The output combines a Serpin B10 name, an HSP47-like collagen-chaperone function and inhibitory-serpin GO terms. These are different functional branches of a shared fold; none is established for this compact nematode protein.
Q18287 is C28G1.2/WBGene00016187 and is not a characterized srp-2 or srp-3 product. Its sequence is 265 residues, with an annotated serpin domain at 96–199. The name and inhibitory GO claims originate from structural donor B2KI30, while the collagen paragraph comes from chicken SERPINH1/HSP47 P13731. The asymmetric TM-align scores reflect unequal sequence lengths and cannot identify a particular paralog. The absence of a called signal peptide does not by itself disprove the existing extracellular IBA.
Some appear
complete, some show extensive deletions, and others appear to contain only the
C-terminal part of the known serpin fold
The complete emitted record is preserved in C28G1.2-protnlm-source.json. Assessments below address the selected protein product; evidence on longer products is identified explicitly.
Serpin B10
UNC (CS 1). “Serpin” is supported at the superfamily level; the specific B10 designation is not established by the structural match. No resolved subfamily phylogeny or target experiment identifies this nematode protein as the B10 counterpart, so the name is too specific to accept but a particular alternative paralog assignment is not asserted.
Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen
UNC (CS 1). The donor is chicken SERPINH1/HSP47, a specialized collagen chaperone. A serpin fold match does not establish that mechanism in C28G1.2, and neither collagen binding nor an appropriate secretory-pathway location was demonstrated for the target. Nematodes do synthesize collagens, so taxon alone does not refute the hypothesis. Donor record; nematode serpin architecture study.
Secreted
UNC (CS 1). Secreted is compatible with the existing extracellular IBA, but a model match to another serpin is not independent confirmation of localization. The retrieved target record lacks a called signal peptide; this is insufficient to prove that secretion is impossible.
All 2 emitted GO claims are individually assessed in C28G1.2-protnlm-predictions-review.yaml.
Serpin superfamily membership is supported by the sequence/domain evidence. Inhibitory serpins, noninhibitory serpins and collagen chaperones must be separated by mechanism, sequence architecture and phylogeny rather than by the shared fold. No PANTHER identifier is assigned when an exact family placement has not been established.
The 1999 comparative study is abstract-only; its architectural conclusions are family context, not a claimed C28G1.2 assay or proof of a defective gene model. No target-specific functional study was located using Q18287, C28G1.2 and the serpin designation. The genuine Falcon report distinguishes the uncharacterized target from assayed worm serpins, but its suggested inhibitory default is not biological validation.