TPSD1
Tryptase delta
Also known as: TRYD_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9BZJ3
- Gene
- TPSD1
- Ensembl
- ENSG00000095917
- Chromosome
- 16
- Canonical length
- 242 aa
- Protein class
- Enzymes, Metabolic proteins, Predicted intracellular proteins
- Secretome location
- Intracellular and membrane
- Quaternary structure
- Homotetramer
OverviewNCBI Gene
Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. Tryptases are enzymatically active only as heparin-stabilized tetramers, and they are resistant to all known endogenous proteinase inhibitors. Several tryptase genes are clustered on chromosome 16p13.3. These genes are characterized by several distinct features. They have a highly conserved 3' UTR and contain tandem repeat sequences at the 5' flank and 3' UTR which are thought to play a role in regulation of the mRNA stability. Although this gene may be an exception, most of the tryptase genes have an intron immediately upstream of the initiator Met codon, which separates the site of transcription initiation from protein coding sequence. This feature is characteristic of tryptases but is unusual in other genes. Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders. This gene was once considered to be a pseudogene, although it is now believed to be a functional gene that encodes a protein. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
242 residues, UniProt reviewed canonical sequence.
>Q9BZJ3|TPSD1
1 MLLLAPQMLS LLLLALPVLA SPAYVAPAPG QALQQTGIVG GQEAPRSKWP WQVSLRVRGP
61 YWMHFCGGSL IHPQWVLTAA HCVEPDIKDL AALRVQLREQ HLYYQDQLLP VSRIIVHPQF
121 YIIQTGADIA LLELEEPVNI SSHIHTVTLP PASETFPPGM PCWVTGWGDV DNNVHLPPPY
181 PLKEVEVPVV ENHLCNAEYH TGLHTGHSFQ IVRDDMLCAG SENHDSCQGD SGGPLVCKVN
241 GTLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TPSD1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.34
- Highest tissue expression
- 20 nTPM
Expression across tissuesHPA
Tissue
- stomach: 20 nTPM
- lung: 17 nTPM
- gallbladder: 13 nTPM
- small intestine: 13 nTPM
- urinary bladder: 12 nTPM
- skin: 9 nTPM
Single-cell type
- mast cells: 136 nCPM
- bergmann glia: 4.6 nCPM
- astrocytes: 3.1 nCPM
- parietal cells: 1.8 nCPM
- epididymal efferent duct ciliated cells: 0.4 nCPM
- vascular smooth muscle cells: 0.4 nCPM
Immune cell
- basophil: 2.9 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- cerebral cortex: 1.6 nTPM
- pons: 1.2 nTPM
- thalamus: 1 nTPM
- hippocampal formation: 0.9 nTPM
- basal ganglia: 0.8 nTPM
- cerebellum: 0.8 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.85
- gnomAD pLI
- 0
- gnomAD missense Z
- -1.62
- DepMap mean gene effect
- 0.04
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads TPSD1 as an antibody target. Whether an autoantibody or antibody against TPSD1 could matter depends on whether native TPSD1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TPSD1 is annotated as secreted, so native TPSD1 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label TPSD1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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