I am working with a Type I transmembrane protein (single span) having a large N-terminal ectodomain (~1000 aa) and a short (100 aa) cytosolic part but no signal peptide was identified as per Signalp server. Verified by cell fractionation that the protein comes in the membrane fraction. Moreover, if the protein is N-terminal tagged, the tag is also detected in the membrane fraction. It implies that the intact protein is transferred to the membrane that is not usual for a type I transmembrane protein which generally possesses a cleavable N-terminal signal sequence.
Any suggestion will be appreciated. thanks in advance.
Dear Anirban Kundu ,
Not exactly sure this is what you are looking for but may be you came across this excellent overview:
Rabouille, C. (2017). Pathways of unconventional protein secretion. Trends in cell biology, 27(3), 230-240.
Article Pathways of Unconventional Protein Secretion
In this review you find some examples of Type I transmembrane proteins lacking a conventional signal sequence.
Kind regards.
Thanks Rob Keller . I appreciate your effort. Hope to find something here.
Check answers to this questions:
https://www.researchgate.net/post/Is_it_essential_to_have_a_signal_peptide_for_a_transmembrane_protein
Annemarie Honegger I read it before posting my query. It was not the thread what I specifically want. Thanks.
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