, Kazuyoshi Endo*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)


Background: The calcitic brachipod shells contain proteins that play pivotal roles in shell formation and are important in understanding the evolution of biomineralization. Here, we performed a large-scale exploration of shell matrix proteins in the brachiopod Laqueus rubellus. Results: A total of 40 proteins from the shell were identified. Apart from five proteins, i.e., ICP-1, MSP130, a cysteine protease, a superoxide dismutase, and actin, all other proteins identified had no homologues in public databases. Among these unknown proteins, one shell matrix protein was identified with a domain architecture that includes a NAD(P) binding domain, an ABC-type transport system, a transmembrane region, and an aspartic acid rich region, which has not been detected in other biominerals. We also identified pectin lyase-like, trypsin inhibitor, and saposin B functional domains in the amino acid sequences of the shell matrix proteins. The repertoire of brachiopod shell matrix proteins also contains two basic amino acid-rich proteins and proteins that have a variety of repeat sequences. Conclusions: Our study suggests an independent origin and unique mechanisms for brachiopod shell formation.

Original languageEnglish
Article number21
JournalProteome Science
Issue number1
Publication statusPublished - 2015 Aug 15
Externally publishedYes


  • Biomineralization
  • Brachiopoda
  • Proteome
  • Shell matrix protein
  • Transcriptome

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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