P06307 · CCKN_HUMAN
- ProteinCholecystokinin
- GeneCCK
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids115 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | hormone activity | |
Molecular Function | neuropeptide hormone activity | |
Molecular Function | peptide hormone receptor binding | |
Biological Process | axonogenesis | |
Biological Process | digestion | |
Biological Process | eating behavior | |
Biological Process | neuron migration | |
Biological Process | signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCholecystokinin
- Short namesCCK
- Cleaved into 10 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP06307
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_018818 | 32 | in dbSNP:rs11571848 | |||
Sequence: G → E | ||||||
Natural variant | VAR_024452 | 95 | in dbSNP:rs3774395 | |||
Sequence: R → W | ||||||
Mutagenesis | 97 | Reduces the quantity of secreted CCK8 by 50%. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 177 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, chain, glycosylation, peptide, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MNSGVCLCVLMAVLAAGALT | ||||||
Propeptide | PRO_0000010537 | 21-44 | ||||
Sequence: QPVPPADPAGSGLQRAEEAPRRQL | ||||||
Chain | PRO_0000010536 | 21-115 | Cholecystokinin | |||
Sequence: QPVPPADPAGSGLQRAEEAPRRQLRVSQRTDGESRAHLGALLARYIQQARKAPSGRMSIVKNLQNLDPSHRISDRDYMGWMDFGRRSAEEYEYPS | ||||||
Glycosylation | 31 | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | ||||||
Peptide | PRO_0000306304 | 46-94 | Cholecystokinin-58 desnonopeptide | |||
Sequence: VSQRTDGESRAHLGALLARYIQQARKAPSGRMSIVKNLQNLDPSHRISD | ||||||
Peptide | PRO_0000010538 | 46-103 | Cholecystokinin-58 | |||
Sequence: VSQRTDGESRAHLGALLARYIQQARKAPSGRMSIVKNLQNLDPSHRISDRDYMGWMDF | ||||||
Peptide | PRO_0000010539 | 65-103 | Cholecystokinin-39 | |||
Sequence: YIQQARKAPSGRMSIVKNLQNLDPSHRISDRDYMGWMDF | ||||||
Peptide | PRO_0000010540 | 71-103 | Cholecystokinin-33 | |||
Sequence: KAPSGRMSIVKNLQNLDPSHRISDRDYMGWMDF | ||||||
Peptide | PRO_0000306305 | 79-103 | Cholecystokinin-25 | |||
Sequence: IVKNLQNLDPSHRISDRDYMGWMDF | ||||||
Peptide | PRO_0000306306 | 86-103 | Cholecystokinin-18 | |||
Sequence: LDPSHRISDRDYMGWMDF | ||||||
Peptide | PRO_0000010541 | 92-103 | Cholecystokinin-12 | |||
Sequence: ISDRDYMGWMDF | ||||||
Peptide | PRO_0000010542 | 96-103 | Cholecystokinin-8 | |||
Sequence: DYMGWMDF | ||||||
Modified residue | 97 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Peptide | PRO_0000306307 | 97-103 | Cholecystokinin-7 | |||
Sequence: YMGWMDF | ||||||
Peptide | PRO_0000306308 | 99-103 | Cholecystokinin-5 | |||
Sequence: GWMDF | ||||||
Modified residue | 103 | Phenylalanine amide | ||||
Sequence: F | ||||||
Propeptide | PRO_0000010543 | 107-115 | ||||
Sequence: SAEEYEYPS | ||||||
Modified residue | 111 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 113 | Sulfotyrosine | ||||
Sequence: Y |
Post-translational modification
The precursor is cleaved by proteases to produce a number of active cholecystokinins.
Cholecystokinin-5
The precursor is cleaved by ACE, which removes the Gly-Arg-Arg peptide at the C-terminus, leading to mature hormone.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in cerebrospinal fluid and urine (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binds to CCK-A receptors in the pancreas and CCK-B receptors in the brain.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 22-52 | Disordered | ||||
Sequence: PVPPADPAGSGLQRAEEAPRRQLRVSQRTDG | ||||||
Compositional bias | 38-52 | Basic and acidic residues | ||||
Sequence: EAPRRQLRVSQRTDG |
Sequence similarities
Belongs to the gastrin/cholecystokinin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length115
- Mass (Da)12,669
- Last updated1988-01-01 v1
- Checksum8A3EE6442FAEAF4B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 38-52 | Basic and acidic residues | ||||
Sequence: EAPRRQLRVSQRTDG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L00354 EMBL· GenBank· DDBJ | AAA53094.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT006991 EMBL· GenBank· DDBJ | AAP35637.1 EMBL· GenBank· DDBJ | mRNA | ||
AY514491 EMBL· GenBank· DDBJ | AAR89908.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC008283 EMBL· GenBank· DDBJ | AAH08283.1 EMBL· GenBank· DDBJ | mRNA |