Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage.
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Human structural analysis identifies distinct catalytic SEC11 subunits within the four-subunit signal peptidase complex.
"the
human SPC exists in two functional paralogs with distinct proteolytic subunits."
Structural basis of signal peptide recognition by the signal peptidase complex.
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The substrate-bound human structure distinguishes SPCS2 from the catalytic SEC11 subunit.
"the catalytic SPC subunit (paralog Sec11A or Sec11C, respectively) is joined by SPCS1 (also known as SPC12), SPCS2 (SPC25), and SPCS3 (SPC22/23)."
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SPCS2 contacts within the complex are made through its transmembrane helix, a region absent from the 74-residue product.
"The TM helix of SPCS2 displays a limited set of contacts"
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Bilayer deformation in the SPC membrane window is affected by SPCS2 deletion and mutation, a membrane-embedded role of the full-length subunit.
"Coarse-grained molecular dynamics (MD) simulations indicate deformation of the lipid bilayer inside of the window that is affected by deletion and mutation of SPC subunit SPCS2"
Exact Spcs2 product-to-reference sequence mapping
Spcs2 re-review sequence and transcript-model comparison of A0A140LHW5 versus canonical Q9CYN2
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A0A140LHW5 shares only the first 66 residues of canonical Q9CYN2 and ends in an unrelated eight-residue tail.
"Identical N-terminal prefix: residues 1-66"
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Neither canonical transmembrane helix lies in the shared segment.
"| Transmembrane | Helical | 87 | 107 | no |"
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The benchmark transcript is a non-canonical Ensembl model lacking canonical exon 3, whose 161-nt length shifts the downstream reading frame.
"| ENSMUSE00000263814 | 99497506 | 99497666 | 161 | False | 2 |"
Frozen exact-input ProtNLM output and UniProt sequence for A0A140LHW5