DNAL1 is a light-chain component of the outer dynein arm. Human binding and disease evidence supports heavy-chain association, alpha-tubulin association and a structural contribution to arm assembly or stability [PMID:15845866; PMID:21496787]. These are complementary features of one motor-complex role, without evidence that DNAL1 itself is an ATPase or autonomous motor.
PMID:15845866, Identification and analysis of axonemal dynein light chain 1 in primary ciliary dyskinesia patients was independently inspected in the UNC-hosted original PDF, Methods (Expression analysis; Co-immunoprecipitation analysis), Results and Figure 2/3 text. Human 190-residue EGFP-DNAL1 expressed in HEK293T cells was mixed with pig tracheal high-salt axonemal extract, and DNAH5 was recovered relative to an EGFP control. This is positive mixed-species extract association, not purified human binary affinity. Human Northern expression in testis and mouse in-situ expression in node, airway and ependyma are separate observations. The negative screen in 86 PCD patients does not contradict the subsequently identified pathogenic DNAL1 allele.
PMID:21496787, Primary ciliary dyskinesia caused by homozygous mutation in DNAL1 was independently inspected in selected Methods, Results and Figure 1/3/4 text. Human wild-type/N150S DNAL1-Myc was expressed in HEK293T cells and combined with rat tracheal high-salt axonemal extract. Matching DNAL1 amounts required different cell-extract inputs. N150S reduced heavy-chain and alpha-tubulin co-recovery by approximately 80%; the separate cellular decay assay established reduced stability. Respiratory cilia from affected individuals lacked normal outer arms. The work supports the structural interaction role but does not directly measure a purified human ternary bridge, ATP-independent human tether mechanics or mechanosensing. Both central publication caches are genuinely abstract-only; the separately recovered originals support the assay detail recorded here, without altering those caches.
PMID:29601588, ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic pre-assembly of dynein arms was inspected in Results (ZMYND10 interactions and DNAI1 stability), Figure 4, supplementary Figure S7 captions, and the plasmid/co-immunoprecipitation/stability Methods. These operative sections name DNAI1. The current DNAL1 annotation and ZMYND10 curated protein record nevertheless attribute a DNAL1 association to this paper. The exact target-specific provenance remains unresolved. A current IntAct/MINT nonmatch is not a negative assay, and neither a wrong-gene verdict nor nonbinding is inferred.
PMID:32296183, A reference map of the human binary protein interactome supplies the HuRI Methods context. The exact positive pair is DNAL1 Q4LDG9–LRRC40 Q9H9A6, including EBI-24553346 (IM-25472-137459), EBI-23484276 and EBI-25039784. Six sequence/taxon hashes across the three records match the displayed 190-residue DNAL1 and 602-residue LRRC40 proteins. A sufficient-binding-region feature covers DNAL1 residues 40–190; it does not identify the molecule as natural isoform 3. The positive generic binding is retained as non-core under the scoped project instruction, without inferring an endogenous complex or specific functional class from partner identity alone.
The actual PTHR15454 tree contains 805 nodes and the alignment 805 sequences. Human leaf PTN002544818 descends from the asserted Eumetazoa node PTN000833961; its ungapped 190-residue sequence matches the official product exactly. Literal IBD records at that node support outer-arm assembly, alpha-tubulin binding and heavy-chain binding, with human DNAL1 experimental grounding [PMID:21496787; PMID:15845866]. A target in its own WITH/FROM list is valid descendant evidence. The ISS donor Q9XHH2 is Chlamydomonas LC1 with an experimental outer-arm annotation, not a second human observation.
The official products are Q4LDG9-1 (190 residues), Q4LDG9-2 (77; deletion of residues 1–113) and Q4LDG9-3 (151; deletion of residues 1–39). Independent feature reconstruction matches all three official FASTAs. The natural shortened products were not functionally tested in the central studies; neither equivalent activity nor inactivity is inferred. N150S is a disease-associated substitution in a full-coding-region construct, not a natural isoform. No additional annotation is proposed: the supported structural role and interactions are already represented.
Ordinary gene and publication fetching succeeded. Falcon genuinely failed with HTTP 403 authentication, and its configured perplexity-lite fallback failed with HTTP 401 insufficient quota. No provider report was generated. The manual assessment uses the genuine publication caches, independently recovered originals and recorded source queries. Source bytes remain unchanged. No original figure-pixel reanalysis is claimed; the cited figures were assessed through their text and captions. Final ordinary validation, derived status and rendering are performed during canonical integration.
The two structured molecular-function entries now distinguish heavy-chain binding from alpha-tubulin association within one integrated outer-dynein-arm role. The alpha-tubulin identity is explicit in the original anti-alpha-tubulin B-5-1-2 immunoblot and Figure 4C. Human WT/N150S DNAL1-Myc was mixed with rat tracheal high-salt axonemal extracts; matched DNAL1 inputs showed reduced recovery of both heavy chain and alpha-tubulin with the mutant. These are controlled mixed-species extract associations, not purified binary affinities or simultaneous ternary bridging. They do not by themselves demonstrate a human A-tubule-specific mechanosensor (PMID:21496787(https://pmc.ncbi.nlm.nih.gov/articles/PMC3146731/), Figure 4 and associated Methods/Results).
The 2005 human EGFP-DNAL1/pig-axoneme DNAH5 assay remains a separate source of heavy-chain association (PMID:15845866(https://cdr.lib.unc.edu/downloads/dz010w61k), expression/co-immunoprecipitation Methods and binding Results). The normal publication caches retain their genuine abstract-only status; separately accessed originals and the source guide supply the precise construct/organism details. The new source-guide antibody excerpt is not placed in cache-validated YAML quotations.
The outer-dynein-arm refinement already exists as an accepted source claim; MODIFY preserves specificity without asserting exclusive localization. All 11 source decisions and three natural product identities remain unchanged. The prior single-core wording is superseded only in representation: two contact functions now make the same integrated biology explicit. No new motility annotation is proposed, and no systematic comparator convention is claimed from a survey that was not performed.