CCKN_MOUSE
ID CCKN_MOUSE Reviewed; 115 AA.
AC P09240; Q53WS9; Q9DCL5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cholecystokinin;
DE Short=CCK;
DE Contains:
DE RecName: Full=Cholecystokinin-33;
DE Short=CCK33;
DE Contains:
DE RecName: Full=Cholecystokinin-12;
DE Short=CCK12;
DE Contains:
DE RecName: Full=Cholecystokinin-8;
DE Short=CCK8;
DE Flags: Precursor;
GN Name=Cck;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/3J;
RX PubMed=2011497; DOI=10.1093/nar/19.1.169;
RA Vitale M., Vashishtha A., Linzer E., Powell D.J., Friedman J.M.;
RT "Molecular cloning of the mouse CCK gene: expression in different brain
RT regions and during cortical development.";
RL Nucleic Acids Res. 19:169-177(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-115, AND AMIDATION AT PHE-103.
RX PubMed=3862083; DOI=10.1073/pnas.82.17.5593;
RA Friedman J.M., Schneider B.S., Powell D.J.;
RT "Differential expression of the mouse cholecystokinin gene during brain and
RT gut development.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5593-5597(1985).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23863714; DOI=10.1172/jci68587;
RA Chandra R., Wang Y., Shahid R.A., Vigna S.R., Freedman N.J., Liddle R.A.;
RT "Immunoglobulin-like domain containing receptor 1 mediates fat-stimulated
RT cholecystokinin secretion.";
RL J. Clin. Invest. 123:3343-3352(2013).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23863714}.
CC -!- TISSUE SPECIFICITY: Expressed and secreted by discrete enteroendocrine
CC cells that reside as single cells scattered among enterocytes in the
CC mucosa of the small intestine. Released into the blood following
CC ingestion of a meal. {ECO:0000269|PubMed:23863714}.
CC -!- PTM: The precursor is cleaved by proteases to produce a number of
CC active cholecystokinins.
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000305}.
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DR EMBL; X59521; CAB94216.1; -; Genomic_DNA.
DR EMBL; X59522; CAB94216.1; JOINED; Genomic_DNA.
DR EMBL; AK002677; BAB22279.1; -; mRNA.
DR EMBL; M11739; AAA37382.1; -; mRNA.
DR CCDS; CCDS23631.1; -.
DR PIR; S22563; S22563.
DR RefSeq; NP_001271437.1; NM_001284508.2.
DR RefSeq; NP_112438.1; NM_031161.4.
DR RefSeq; XP_017168605.1; XM_017313116.1.
DR AlphaFoldDB; P09240; -.
DR SMR; P09240; -.
DR BioGRID; 198541; 1.
DR STRING; 10090.ENSMUSP00000035120; -.
DR PhosphoSitePlus; P09240; -.
DR PaxDb; P09240; -.
DR PeptideAtlas; P09240; -.
DR PRIDE; P09240; -.
DR ProteomicsDB; 265611; -.
DR Antibodypedia; 29187; 272 antibodies from 34 providers.
DR DNASU; 12424; -.
DR Ensembl; ENSMUST00000035120; ENSMUSP00000035120; ENSMUSG00000032532.
DR Ensembl; ENSMUST00000215228; ENSMUSP00000149679; ENSMUSG00000032532.
DR GeneID; 12424; -.
DR KEGG; mmu:12424; -.
DR UCSC; uc009sdg.3; mouse.
DR CTD; 885; -.
DR MGI; MGI:88297; Cck.
DR VEuPathDB; HostDB:ENSMUSG00000032532; -.
DR eggNOG; ENOG502S472; Eukaryota.
DR GeneTree; ENSGT00390000003571; -.
DR HOGENOM; CLU_169783_0_0_1; -.
DR InParanoid; P09240; -.
DR OMA; YSGLCIC; -.
DR OrthoDB; 1524113at2759; -.
DR PhylomeDB; P09240; -.
DR TreeFam; TF333419; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 12424; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Cck; mouse.
DR PRO; PR:P09240; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P09240; protein.
DR Bgee; ENSMUSG00000032532; Expressed in primary motor cortex and 140 other tissues.
DR ExpressionAtlas; P09240; baseline and differential.
DR Genevisible; P09240; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043203; C:axon hillock; ISO:MGI.
DR GO; GO:0043194; C:axon initial segment; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0005184; F:neuropeptide hormone activity; IDA:MGI.
DR GO; GO:0051428; F:peptide hormone receptor binding; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0007586; P:digestion; IBA:GO_Central.
DR GO; GO:0042755; P:eating behavior; IDA:MGI.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0032099; P:negative regulation of appetite; ISO:MGI.
DR GO; GO:2000986; P:negative regulation of behavioral fear response; ISO:MGI.
DR GO; GO:1903999; P:negative regulation of eating behavior; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:MGI.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0008542; P:visual learning; ISO:MGI.
DR InterPro; IPR015499; CCK-like.
DR InterPro; IPR001651; Gastrin/CCK.
DR InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR PANTHER; PTHR10786; PTHR10786; 1.
DR Pfam; PF00918; Gastrin; 1.
DR PROSITE; PS00259; GASTRIN; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Hormone; Reference proteome;
KW Secreted; Signal; Sulfation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..115
FT /note="Cholecystokinin"
FT /id="PRO_0000010552"
FT PROPEP 21..70
FT /id="PRO_0000010553"
FT PEPTIDE 71..103
FT /note="Cholecystokinin-33"
FT /id="PRO_0000010554"
FT PEPTIDE 92..103
FT /note="Cholecystokinin-12"
FT /id="PRO_0000010555"
FT PEPTIDE 96..103
FT /note="Cholecystokinin-8"
FT /id="PRO_0000010556"
FT PROPEP 107..115
FT /id="PRO_0000010557"
FT MOD_RES 97
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9TS44"
FT MOD_RES 103
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:3862083"
FT MOD_RES 111
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 113
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CONFLICT 37
FT /note="Q -> E (in Ref. 1; CAB94216)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="T -> P (in Ref. 1; CAB94216)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="G -> R (in Ref. 1; CAB94216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 115 AA; 12770 MW; 7841B11D39BB52DA CRC64;
MKSGVCLCVV MAVLAAGALA QPVVPAEATD PVEQRAQEAP RRQLRAVLRT DGEPRARLGA
LLARYIQQVR KAPSGRMSVL KNLQSLDPSH RISDRDYMGW MDFGRRSAED YEYPS
