Maps InterPro signature matches to GO terms. For ADAMTSL5 the relevant signature is IPR013273 ADAMTS/ADAMTS-like, whose sole GO mapping is GO:0030198 extracellular matrix organization. The signature covers 26,580 proteins and spans both the catalytic ADAMTS proteases and the non-catalytic ADAMTS-like proteins.

PAINT phylogenetic propagation. For ADAMTSL5 the single IBA row derives from PANTHER node PTN000347317 in family PTHR13723, with 16 protein donors. The GOA WITH/FROM field matches the cached PAINT seed list for that node exactly.

Maps the UniProt Secreted subcellular location keyword (SL-0243) to GO:0005576 extracellular region. Correct for ADAMTSL5, which has a signal peptide and experimentally demonstrated secretion.

ADAMTSL5 is a secreted, N-glycosylated ~60 kDa glycoprotein. Recombinant protein is recovered from the conditioned medium of transfected HEK293F, COS-1 and CHO-K1 cells and deposits into the peri-cellular and baso-lateral extracellular matrix.

ADAMTSL5 binds heparin through its C-terminal NTR module in a salt-sensitive ionic interaction; only the NTR-containing C-terminal fragment is retained on heparin-agarose.

ADAMTSL5 binds both fibrillin-1 and fibrillin-2 and co-localises with assembled fibrillin microfibrils in fibroblast extracellular matrix - the first family member shown to bind both fibrillins.

Critically, the same experiment found no effect of ADAMTSL5 on microfibril assembly, and direct binding to fibronectin was not supported. This is the only direct test of a matrix-organizing role for ADAMTSL5 and it was negative, though reported as data not shown.

The ADAMTS-like proteins, including ADAMTSL5, have no catalytic domain and hence no proteolytic activity - the basis for rejecting any protease-derived functional inference for this gene.

In mouse organogenesis ADAMTSL5 is broadly expressed, prominently in musculoskeletal tissues - skeletal muscle, cartilage and bone - and in many epithelia. Cartilage and bone are not elastic-fibre tissues.

A general review of elastic fibre composition, assembly and disease. Its abstract does not mention ADAMTSL5. QuickGO shows it is used as the TAS reference for 66 annotations across 62 distinct entities, 41 of which receive GO:0071953 elastic fiber - a bulk curation pass rather than a gene-specific traceable statement. The same pass assigned the more specific GO:0001527 microfibril to 15 other proteins.

The HuRI systematic yeast two-hybrid screen, source of all three GO:0005515 rows for ADAMTSL5 (partners CYSRT1, KRTAP5-9 and FHL5). IntAct logs each partner under three sub-methods of the same experiment - two hybrid array, two hybrid prey pooling approach and validated two hybrid - all at MI-score 0.56, so UniProt's NbExp=3 is one screen counted three ways rather than three independent observations.

ADAMTSL5 is an HLA-C*06:02-presented melanocytic autoantigen recognised by a Valpha3S1/Vbeta13S1 CD8+ T cell receptor from a psoriasis patient, and ADAMTSL5 stimulation induced IL-17A in CD8+ T cells from psoriasis patients only. The recognised peptide VRSRRCLRL maps to residues 67-75, inside the TSP type-1 domain.

ADAMTSL5 is activated by gene-body CpG island hypermethylation in mouse and human hepatocellular carcinoma. Depletion interfered with tumorigenic properties, while overexpression conferred tumorigenicity on pre-tumoural hepatocytes sensitised by modest MET expression.

All 16 protein donors on the GO:0031012 IBA row carry their own experimental IDA/HDA evidence for that term or a descendant, and the donor set spans four distinct locations, making GO:0031012 the correct least common ancestor.

Propagation from PANTHER node PTN000347317 is incoherent across the human family: GO:0031012 reached 5 of 7 non-catalytic members and GO:0030198 only 3 of 7, while human PAPLN received no IBA at all despite three of its own orthologs being seeds for GO:0031012 at that node.

The three GO:0005515 partners are extreme Y2H hubs (517, 213 and 108 distinct IntAct partners against ADAMTSL5's 12) and all are topologically inaccessible to a secreted protein.

ADAMTSL5 has no zinc-binding metalloprotease motif - no HExxHxxGxxHD and no HExxH substring at all in its 481 residues - confirming the loss of catalysis independently of UniProt's CAUTION line.

Provider deep-research record. Its narrative of the fibrillin, heparin, psoriasis and hepatocellular carcinoma literature is broadly accurate and every citation is a numeric PMID, but its GO grounding proposes GO:0008289 lipid binding and GO:0098772 molecular function regulator activity, neither of which has any support - the demonstrated ligand is heparin, a glycosaminoglycan. Not imported.