Detail Information for IndEnz0001000539
IED ID IndEnz0001000539
Enzyme Type ID amylase000539
Protein Name Cholecystokinin
CCK

Cleaved into: Cholecystokinin-58
CCK58
; Cholecystokinin-58 desnonopeptide
1-49
-CCK58
; Cholecystokinin-39
CCK39
; Cholecystokinin-33
CCK33
; Cholecystokinin-25
CCK25
; Cholecystokinin-18
CCK18
; Cholecystokinin-12
CCK12
; Cholecystokinin-8
CCK8
; Cholecystokinin-7
CCK7
; Cholecystokinin-5
CCK5
Gene Name CCK
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MNSGVCLCVLMAVLAAGALTQPVPPADPAGSGLQRAEEAPRRQLRVSQRTDGESRAHLGALLARYIQQARKAPSGRMSIVKNLQNLDPSHRISDRDYMGWMDFGRRSAEEYEYPS
Enzyme Length 115
Uniprot Accession Number P06307
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme 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.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (1); Modified residue (4); Mutagenesis (1); Natural variant (2); Peptide (10); Propeptide (2); Region (1); Signal peptide (1)
Keywords 3D-structure;Amidation;Cleavage on pair of basic residues;Hormone;Reference proteome;Secreted;Signal;Sulfation
Interact With Q6DHV7-2; Q6UY14-3; Q9NU02; Q66PJ3-4; Q6XD76; C1IDX9; Q9NSI6-4; O00257-3; Q494V2-2; Q8WUX9; Q9Y3D0; Q99966; O95278-6; Q6NXG1-3; P06241; Q06547-3; O75409; Q6NXT2; P53701; Q9NRZ9-6; Q9UK76; Q8N1A0; Q6DKI2; Q9H2C1; Q16609; Q8NI22; P01106; Q9UJ70-2; P25208; Q8NFH3; Q7Z3B4; Q07869; P02775; Q6ZMI0-5; P23942; P29074; Q96HR9-2; Q04206; P47804-3; Q15382; P62701; Q66K80; Q7L8J4; Q8IYM2; Q9C004; Q5W111-2; Q96BD6; Q92797-2; P62253; Q9UHD9; Q9P1Q0-4; Q9NX94; Q8IWT0-2; Q53FD0-2; Q96JL9-2; P32239
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 97; /note=Sulfotyrosine; /evidence=ECO:0000269|PubMed:11076522; MOD_RES 103; /note=Phenylalanine amide; /evidence=ECO:0000269|PubMed:3856870; MOD_RES 111; /note=Sulfotyrosine; /evidence=ECO:0000250; MOD_RES 113; /note=Sulfotyrosine; /evidence=ECO:0000250
Post Translational Modification PTM: The precursor is cleaved by proteases to produce a number of active cholecystokinins.
Signal Peptide SIGNAL 1..20
Structure 3D Electron microscopy (2)
Cross Reference PDB 7MBX; 7MBY;
Mapped Pubmed ID 10191087; 10220011; 10235270; 10668930; 11140838; 11244486; 11368834; 11443535; 11509018; 11713976; 11713982; 11713985; 11724786; 11803530; 12116180; 12116188; 12198366; 12572876; 12627463; 12777967; 1280419; 12915664; 12920059; 14764444; 15100163; 15313848; 15328192; 15354400; 15533776; 15624269; 15682471; 15740988; 15743365; 15837012; 16185316; 16754659; 17192493; 17208296; 17332474; 17365745; 17438102; 17964616; 18066654; 18154642; 18234641; 18396340; 18423848; 18555802; 18577758; 18996102; 1905813; 19058789; 19086053; 19339394; 19497313; 19741117; 19760980; 19874574; 19914303; 20023595; 20036221; 20424473; 20457200; 20602615; 20732371; 20734064; 20930049; 21154912; 21186400; 21506165; 21542221; 21753024; 21985915; 22188045; 23064014; 23233532; 23349895; 23399917; 23564449; 23975326; 24001751; 24177032; 24252886; 24692543; 24914377; 25331205; 25984632; 26429068; 26454231; 26762368; 26878472; 27084212; 27875537; 29381655; 29729168; 30121362; 3086311; 30902899; 31541684; 34086670; 8503909; 8664309; 9491815; 9603610; 9754694;
Motif
Gene Encoded By
Mass 12,669
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda