SSF50814

Lipocalins

SUPERFAMILY entry
Member databaseSUPERFAMILY
SUPERFAMILY typehomologous superfamily

Description
Imported from IPR012674

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
[1]
. Of these families, the lipocalin family (
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
[2, 3, 4, 5]
. 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
[6]
.

References
Imported from IPR012674

1.The lipocalin protein family: structural and sequence overview. Flower DR, North AC, Sansom CE. Biochim. Biophys. Acta 1482, 9-24, (2000). View articlePMID: 11058743

2.Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence. Urade Y, Eguchi N. Prostaglandins Other Lipid Mediat. 68-69, 375-82, (2002). View articlePMID: 12432930

3.Major urinary proteins, alpha(2U)-globulins and aphrodisin. Cavaggioni A, Mucignat-Caretta C. Biochim. Biophys. Acta 1482, 218-28, (2000). View articlePMID: 11058763

4.Immunocalins: a lipocalin subfamily that modulates immune and inflammatory responses. Logdberg L, Wester L. Biochim. Biophys. Acta 1482, 284-97, (2000). PMID: 11058769

5.The core lipocalin, bovine beta-lactoglobulin. Sawyer L, Kontopidis G. Biochim. Biophys. Acta 1482, 136-48, (2000). View articlePMID: 11058756

6.YodA from Escherichia coli is a metal-binding, lipocalin-like protein. David G, Blondeau K, Schiltz M, Penel S, Lewit-Bentley A. J. Biol. Chem. 278, 43728-35, (2003). View articlePMID: 12909634

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