A0A140LHW5 is a short Spcs2-derived product lacking the membrane-spanning architecture of the full subunit. The peptidase prediction assigns catalytic activity to an accessory subunit. Complex membership and signal-peptide processing are plausible for full-length Spcs2 but unproven for this selected product.
A0A140LHW5 and Q9CYN2 share MGI:1913874. The first 66 residues are identical; the selected product has an eight-residue alternative tail. Both reference transmembrane helices (87–107 and 112–132) lie outside that conserved segment. The global alignment of the eight-residue tail to isolated reference residues is not evidence that a transmembrane helix is retained.
the
human SPC exists in two functional paralogs with distinct proteolytic subunits.
the catalytic SPC subunit (paralog Sec11A or Sec11C, respectively) is joined by SPCS1 (also known as SPC12), SPCS2 (SPC25), and SPCS3 (SPC22/23).
The complete emitted record is preserved in Spcs2-protnlm-source.json. Assessments below address the selected protein product; evidence on longer products is identified explicitly.
Signal peptidase complex subunit 2
CNN (CS 2) as a gene-of-origin label, with an essential truncation qualification: the sequence shares the Spcs2 N terminus. UNC if interpreted as an assembled, functional signal peptidase subunit. Sequence mapping.
Endoplasmic reticulum membrane
UNC (CS 1). The two reference membrane helices are absent from the retained sequence. Indirect ER association remains possible through protein partners, but it is not demonstrated for A0A140LHW5; absence of a transmembrane helix alone is not proof of exclusively soluble localization.
All 3 emitted GO claims are individually assessed in Spcs2-protnlm-predictions-review.yaml.
The exact accession has no PANTHER assignment. Q9CYN2 provides independently verified same-gene context for PTHR13085; that family membership does not validate the selected short product as an assembled subunit or enzyme.
The exact-product GOA snapshot is empty. No core molecular function is asserted. Human complex structures establish the catalytic/accessory distinction, while exact mouse product expression, membrane binding and complex incorporation remain unresolved.
Exact sequence mapping: Spcs2-bioinformatics/RESULTS.md. Global alignments can place nonhomologous alternative tails opposite gaps or distant residues; only conserved segments and explicitly retained feature intervals support functional transfer.
The genuine Falcon report is retained. Its gene-level synthesis is interpreted through the exact product sequence and the primary sources above; the truncation boundary and paralog distinctions are assessed independently.
ProtNLM2 files were not opened or used. Sources: UniProt A0A140LHW5 and Q9CYN2, Ensembl
gene ENSMUSG00000035227, PANTHER PTHR13085 family files, PMID:34388369, PMID:42173868,
and the Falcon deep-research report (gene-level; it does not notice that the accession is
a short alternative product).
New analysis: Spcs2-bioinformatics/compare_sequences_rereview.py -> RESULTS-rereview.md
(live UniProt + Ensembl REST fetch; earlier RESULTS.md left untouched).
GOA has zero rows for A0A140LHW5, so there are no existing annotations to act on.
I propose no NEW annotations: the activities and complex membership of SPCS2 are
established for the full-length two-pass membrane protein (human Q15005 and mouse Q9CYN2,
both PANTHER PTHR13085:SF0, PAINT node PTN000317824 IBD for GO:0005787 signal peptidase
complex, GO:0045047, GO:0051604). The fragment has no PANTHER assignment and lacks the
membrane region through which SPCS2 contacts the complex
PMID:42173868, so neither
complex membership nor ER-membrane localization can be transferred. The SPC is catalysed
by SEC11A/C PMID:42173868, so peptidase activity would be wrong even for full-length Spcs2.
core_functions left empty deliberately.