InterPro : IPR002970

Name  Tick histamine-binding protein Short Name  Tick_his-bd
Type  Family Description  The lipocalins are a diverse, interesting, yet poorly understood family of proteins composed, in the main, of extracellular ligand-binding proteinsdisplaying high specificity for small hydrophobic molecules [, ]. Functionsof these proteins include transport of nutrients, control of cell regulation, pheromone transport, cryptic colouration and the enzymatic synthesisof prostaglandins.The crystal structures of several lipocalins have been solved and show a novel 8-stranded anti-parallel beta-barrel fold well conserved within thefamily. Sequence similarity within the family is at a much lower level andwould seem to be restricted to conserved disulphides and 3 motifs, whichform a juxtaposed cluster that may act as a common cell surface receptorsite []. By contrast, at the more variable end of the fold are found an internal ligand binding site and a putative surface for the formation of macromolecular complexes []. The anti-parallel beta-barrel fold is alsoexploited by the fatty acid-binding proteins (which function similarly bybinding small hydrophobic molecules), by avidin and the closely relatedmetalloprotease inhibitors, and by triabin. Similarity at the sequencelevel, however, is less obvious, being confined to a single short N-terminal motif.The lipocalin family can be subdivided into kernal and outlier sets. Thekernal lipocalins form the largest self-consistent group, comprising the subfamily of tick histamine-binding proteins. The outlier lipocalins form several smaller distinct subgroups: the OBPs, the von Ebner's gland proteins, alpha-1-acid glycoproteins, tick histamine binding proteins and the nitrophorins.The tick histamine binding proteins are the most recently identified set of outlier lipocalins. The structure of one tick histamine binding protein hasbeen solved []and has shown the proteins to have the characteristic lipocalin fold but without any appreciable sequence similarity. The tickhistamine binding proteins are secreted into the saliva of the ixodid tick Rhipicephalus appendiculatusand share functional similarity with the nitrophorins, sequestering histamine at the wound site. Because the tickhistamine binding proteins outcompete histamine receptors, they are able toovercome host inflammatory and immune responses. This enables the ticks tofeed for extended periods, lasting from days to several weeks, and are able to gorge themselves on large blood meals increasing their body mass 100 fold.Unlike nitrophorins, the tick proteins do not bind haem (or other cofactor),but ligate histamine directly in two rigid orthogonally-arranged binding sites, at opposing ends of the lipocalin anti-parallel beta-barrel, whichhave an unusually polar character.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

1 Contains

Id Name Short Name Type
IPR011038 Calycin-like Calycin-like Domain

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Flower DR Multiple molecular recognition properties of the lipocalin protein family. 1995 J Mol Recognit 8 185-95
Pervaiz S Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC. 1985 Science 228 335-7
Flower DR The lipocalin protein family: structure and function. 1996 Biochem J 318 ( Pt 1) 1-14
Paesen GC Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure. 1999 Mol Cell 3 661-71

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)