The normal Seed8 import supplies ANOS1/P23352, with 16 source annotations. Preserve every source object, qualifier and supporting-entity identifier. Main 39bed05e675793816eecae865765ce2791132884 has no ANOS1 or ADMLX/KAL/KAL1/KALIG1 gene/history path, matching branch or open review PR in the complete current inventory. The baseline and remote proof are in tmp/ANOS1-initial/.
The configured Falcon attempt and perplexity-lite fallback failed without a report; the actual receipt records 5.654 seconds. These notes are manual research, not a generated provider report. Existing publication records remain unchanged. A four-PMID normal batch timed out after 45 seconds with no output; a subsequent single-PMID localization request timed out after 30 seconds with no output. This does not establish five completed individual fetch failures. Source closure remains pending.
The reviewed UniProt record describes a secreted, peripheral membrane glycoprotein that interacts with FGFR1 and heparin. Its WAP and fibronectin-type-III domains do not, by themselves, establish enzyme inhibition. Human and chick constructs were expressed in the original cell-surface processing study; COS host identity must not be substituted for the species of the protein. PMID:8842728(https://pubmed.ncbi.nlm.nih.gov/8842728/) reports a membrane-associated precursor and a diffusible processed product that retains surface binding. The complete cached abstract was read, not its full paper. Its chemoattractant proposal was a hypothesis; later migration assays provide independent evidence.
The complete cached abstracts of PMID:1913827(https://pubmed.ncbi.nlm.nih.gov/1913827/) and PMID:1922361(https://pubmed.ncbi.nlm.nih.gov/1922361/) concern gene identification and sequence similarities. They are not direct adhesion or axon-guidance experiments. Later functional work can support the biological assertions without retrospectively assigning assays to those early papers.
PMID:19696444(https://pubmed.ncbi.nlm.nih.gov/19696444/) directly examines FGFR1 interaction and order-dependent signaling-complex assembly. The complete normal cached abstract and indexed original Introduction/Discussion were read. ANOS1 modulates a receptor/FGF2/glycosaminoglycan complex; it is not established here as an independently sufficient growth factor. FGFR1 binding is the defensible refinement of the source's generic interaction term. Separate FGFR2 binding is weaker and does not justify a new receptor role. The two cached Reactome events, R-HSA-5654514 and R-HSA-5654515, were read in full and distinguish ANOS1–FGFR1c and ANOS1–heparan-sulfate interactions. Their extracellular location is consistent with the experimental record.
For PMID:40546398(https://pubmed.ncbi.nlm.nih.gov/40546398/), the normal cache's complete abstract, targeted immunohistochemical Methods and nearby tissue-expression passages were read. The Methods explicitly say "ANOS1 was localized in the cytoplasm" while describing scoring of stained cells. This experiment is not itself a direct interstitial-matrix localization assay. The paper's expression, prognosis and pathway-enrichment correlations do not establish a core EMT or cancer-signaling mechanism. This is a citation-scope issue rather than evidence that extracellular ANOS1 is absent. The independently established human matrix localization in PMID:10340754 can support the existing location while preserving the GOA source and documenting the limitation of its original citation. No full figure-image or supplementary-data review has yet been performed.
The local PAINT slice places cell surface and neuron differentiation at PANTHER:PTN000364816 in PTHR14131. The full tree and MSA have not been inspected. Preserve the inherited assertions: the primary human evidence is compatible, and donor count is not an objection. Do not copy current local slice seed changes into the original GOA supporting-entity fields. No ANOS1/P23352/KAL1 match was found in gocams/index.tsv.
The HuRI PMID:32296183 normal cache contains a full-text extraction. Its complete abstract has been read; the exact ANOS1–NCALD and ANOS1–UBQLN1 experimental data rows have not been adjudicated. Neither localization mismatch nor title silence refutes a binary-screen interaction. Pending that evidence, retain two UNDECIDED decisions, without inventing a functional binding refinement.
Official AmiGO definitions were checked for GO:0005105 (type 1 fibroblast growth factor receptor binding), GO:0008201 (heparin binding, with heparan sulfate binding as a synonym), GO:0016504 (peptidase activator activity), and GO:0140149 (non-collagenous component of interstitial matrix). The SMART WAP domain entry reports the broad IPR008197 mapping to peptidase inhibition and also documents functional diversity among WAP proteins. Candidate NEW entries are restricted to direct heparin binding and, subject to assay verification, peptidase activation; no NEW BP is proposed.
The independent prospective consultation reviewed all 16 decisions and identified finite evidence conditions; it did not certify final source closure. Preserve UNDECIDED for the two unadjudicated HuRI pairs. The WAP-domain inhibitor transfer is also provisionally UNDECIDED: two tested enzymes do not establish a universal negative, even though the domain-to-function inference is questionable.
The original 1998 adhesion paper, author-supplied full-text copy was consulted specifically at Cells, protein/peptide Methods and adhesion Results/Figures 1–3. Its adhesion Results explicitly identify the protein as produced from human KAL-1 cDNA in CHO cells. The 32R1 peptide is likewise human. This closes the protein-species question for the adhesion evidence independently of the rodent neuronal hosts. It does not by itself settle the separate 2002 axon-guidance experiment's construct or antibody specificity. The accessible copy was used for reading, not substituted for an immutable normal publication cache.
The 2004 biochemical paper was subsequently read through the actual construct, binding and protease-assay Methods and associated Results/Discussion. Tagged recombinant constructs were purified from S2 cells; chromogenic-substrate assays measured uPA activity with protein-negative/GFP controls. Its Discussion proposes a WAP disulfide-geometry difference from elafin, rather than experimentally excluding all inhibitory activities. These observations support conditional uPA activation without establishing a plasmin-cascade biological process or unrestricted protease inhibition. Figure legends were read; figure pixels and supplements were not examined. Explicit construct-species closure remains distinct from the S2 expression host.
The exact Source33 archive was recovered and verified against its published artifact digest. All five normal records (9730987, 10340754, 12007408, 15324302 and 15548653) are abstract-only. Their complete cached abstracts and identifier/title/DOI fields were read and matched the prior official-source assessment. The recovery does not change the externally read primary-body scope above or imply that those bodies are present in the normal cache. Technical validation and canonical import are recorded separately.
The original 2004 neuronal paper was also read at the FNC-B4 culture and neurite Methods, neurite-response Results and FGFR1 inhibition/complex experiments. Human olfactory neuroblasts were cultured in three-dimensional collagen; anosmin-1 effects depended on dose and FGFR1 signaling. The co-immunoprecipitation result establishes coassociation, while the later 2009 binding experiment supplies direct receptor-interaction evidence. Heterologous BaF3 assays do not establish the protein construct species by host identity. No figure-pixel or full supplement inspection is claimed.
The 2002 axon-guidance construct/antibody scope remains unresolved after the accessible abstract and unsuccessful original-body access attempts. That annotation stays uncertain. The two HuRI pairs and the WAP-domain peptidase-inhibitor transfer also remain explicitly uncertain. Finite uncertainty is retained without asserting that an experimentally curated interaction is false.
All five normal records were imported without overwriting a prior cache. Their exact titles and abstract quotations now support the relevant assertions, and every PMID availability flag reflects the cached record. All 16 original annotation objects remain unchanged outside their review fields. Four finite evidence uncertainties remain explicit; completion records the finished assessment, not a resolution of every biological question. No new process annotation was added.
This section supersedes the earlier unresolved 2002 construct scope and the provisional WAP-domain decision. The 16 source assertions, prior NEW heparin annotation, raw files, normal publication records and published history remain intact. The two independent consultations distinguish source identity from the experiments actually read.
GO:0008201 specifies heparin binding. Its heparan-sulfate synonym has RELATED, not EXACT, scope; GO:1904399 separately specifies heparan-sulfate binding. Both have glycosaminoglycan-binding ancestry. The previous claim that the terms were equivalent is withdrawn. The retained heparin MF describes the ligand actually used in biochemical assays, while physiological cell-surface HS interactions are discussed separately.
The original 2004 biochemical paper, author-uploaded copy was read at recombinant-protein, ELISA/SPR and protease Methods, corresponding Results and WAP Discussion. Figure 3 uses HS in ELISA; Figure 4/Table 1 use heparin in SPR. The SPR Methods explicitly state “immobilized biotin conjugated heparin”. Thus the abstract's compressed HS/SPR wording does not describe the assay reagent precisely. The previous NEW GO:0008201 remains supported by the independently cited 2009 heparin-complex study; no additional MF is added here.
The same original paper reports enhanced uPA amidolytic activity and “had no effect on thrombin amidolytic activity”. The WAP-derived IEA inhibitor assignment exceeds the demonstrated activity and is marked over-annotated. This is not a universal NOT assertion: other peptidases were not excluded. The exact cached uPA result and this externally read thrombin scope are kept separate. The normal 2004 record remains abstract-only.
The original 2002 Cell paper, author-uploaded copy was read at Figure 1, Figure 7 and tandem-assay Results, Cells and axon-guidance Methods. Figure 1A/B (p. 219) explicitly identifies “Purified anosmin-1 produced by CHO cells transfected with the human KAL-1 cDNA”. Cells Methods (p. 226) identify clone 2.3d11. Figure 7 links the producer-cell preparation to directional attraction of E15 rat olfactory-bulb axons; tandem geometry separates attraction from simple growth promotion. E17 axons and dorsal-root-ganglion controls respond differently. Figure images and all supplements were not independently inspected.
The human protein supplies the extracellular cue; CHO cells produce it and rat neurons respond. This closes the earlier construct boundary without relying on rodent antibody reactivity or later clone continuity. Existing axon guidance is accepted using this later independent evidence while preserving the original 1991 TAS source. The result does not establish guidance of every axon or initial lateral-olfactory-tract formation. No new BP is proposed. Existing chemotaxis and neuronal-differentiation core context describes cue/modulator participation, not locomotion of the protein.
The ANOS1–NCALD and ANOS1–UBQLN1 HuRI pair experiments remain unadjudicated. General article availability does not replace their construct and pair-table evidence. Under the explicit user action definitions, genericity alone does not show these experimental assertions are incorrect; they remain UNDECIDED. Empty notes-only support entries were removed instead of presenting this evidence boundary as a positive experimental finding.
The FGFR1 refinement now quotes the weaker FGFR2IIIc and negligible FGFR3IIIc comparison. Reference reviews name the experiments or remaining access limits. Human interstitial-matrix evidence remains PMID:10340754; the unresolved linkage to the gastric-cancer IHC source is retained without a blanket miscitation judgment. Cache titles, normal availability flags, source identifiers and the published history are unchanged.