Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF18659e5tszA1 A: alpha duplicates or obligate multimersX: Traversal protein CelTOS (From Topology)H: Traversal protein CelTOS (From Topology)T: Traversal protein CelTOSF: PF18659ECOD (1.6)
BPF18659e5tszB1 A: alpha duplicates or obligate multimersX: Traversal protein CelTOS (From Topology)H: Traversal protein CelTOS (From Topology)T: Traversal protein CelTOSF: PF18659ECOD (1.6)
CPF18659e5tszC1 A: alpha duplicates or obligate multimersX: Traversal protein CelTOS (From Topology)H: Traversal protein CelTOS (From Topology)T: Traversal protein CelTOSF: PF18659ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C
PF18659Cell-traversal protein for ookinetes and sporozoites (CelTOS)Cell-traversal protein for ookinetes and sporozoitesCell-traversal protein for ookinetes and sporozoites (CelTOS) is a conserved protein that is essential for traversal of malaria parasites in both the mosquito vector and human host and is therefore critical for malaria transmission and disease pathog ...Cell-traversal protein for ookinetes and sporozoites (CelTOS) is a conserved protein that is essential for traversal of malaria parasites in both the mosquito vector and human host and is therefore critical for malaria transmission and disease pathogenesis. It specifically binds phosphatidic acid commonly present within the inner leaflet of plasma membranes, and potently disrupts liposomes composed of phosphatidic acid by forming pores. CelTOS resembles class I viral membrane fusion glycoproteins and a bacterial pore-forming toxin with roles in membrane binding and disruption. CelTOS forms an alpha helical dimer that resembles a tuning fork. Structure analysis indicate that it has a distinct structural architecture with two subdomains that independently resemble membrane binding and/or disrupting proteins and could simultaneously act during disruption [1].
Domain

InterPro: Protein Family Classification InterPro Database Homepage