Der p 1, a major house dust mite allergen and a secreted papain-like cysteine protease (peptidase C1 family). Produced in the mite digestive tract and excreted in faecal pellets, its proteolytic activity is central to its allergenicity: it cleaves epithelial tight-junction and immune proteins and activates host receptors (e.g. MRGPRX1), promoting allergic sensitization. It is recognized by IgE in the large majority of dust-mite-allergic patients.
The preferred accession for this review is P08176. These relationships are manually assessed.
REFERENCE PROTEOME CANDIDATE · Reviewed 2026-10-19
Reference proteome: UP000887458
Retain P08176 as the primary Swiss-Prot accession. The full 320-residue query is represented within a much longer 837-residue reference model: 300 identities over 320 paired residues, but only 35.84% identity when all global-alignment columns are counted. The target is labeled MCM2_2/MCM DNA helicase despite peptidase-C1 family evidence. This is a possible fused or otherwise problematic gene model, not an established intact equivalent; retain a candidate for genomic/model review.
MMseqs2 searched 14,675 sequences across UP000887458 at E <= 1e-5 and sensitivity 7.5, returning 22 hits. Every returned sequence was globally aligned using BLOSUM62 with gap-open -10 and extension -0.5. Scores and sequences for all 22 returned candidates are retained, with 10 detailed alignment files. The heuristic search does not establish genomic absence or unique locus identity.
file:DERPT/Derp1/Derp1-record-evidence.yaml
target_sequence_count: 14675
file:DERPT/Derp1/Derp1-record-evidence.yaml
candidate_count: 22
A0ABQ8JGY3: 300 identities across 837 global-alignment columns (35.8423% identity including gaps), 20 substitutions and 517 gap columns. Query coverage is 100.0%; target coverage is 38.2318%. Sequence similarity is interpreted in the manual rationale. Identity over paired residues is 93.7500% (300/320); gap columns are excluded from this denominator.
file:DERPT/Derp1/Derp1-record-evidence.yaml
query_length: 320 target_length: 837 alignment_columns: 837 identities: 300 mismatches: 20 gap_columns: 517 identity_percent: 35.8423 query_coverage_percent: 100.0 target_coverage_percent: 38.2318
The primary accession is outside every searched exact-taxon reference proteome. Current UniProt records place A0ABQ8JGY3 in UP000887458 and give it the same taxon as the primary.
file:DERPT/Derp1/Derp1-record-evidence.yaml
primary_in_any_reference_proteome: false
file:DERPT/Derp1/Derp1-record-evidence.yaml
alternative_in_reference_proteome: true
file:DERPT/Derp1/Derp1-record-evidence.yaml
same_taxon: true
Sampled UniSave observations: 14-OCT-2015, entry version 114.: no Proteomes cross-reference; 07-OCT-2020, entry version 131.: no Proteomes cross-reference; 29-MAY-2024, entry version 142.: UP000515146. These dated observations do not establish uninterrupted membership/absence, the exact change date, or UniProt's motivation.
file:DERPT/Derp1/Derp1-record-evidence.yaml
entry_date: 14-OCT-2015, entry version 114. proteomes: []
file:DERPT/Derp1/Derp1-record-evidence.yaml
entry_date: 07-OCT-2020, entry version 131. proteomes: []
file:DERPT/Derp1/Derp1-record-evidence.yaml
entry_date: 29-MAY-2024, entry version 142. proteomes: - UP000515146
The reference model is named MCM2_2 but also carries peptidase-C1 family membership; the very long model and strong embedded query match require inspection rather than trusting its name.
file:DERPT/Derp1/Derp1-record-evidence.yaml
value: MCM2_2
file:DERPT/Derp1/Derp1-record-evidence.yaml
Belongs to the peptidase C1 family
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005576 extracellular region | IEA GO_REF:0000044 | ACCEPT | Summary: Der p 1 is a secreted/excreted mite protease; extracellular localization is correct. Reason: Secreted in mite faeces; acts in the extracellular space. |
| GO:0006508 proteolysis | IEA GO_REF:0000002 | ACCEPT | Summary: Der p 1 is a proteolytic enzyme; proteolysis is its core biological process. Reason: Direct consequence of its cysteine-protease activity. Supporting Evidence: file:DERPT/Derp1/Derp1-uniprot.txt Thiol protease, with a preference for substrates with a large |
| GO:0008234 cysteine-type peptidase activity | IEA GO_REF:0000002 | ACCEPT | Summary: Electronic assignment of cysteine-protease activity, consistent with the peptidase C1 family. Reason: Der p 1 is a papain-family thiol protease. Supporting Evidence: file:DERPT/Derp1/Derp1-uniprot.txt Belongs to the peptidase C1 family. |
| GO:0005576 extracellular region | EXP PMID:16148130 The crystal structure of recombinant proDer p 1, a major hou... | ACCEPT | Summary: Experimentally localized to the extracellular (excreted) mite material. Reason: Experimental support for extracellular localization. |
| GO:0008234 cysteine-type peptidase activity | IDA PMID:28768771 Activation of mas-related G-protein-coupled receptors by the... | ACCEPT | Summary: Direct demonstration of thiol-protease activity (preference for large hydrophobic or basic P2 residues); Der p 1 cleaves and activates the host receptor MRGPRX1. Reason: Experimentally demonstrated cysteine-protease activity; the core molecular function. Supporting Evidence: file:DERPT/Derp1/Derp1-uniprot.txt Thiol protease, with a preference for substrates with a large |
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Experiment: Compare wild-type and catalytically-inactive (active-site Cys mutant) Der p 1 in epithelial tight-junction cleavage and murine sensitization assays.
Hypothesis: Der p 1 protease activity is required for its adjuvant/sensitizing effect.
Type: structure-function / in vivo assay
Der p 1, major house dust mite allergen; secreted papain-like cysteine protease (peptidase C1). ACCEPT cysteine-type peptidase activity (IDA) + proteolysis + extracellular. Protease activity (cleaves tight junctions, activates MRGPRX1) underlies allergenicity. Characterized.
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