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The basic functional domains of mammalian CLCA proteins are conserved in gCLCA1.

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posted on 13.04.2022, 17:42 authored by Florian Bartenschlager, Nikolai Klymiuk, Christoph Weise, Benno Kuropka, Achim D. Gruber, Lars Mundhenk

Schematic depiction of the gCLCA1 protein and of CLCA proteins of clusters 1, 3, and 4 in three mammalian representatives (human, pig and mouse). A cleavable N-terminal signal peptide (dark brown box), an N-CLCA domain (N-CLCA, light brown box), a vWA-domain (vWA, light green box), a β-sheet rich domain (bsr, dark green box) and a fibronectin type III domain (fn3, light blue box) were predicted by in silico analyses and manual sequence alignments. The N-CLCA domain comprises an intact zinc-dependent metalloprotease motif (HExxH, vertical yellow bar). The vWA domain contains a MIDAS site (DxSxS, T, D, vertical yellow bar). Vertical dark red bars indicate cysteine residues, predominantly in the N-CLCA domain. The gCLCA1 protein is putatively cleaved after the amino acids QNR at aa position 705 (scissor). gCLCA1 has a putative C-terminal transmembrane domain (TM, light red box) similarly to the CLCA representatives of cluster 4. The gCLCA1 protein is an N-linked glycoprotein with 12 predicted glycosylation sites. The number of glycosylation sites is higher than in the CLCA proteins of cluster 4, followed by the proteins of cluster 3 and 1. Putative glycosylation sites are indicated by -icons. Numbers display the absolute position, for protein domains further specified by the first or last three amino acids of each domain, respectively.

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