CELA3B
Chymotrypsin-like elastase family member 3B
Also known as: CBPP, CEL3B_HUMAN, ELA3B
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P08861
- Gene
- CELA3B
- Ensembl
- ENSG00000219073
- Chromosome
- 1
- Canonical length
- 270 aa
- Protein class
- Enzymes, Predicted intracellular proteins, Predicted secreted proteins
- Subcellular location
- Cytosol
- Secretome location
- Secreted to digestive system
OverviewNCBI Gene
Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, elastase 3B has little elastolytic activity. Like most of the human elastases, elastase 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after alanine residues. Elastase 3B may also function in the intestinal transport and metabolism of cholesterol. Both elastase 3A and elastase 3B have been referred to as protease E and as elastase 1, and excretion of this protein in fecal material is frequently used as a measure of pancreatic function in clinical assays. [provided by RefSeq, May 2009]
Canonical amino-acid sequenceUniProt
270 residues, UniProt reviewed canonical sequence.
>P08861|CELA3B
1 MMLRLLSSLL LVAVASGYGP PSSRPSSRVV NGEDAVPYSW PWQVSLQYEK SGSFYHTCGG
61 SLIAPDWVVT AGHCISSSRT YQVVLGEYDR AVKEGPEQVI PINSGDLFVH PLWNRSCVAC
121 GNDIALIKLS RSAQLGDAVQ LASLPPAGDI LPNETPCYIT GWGRLYTNGP LPDKLQEALL
181 PVVDYEHCSR WNWWGSSVKK TMVCAGGDIR SGCNGDSGGP LNCPTEDGGW QVHGVTSFVS
241 AFGCNTRRKP TVFTRVSAFI DWIEETIASHLocalizationUniProt · AlphaFold · HPA
Whether an antibody against CELA3B 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)
- 0.28
- Highest tissue expression
- 46,794 nTPM
Expression across tissuesHPA
Tissue
- pancreas: 46,794 nTPM
- stomach: 16 nTPM
- blood vessel: 13 nTPM
- ovary: 9.5 nTPM
- salivary gland: 9.2 nTPM
- heart muscle: 7.9 nTPM
Single-cell type
- pancreatic acinar cells: 1,221 nCPM
- late spermatids: 41 nCPM
- early spermatids: 7.1 nCPM
- pancreatic duct cells: 6 nCPM
- colonocytes: 5.8 nCPM
- gastric chief cells: 5.5 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- amygdala: 0 nTPM
- basal ganglia: 0 nTPM
- cerebellum: 0 nTPM
- cerebral cortex: 0 nTPM
- choroid plexus: 0 nTPM
- hippocampal formation: 0 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)
- 1.63
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.81
- DepMap mean gene effect
- 0.11
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 1% 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 CELA3B as an antibody target. Whether an autoantibody or antibody against CELA3B could matter depends on whether native CELA3B is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
CELA3B is annotated as secreted, so native CELA3B 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 CELA3B as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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