The domain within your query sequence starts at position 36 and ends at position 169; the E-value for the Lipocalin domain shown below is 1.6e-8.



PFAM accession number:PF00061
Interpro abstract (IPR000566):

Proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids share limited regions of sequence homology and a common tertiary structure architecture [ (PUBMED:3622999) (PUBMED:1608945) (PUBMED:2217163) (PUBMED:7684291) (PUBMED:3238752) ]. This is an eight stranded antiparallel beta-barrel with a repeated + 1 topology enclosing a internal ligand binding site [ (PUBMED:7684291) (PUBMED:2217163) ]. The name 'lipocalin' has been proposed [ (PUBMED:3622999) ] for this protein family, but cytosolic fatty-acid binding proteins are also included. The sequences of most members of the family, the core or kernal lipocalins, are characterised by three short conserved stretches of residues, while others, the outlier lipocalin group, share only one or two of these [ (PUBMED:1834059) (PUBMED:7684291) ]. Proteins known to belong to this family include alpha-1-microglobulin (protein HC); alpha-1-acid glycoprotein (orosomucoid) [ (PUBMED:3064105) ]; aphrodisin; apolipoprotein D; beta-lactoglobulin; complement component C8 gamma chain [ (PUBMED:1707134) ]; crustacyanin [ (PUBMED:2026162) ]; epididymal-retinoic acid binding protein (E-RABP) [ (PUBMED:8069623) ]; insectacyanin; odorant-binding protein (OBP); human pregnancy-associated endometrial alpha-2 globulin; probasin (PB), a rat prostatic protein; prostaglandin D synthase ( EC ) [ (PUBMED:1723819) ]; purpurin; Von Ebner's gland protein (VEGP) [ (PUBMED:7514123) ]; and lizard epididymal secretory protein IV (LESP IV) [ (PUBMED:8486691) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Lipocalin