| Description | This entry represents the Latexin-type cystatin domain.Latexin (LXN), or tissue carboxypeptidase inhibitor (TCI), is the only known mammalian carboxypeptidase inhibitor (CPI). It is expressed in a cell type-specific manner in both central and peripheral nervous systems in the rat []. LTX has no detectable sequence similarity with plant and parasite inhibitors, but it is related to a human putative tumor suppressor protein, TIG1 (). TIG1 is larger than latexin, and the additional residues are thought to encode a membrane anchor at the N terminus. Other proteins with sequence identity to LXN are found in chicken (Ovocalyxin-32, ) and Xenopus, but no related proteins were found in nonvertebrates. Chicken Ovocalyxin-32 is a protein involved in egg shell production [ , ].The structure of LXN ( ) shows no structural relationship with other CPIs. Furthermore, despite a lack of detectable sequence duplication, the structure incorporates two topologically analogous domains related by pseudo two-fold symmetry. Each domain comprises a curved five-stranded antiparallel β-sheet wrapped around an α-helix. These domains share a cystatin fold architecture found in proteins that inhibit cysteine proteases, suggesting an evolutionary and possibly functional relationship. LXN may have evolved from an ancestral cystatin-like protein as a consequence of a gene duplication event. The LXN-type cystatin domains are packed against each other through the helices and linked by a connecting segment encompassing a third α-helix. The two domains are arranged so that there is a cleft in this part of the structure that can accommodate a peptide chain [ , ]. | Name | Latexin-type cystatin domain |
| Short Name | CYSTATIN_LXN | Type | Domain |
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