Calycin
IPR012674
Definition
Calycins form a large protein superfamily that share similar β-barrel structures. Calycins can be divided into families that include lipocalins, fatty acid binding proteins, triabin, and thrombin inhibitor PMID:11058743. Of these families, the lipocalin family ([interpro:IPR002345]) is the largest and functionally the most diverse. Lipocalins are extracellular proteins that share several common recognition properties such as ligand binding, receptor binding and the formation of complexes with other macromolecules. Lipocalins include the retinol binding protein, lipocalin allergen, aphrodisin (a sex hormone), alpha-2U-globulin, prostaglandin D synthase, beta-lactoglobulin, bilin-binding protein, and the nitrophorins [[cite:PMID:12432930], [cite:PMID:11058763], [cite:PMID:11058769], [cite:PMID:11058756]]. Bacterial hypothetical proteins YodA from Escherichia coli and YwiB from Bacillus subtilis share a similar calycin β-barrel structure. Part of the YodA hypothetical protein has a calycin-like structure PMID:12909634.
39 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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