ID   COL_CANLF               Reviewed;         112 AA.
AC   P19090;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Colipase;
DE   Flags: Precursor;
GN   Name=CLPS;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=2216731; DOI=10.1093/nar/18.18.5549;
RA   Fukuoka S., Taniguchi Y., Kitagawa Y., Scheele G.;
RT   "Full length cDNA sequence encoding canine pancreatic colipase.";
RL   Nucleic Acids Res. 18:5549-5549(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Pancreas;
RX   PubMed=7684378; DOI=10.1016/s0021-9258(18)82126-3;
RA   Fukuoka S., Zhang D.E., Taniguchi Y., Scheele G.A.;
RT   "Structure of the canine pancreatic colipase gene includes two protein-
RT   binding sites in the promoter region.";
RL   J. Biol. Chem. 268:11312-11320(1993).
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:0000250|UniProtKB:P04118}.
CC   -!- FUNCTION: Enterostatin has a biological activity as a satiety signal.
CC       {ECO:0000250|UniProtKB:P04118}.
CC   -!- SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase.
CC       {ECO:0000250|UniProtKB:P04118}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the pancreas.
CC   -!- SIMILARITY: Belongs to the colipase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00674}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X53564; CAA37636.1; -; mRNA.
DR   EMBL; M63427; AAA03513.1; -; Unassigned_DNA.
DR   PIR; A46717; A46717.
DR   RefSeq; NP_001003287.1; NM_001003287.1.
DR   AlphaFoldDB; P19090; -.
DR   SMR; P19090; -.
DR   STRING; 9612.ENSCAFP00000001934; -.
DR   PaxDb; P19090; -.
DR   GeneID; 403970; -.
DR   KEGG; cfa:403970; -.
DR   CTD; 1208; -.
DR   eggNOG; ENOG502S4NY; Eukaryota.
DR   HOGENOM; CLU_165591_0_0_1; -.
DR   InParanoid; P19090; -.
DR   OMA; NSIQCKS; -.
DR   OrthoDB; 1504784at2759; -.
DR   TreeFam; TF336178; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0032094; P:response to food; IBA:GO_Central.
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_0000005690"
FT   CHAIN           23..112
FT                   /note="Colipase"
FT                   /id="PRO_0000005691"
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"
SQ   SEQUENCE   112 AA;  12035 MW;  96EB5B821BA8CA71 CRC64;
     MEKILVLLLV ALAVVYAVPD PRGIIIHLED GELCLNSVQC KSKCCHRATG LSLARCAPKA
     SENSECSAKT LYGVYYKCPC ERGLTCEGDK SIVGSITNTN FGVCHDAGRS KK