ID   COL_RAT                 Reviewed;         112 AA.
AC   P17084;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Colipase {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Clps {ECO:0000312|RGD:2363};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY LIPID
RP   INGESTION.
RX   PubMed=2129524; DOI=10.1016/0006-291x(90)91740-j;
RA   Wicker C., Puigserver A.;
RT   "Rat pancreatic colipase mRNA: nucleotide sequence of a cDNA clone and
RT   nutritional regulation by a lipidic diet.";
RL   Biochem. Biophys. Res. Commun. 167:130-136(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   FUNCTION.
RX   PubMed=8203536; DOI=10.1152/ajpgi.1994.266.5.g914;
RA   Payne R.M., Sims H.F., Jennens M.L., Lowe M.E.;
RT   "Rat pancreatic lipase and two related proteins: enzymatic properties and
RT   mRNA expression during development.";
RL   Am. J. Physiol. 266:G914-G921(1994).
CC   -!- FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows the
CC       lipase to anchor itself to the lipid-water interface. Without colipase
CC       the enzyme is washed off by bile salts, which have an inhibitory effect
CC       on the lipase. {ECO:0000269|PubMed:8203536}.
CC   -!- FUNCTION: Enterostatin has a biological activity as a satiety signal.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase.
CC       {ECO:0000255|PROSITE-ProRule:PRU00674}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the pancreas.
CC       {ECO:0000269|PubMed:2129524, ECO:0000269|PubMed:8203536}.
CC   -!- DEVELOPMENTAL STAGE: Readily detectable during gestation, reaches adult
CC       levels by 17-20 days gestation, rises markedly at 7 days of age but
CC       falls to adult levels by 14 days and remains at that level throughout
CC       the suckling-weanling period. {ECO:0000269|PubMed:8203536}.
CC   -!- INDUCTION: Expression levels increase upon lipid ingestion.
CC       {ECO:0000269|PubMed:2129524}.
CC   -!- SIMILARITY: Belongs to the colipase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00674}.
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DR   EMBL; M33333; AAA40943.1; -; mRNA.
DR   EMBL; M58370; AAA20505.1; -; mRNA.
DR   PIR; I51909; I51909.
DR   RefSeq; NP_037271.1; NM_013139.1.
DR   AlphaFoldDB; P17084; -.
DR   SMR; P17084; -.
DR   STRING; 10116.ENSRNOP00000000611; -.
DR   PaxDb; P17084; -.
DR   GeneID; 25680; -.
DR   KEGG; rno:25680; -.
DR   UCSC; RGD:2363; rat.
DR   CTD; 1208; -.
DR   RGD; 2363; Clps.
DR   eggNOG; ENOG502S4NY; Eukaryota.
DR   InParanoid; P17084; -.
DR   PhylomeDB; P17084; -.
DR   Reactome; R-RNO-192456; Digestion of dietary lipid.
DR   Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR   PRO; PR:P17084; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008047; F:enzyme activator activity; IDA:RGD.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IDA:RGD.
DR   GO; GO:0009791; P:post-embryonic development; IEP:RGD.
DR   GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR   GO; GO:0032094; P:response to food; IEP:RGD.
DR   CDD; cd00039; COLIPASE; 1.
DR   InterPro; IPR001981; Colipase.
DR   InterPro; IPR017914; Colipase_C.
DR   InterPro; IPR017915; Colipase_CS.
DR   InterPro; IPR017913; Colipase_N.
DR   PANTHER; PTHR10041; PTHR10041; 1.
DR   Pfam; PF01114; Colipase; 1.
DR   Pfam; PF02740; Colipase_C; 1.
DR   PRINTS; PR00128; COLIPASE.
DR   SMART; SM00023; COLIPASE; 1.
DR   PROSITE; PS00121; COLIPASE_1; 1.
DR   PROSITE; PS51342; COLIPASE_2; 1.
PE   2: Evidence at transcript level;
KW   Digestion; Disulfide bond; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT   PROPEP          18..22
FT                   /note="Enterostatin, activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000005706"
FT   CHAIN           23..112
FT                   /note="Colipase"
FT                   /id="PRO_0000005707"
FT   DISULFID        34..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        40..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        44..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        66..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        80..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   CONFLICT        18
FT                   /note="A -> V (in Ref. 1; AAA40943)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   112 AA;  12252 MW;  E5B6B7D4A7C05BFA CRC64;
     MKVLVVLLVT LVAVAYAAPG PRGLFINLED GEICVNSMQC KSRCCQHDTI LGIARCTHKA
     MENSECSPKT LYGIYYRCPC ERGLTCEGDR SIIGAITNTN YGVCLDSTRS KQ