PRAP1
Proline-rich acidic protein 1
Also known as: PRAP1_HUMAN, UPA
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q96NZ9
- Gene
- PRAP1
- Ensembl
- ENSG00000165828
- Chromosome
- 10
- Canonical length
- 151 aa
- Protein class
- Predicted secreted proteins
- Secretome location
- Secreted to digestive system
OverviewNCBI Gene
Predicted to enable triglyceride binding activity. Involved in DNA damage response, signal transduction by p53 class mediator; deactivation of mitotic spindle assembly checkpoint; and negative regulation of apoptotic process. Predicted to be located in endoplasmic reticulum and extracellular region. [provided by Alliance of Genome Resources, Jul 2025]
Canonical amino-acid sequenceUniProt
151 residues, UniProt reviewed canonical sequence.
>Q96NZ9|PRAP1
1 MRRLLLVTSL VVVLLWEAGA VPAPKVPIKM QVKHWPSEQD PEKAWGARVV EPPEKDDQLV
61 VLFPVQKPKL LTTEEKPRGQ GRGPILPGTK AWMETEDTLG HVLSPEPDHD SLYHPPPEED
121 QGEERPRLWV MPNHQVLLGP EEDQDHIYHP QLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PRAP1 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)
- 0.7
- Highest tissue expression
- 1,069 nTPM
Expression across tissuesHPA
Tissue
- small intestine: 1,069 nTPM
- duodenum: 991 nTPM
- liver: 718 nTPM
- kidney: 166 nTPM
- colon: 70 nTPM
- choroid plexus: 57 nTPM
Single-cell type
- enterocytes: 11,248 nCPM
- colonocytes: 665 nCPM
- paneth cells: 534 nCPM
- enteric transient amplifying cells: 418 nCPM
- hepatocytes: 331 nCPM
- epididymal efferent duct absorptive cells: 194 nCPM
Immune cell
- naive B-cell: 0.3 nTPM
- basophil: 0.2 nTPM
- memory B-cell: 0.2 nTPM
- plasmacytoid DC: 0.2 nTPM
- gdT-cell: 0.1 nTPM
- naive CD4 T-cell: 0.1 nTPM
Brain region
- choroid plexus: 16 nTPM
- medulla oblongata: 4.9 nTPM
- pons: 4.8 nTPM
- white matter: 4.3 nTPM
- midbrain: 4 nTPM
- amygdala: 3.9 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)
- 1.26
- gnomAD pLI
- 0.03
- gnomAD missense Z
- 0.38
- DepMap mean gene effect
- 0.19
- 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
- cellular response to X-ray
- deactivation of mitotic spindle assembly checkpoint
- DNA damage response
- DNA damage response, signal transduction by p53 class mediator
- negative regulation of apoptotic process
- positive regulation of phospholipid transport
- positive regulation of triglyceride transport
- positive regulation of intestinal lipid absorption
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Proline-rich acidic protein 1
- Proline-rich acidic protein 1, pregnancy-specific uterine
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PRAP1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PRAP1 as an antibody target. Whether an autoantibody or antibody against PRAP1 could matter depends on whether native PRAP1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PRAP1 is annotated as secreted, so native PRAP1 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 PRAP1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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