ID   CCKN_HUMAN              Reviewed;         115 AA.
AC   P06307;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Cholecystokinin;
DE            Short=CCK;
DE   Contains:
DE     RecName: Full=Cholecystokinin-58;
DE              Short=CCK58;
DE   Contains:
DE     RecName: Full=Cholecystokinin-58 desnonopeptide;
DE     AltName: Full=(1-49)-CCK58;
DE   Contains:
DE     RecName: Full=Cholecystokinin-39;
DE              Short=CCK39;
DE   Contains:
DE     RecName: Full=Cholecystokinin-33;
DE              Short=CCK33;
DE   Contains:
DE     RecName: Full=Cholecystokinin-25;
DE              Short=CCK25;
DE   Contains:
DE     RecName: Full=Cholecystokinin-18;
DE              Short=CCK18;
DE   Contains:
DE     RecName: Full=Cholecystokinin-12;
DE              Short=CCK12;
DE   Contains:
DE     RecName: Full=Cholecystokinin-8;
DE              Short=CCK8;
DE   Contains:
DE     RecName: Full=Cholecystokinin-7;
DE              Short=CCK7;
DE   Contains:
DE     RecName: Full=Cholecystokinin-5;
DE              Short=CCK5;
DE   Flags: Precursor;
GN   Name=CCK;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kato K., Takahashi Y., Matsubara K.;
RT   "Molecular cloning of the human cholecystokinin gene.";
RL   Ann. N. Y. Acad. Sci. 448:613-615(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND AMIDATION AT PHE-103.
RX   PubMed=3856870; DOI=10.1073/pnas.82.7.1931;
RA   Takahashi Y., Kato K., Hayashizaki Y., Wakabayashi T., Ohtsuka E.,
RA   Matsuki S., Ikehara M., Matsubara K.;
RT   "Molecular cloning of the human cholecystokinin gene by use of a synthetic
RT   probe containing deoxyinosine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:1931-1935(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-32.
RG   NIEHS SNPs program;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEOLYTIC CLEAVAGE (CHOLECYSTOKININ-5).
RX   PubMed=9371719; DOI=10.1042/bj3280587;
RA   Isaac R.E., Williams T.A., Sajid M., Corvol P., Coates D.;
RT   "Cleavage of arginyl-arginine and lysyl-arginine from the C-terminus of
RT   pro-hormone peptides by human germinal angiotensin I-converting enzyme
RT   (ACE) and the C-domain of human somatic ACE.";
RL   Biochem. J. 328:587-591(1997).
RN   [7]
RP   PROTEOLYTIC CLEAVAGE (CHOLECYSTOKININ-5).
RX   PubMed=10336644; DOI=10.1046/j.1432-1327.1999.00419.x;
RA   Isaac R.E., Michaud A., Keen J.N., Williams T.A., Coates D., Wetsel W.C.,
RA   Corvol P.;
RT   "Hydrolysis by somatic angiotensin-I converting enzyme of basic dipeptides
RT   from a cholecystokinin/gastrin and a LH-RH peptide extended at the C-
RT   terminus with gly-Arg/Lys-arg, but not from diarginyl insulin.";
RL   Eur. J. Biochem. 262:569-574(1999).
RN   [8]
RP   MUTAGENESIS OF TYR-97, AND SULFATION AT TYR-97.
RX   PubMed=11076522; DOI=10.1021/bi0011072;
RA   Vishnuvardhan D., Beinfeld M.C.;
RT   "Role of tyrosine sulfation and serine phosphorylation in the processing of
RT   procholecystokinin to amidated cholecystokinin and its secretion in
RT   transfected AtT-20 cells.";
RL   Biochemistry 39:13825-13830(2000).
RN   [9]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-31.
RX   PubMed=25326458; DOI=10.1074/mcp.m114.043703;
RA   Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L.,
RA   Nilsson J., Larson G.;
RT   "Identification of chondroitin sulfate linkage region glycopeptides reveals
RT   prohormones as a novel class of proteoglycans.";
RL   Mol. Cell. Proteomics 14:41-49(2015).
RN   [10]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-31.
RX   PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617;
RA   Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.;
RT   "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected
RT   Correlation Between Glycan Sulfation and Attachment Site Characteristics.";
RL   Mol. Cell. Proteomics 22:100617-100617(2023).
CC   -!- FUNCTION: This peptide hormone induces gall bladder contraction and the
CC       release of pancreatic enzymes in the gut. Its function in the brain is
CC       not clear. Binding to CCK-A receptors stimulates amylase release from
CC       the pancreas, binding to CCK-B receptors stimulates gastric acid
CC       secretion. {ECO:0000250|UniProtKB:Q9TS44}.
CC   -!- SUBUNIT: Binds to CCK-A receptors in the pancreas and CCK-B receptors
CC       in the brain. {ECO:0000250|UniProtKB:Q9TS44}.
CC   -!- INTERACTION:
CC       P06307; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-6624398, EBI-18899653;
CC       P06307; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-6624398, EBI-10173507;
CC       P06307; Q9NU02: ANKEF1; NbExp=3; IntAct=EBI-6624398, EBI-8464238;
CC       P06307; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-6624398, EBI-5280499;
CC       P06307; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-6624398, EBI-10254793;
CC       P06307; C1IDX9: ATG12; NbExp=3; IntAct=EBI-6624398, EBI-25836940;
CC       P06307; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-6624398, EBI-10693038;
CC       P06307; O00257-3: CBX4; NbExp=3; IntAct=EBI-6624398, EBI-4392727;
CC       P06307; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-6624398, EBI-11953200;
CC       P06307; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-6624398, EBI-749253;
CC       P06307; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-6624398, EBI-744045;
CC       P06307; Q99966: CITED1; NbExp=3; IntAct=EBI-6624398, EBI-2624951;
CC       P06307; O95278-6: EPM2A; NbExp=3; IntAct=EBI-6624398, EBI-25836908;
CC       P06307; Q6NXG1-3: ESRP1; NbExp=3; IntAct=EBI-6624398, EBI-21567429;
CC       P06307; P06241: FYN; NbExp=3; IntAct=EBI-6624398, EBI-515315;
CC       P06307; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-6624398, EBI-9088619;
CC       P06307; O75409: H2AP; NbExp=3; IntAct=EBI-6624398, EBI-6447217;
CC       P06307; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-6624398, EBI-2868501;
CC       P06307; P53701: HCCS; NbExp=3; IntAct=EBI-6624398, EBI-10763431;
CC       P06307; Q9NRZ9-6: HELLS; NbExp=3; IntAct=EBI-6624398, EBI-12003732;
CC       P06307; Q9UK76: JPT1; NbExp=3; IntAct=EBI-6624398, EBI-720411;
CC       P06307; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-6624398, EBI-8473062;
CC       P06307; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-6624398, EBI-9088829;
CC       P06307; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-6624398, EBI-25835523;
CC       P06307; Q16609: LPAL2; NbExp=3; IntAct=EBI-6624398, EBI-10238012;
CC       P06307; Q8NI22: MCFD2; NbExp=3; IntAct=EBI-6624398, EBI-2689785;
CC       P06307; P01106: MYC; NbExp=3; IntAct=EBI-6624398, EBI-447544;
CC       P06307; Q9UJ70-2: NAGK; NbExp=3; IntAct=EBI-6624398, EBI-11526455;
CC       P06307; P25208: NFYB; NbExp=3; IntAct=EBI-6624398, EBI-389728;
CC       P06307; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-6624398, EBI-1059321;
CC       P06307; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-6624398, EBI-741048;
CC       P06307; Q07869: PPARA; NbExp=3; IntAct=EBI-6624398, EBI-78615;
CC       P06307; P02775: PPBP; NbExp=3; IntAct=EBI-6624398, EBI-718973;
CC       P06307; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-6624398, EBI-25835994;
CC       P06307; P23942: PRPH2; NbExp=3; IntAct=EBI-6624398, EBI-25836834;
CC       P06307; P29074: PTPN4; NbExp=3; IntAct=EBI-6624398, EBI-710431;
CC       P06307; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-6624398, EBI-14065960;
CC       P06307; Q04206: RELA; NbExp=3; IntAct=EBI-6624398, EBI-73886;
CC       P06307; P47804-3: RGR; NbExp=3; IntAct=EBI-6624398, EBI-25834767;
CC       P06307; Q15382: RHEB; NbExp=3; IntAct=EBI-6624398, EBI-1055287;
CC       P06307; P62701: RPS4X; NbExp=3; IntAct=EBI-6624398, EBI-354303;
CC       P06307; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-6624398, EBI-10248967;
CC       P06307; Q7L8J4: SH3BP5L; NbExp=3; IntAct=EBI-6624398, EBI-747389;
CC       P06307; Q8IYM2: SLFN12; NbExp=3; IntAct=EBI-6624398, EBI-2822550;
CC       P06307; Q9C004: SPRY4; NbExp=3; IntAct=EBI-6624398, EBI-354861;
CC       P06307; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-6624398, EBI-12408727;
CC       P06307; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-6624398, EBI-2659201;
CC       P06307; Q92797-2: SYMPK; NbExp=3; IntAct=EBI-6624398, EBI-21560407;
CC       P06307; P62253: UBE2G1; NbExp=3; IntAct=EBI-6624398, EBI-2340619;
CC       P06307; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-6624398, EBI-947187;
CC       P06307; Q9P1Q0-4: VPS54; NbExp=3; IntAct=EBI-6624398, EBI-25835297;
CC       P06307; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-6624398, EBI-10316321;
CC       P06307; Q8IWT0-2: ZBTB8OS; NbExp=3; IntAct=EBI-6624398, EBI-12956041;
CC       P06307; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-6624398, EBI-14104088;
CC       P06307; Q96JL9-2: ZNF333; NbExp=3; IntAct=EBI-6624398, EBI-25835852;
CC       PRO_0000010542; P32239: CCKBR; NbExp=2; IntAct=EBI-6624436, EBI-1753137;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:37453717}.
CC   -!- TISSUE SPECIFICITY: Detected in cerebrospinal fluid and urine (at
CC       protein level). {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:37453717}.
CC   -!- PTM: The precursor is cleaved by proteases to produce a number of
CC       active cholecystokinins.
CC   -!- PTM: [Cholecystokinin-5]: The precursor is cleaved by ACE, which
CC       removes the Gly-Arg-Arg peptide at the C-terminus, leading to mature
CC       hormone. {ECO:0000269|PubMed:10336644, ECO:0000269|PubMed:9371719}.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/cck/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Cholecystokinin entry;
CC       URL="https://en.wikipedia.org/wiki/Cholecystokinin";
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DR   EMBL; L00354; AAA53094.1; -; Genomic_DNA.
DR   EMBL; BT006991; AAP35637.1; -; mRNA.
DR   EMBL; AY514491; AAR89908.1; -; Genomic_DNA.
DR   EMBL; BC008283; AAH08283.1; -; mRNA.
DR   CCDS; CCDS2696.1; -.
DR   PIR; A01623; GMHUCP.
DR   RefSeq; NP_000720.1; NM_000729.5.
DR   RefSeq; NP_001167609.1; NM_001174138.2.
DR   PDB; 7EZH; EM; 3.20 A; P=96-103.
DR   PDB; 7EZK; EM; 3.10 A; P=96-103.
DR   PDB; 7EZM; EM; 2.90 A; P=96-103.
DR   PDB; 7MBX; EM; 1.95 A; P=96-103.
DR   PDB; 7MBY; EM; 2.44 A; P=96-103.
DR   PDB; 7XOU; EM; 3.20 A; L=96-103.
DR   PDBsum; 7EZH; -.
DR   PDBsum; 7EZK; -.
DR   PDBsum; 7EZM; -.
DR   PDBsum; 7MBX; -.
DR   PDBsum; 7MBY; -.
DR   PDBsum; 7XOU; -.
DR   AlphaFoldDB; P06307; -.
DR   EMDB; EMD-23749; -.
DR   EMDB; EMD-23750; -.
DR   EMDB; EMD-31387; -.
DR   EMDB; EMD-31388; -.
DR   EMDB; EMD-31389; -.
DR   SMR; P06307; -.
DR   BioGRID; 107327; 13.
DR   IntAct; P06307; 56.
DR   STRING; 9606.ENSP00000379472; -.
DR   BindingDB; P06307; -.
DR   ChEMBL; CHEMBL1649050; -.
DR   DrugBank; DB13729; Camostat.
DR   GlyGen; P06307; 1 site.
DR   iPTMnet; P06307; -.
DR   PhosphoSitePlus; P06307; -.
DR   BioMuta; CCK; -.
DR   DMDM; 115945; -.
DR   MassIVE; P06307; -.
DR   PaxDb; 9606-ENSP00000379472; -.
DR   PeptideAtlas; P06307; -.
DR   ProteomicsDB; 51882; -.
DR   Antibodypedia; 29187; 300 antibodies from 34 providers.
DR   DNASU; 885; -.
DR   Ensembl; ENST00000334681.9; ENSP00000335657.5; ENSG00000187094.12.
DR   Ensembl; ENST00000396169.7; ENSP00000379472.2; ENSG00000187094.12.
DR   Ensembl; ENST00000434608.1; ENSP00000409124.1; ENSG00000187094.12.
DR   GeneID; 885; -.
DR   KEGG; hsa:885; -.
DR   MANE-Select; ENST00000396169.7; ENSP00000379472.2; NM_000729.6; NP_000720.1.
DR   AGR; HGNC:1569; -.
DR   CTD; 885; -.
DR   DisGeNET; 885; -.
DR   GeneCards; CCK; -.
DR   HGNC; HGNC:1569; CCK.
DR   HPA; ENSG00000187094; Group enriched (brain, intestine).
DR   MIM; 118440; gene.
DR   neXtProt; NX_P06307; -.
DR   OpenTargets; ENSG00000187094; -.
DR   PharmGKB; PA26141; -.
DR   VEuPathDB; HostDB:ENSG00000187094; -.
DR   eggNOG; ENOG502S472; Eukaryota.
DR   GeneTree; ENSGT00390000003571; -.
DR   HOGENOM; CLU_169783_0_0_1; -.
DR   InParanoid; P06307; -.
DR   OMA; YSGLCIC; -.
DR   OrthoDB; 5293435at2759; -.
DR   PhylomeDB; P06307; -.
DR   TreeFam; TF333419; -.
DR   PathwayCommons; P06307; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   SignaLink; P06307; -.
DR   SIGNOR; P06307; -.
DR   BioGRID-ORCS; 885; 15 hits in 1146 CRISPR screens.
DR   ChiTaRS; CCK; human.
DR   GeneWiki; Cholecystokinin; -.
DR   GenomeRNAi; 885; -.
DR   Pharos; P06307; Tbio.
DR   PRO; PR:P06307; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P06307; Protein.
DR   Bgee; ENSG00000187094; Expressed in frontal pole and 125 other cell types or tissues.
DR   ExpressionAtlas; P06307; baseline and differential.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; TAS:ProtInc.
DR   GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR   GO; GO:0051428; F:peptide hormone receptor binding; IPI:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0007586; P:digestion; IBA:GO_Central.
DR   GO; GO:0042755; P:eating behavior; ISS:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR015499; CCK-like.
DR   InterPro; IPR001651; Gastrin/CCK.
DR   InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR   PANTHER; PTHR10786; CHOLECYSTOKININ; 1.
DR   PANTHER; PTHR10786:SF0; CHOLECYSTOKININ; 1.
DR   Pfam; PF00918; Gastrin; 1.
DR   SMART; SM00029; GASTRIN; 1.
DR   PROSITE; PS00259; GASTRIN; 1.
DR   Genevisible; P06307; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Cleavage on pair of basic residues; Glycoprotein;
KW   Hormone; Proteoglycan; Reference proteome; Secreted; Signal; Sulfation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..115
FT                   /note="Cholecystokinin"
FT                   /id="PRO_0000010536"
FT   PROPEP          21..44
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000010537"
FT   PEPTIDE         46..103
FT                   /note="Cholecystokinin-58"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000010538"
FT   PEPTIDE         46..94
FT                   /note="Cholecystokinin-58 desnonopeptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000306304"
FT   PEPTIDE         65..103
FT                   /note="Cholecystokinin-39"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000010539"
FT   PEPTIDE         71..103
FT                   /note="Cholecystokinin-33"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000010540"
FT   PEPTIDE         79..103
FT                   /note="Cholecystokinin-25"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000306305"
FT   PEPTIDE         86..103
FT                   /note="Cholecystokinin-18"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000306306"
FT   PEPTIDE         92..103
FT                   /note="Cholecystokinin-12"
FT                   /evidence="ECO:0000250|UniProtKB:P01356"
FT                   /id="PRO_0000010541"
FT   PEPTIDE         96..103
FT                   /note="Cholecystokinin-8"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000010542"
FT   PEPTIDE         97..103
FT                   /note="Cholecystokinin-7"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000306307"
FT   PEPTIDE         99..103
FT                   /note="Cholecystokinin-5"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT                   /id="PRO_0000306308"
FT   PROPEP          107..115
FT                   /id="PRO_0000010543"
FT   REGION          22..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         97
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:11076522"
FT   MOD_RES         103
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:3856870"
FT   MOD_RES         111
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT   MOD_RES         113
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT   CARBOHYD        31
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:25326458,
FT                   ECO:0000269|PubMed:37453717"
FT   VARIANT         32
FT                   /note="G -> E (in dbSNP:rs11571848)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_018818"
FT   VARIANT         95
FT                   /note="R -> W (in dbSNP:rs3774395)"
FT                   /id="VAR_024452"
FT   MUTAGEN         97
FT                   /note="Y->F: Reduces the quantity of secreted CCK8 by 50%."
FT                   /evidence="ECO:0000269|PubMed:11076522"
SQ   SEQUENCE   115 AA;  12669 MW;  8A3EE6442FAEAF4B CRC64;
     MNSGVCLCVL MAVLAAGALT QPVPPADPAG SGLQRAEEAP RRQLRVSQRT DGESRAHLGA
     LLARYIQQAR KAPSGRMSIV KNLQNLDPSH RISDRDYMGW MDFGRRSAEE YEYPS
//