ID   COL_MYOCO               Reviewed;         111 AA.
AC   P42889;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Colipase;
DE   Flags: Precursor;
GN   Name=CLPS;
OS   Myocastor coypus (Coypu) (Nutria).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC   Myocastoridae; Myocastor.
OX   NCBI_TaxID=10157;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-41.
RC   TISSUE=Pancreas;
RX   PubMed=7851384; DOI=10.1111/j.1432-1033.1995.tb20375.x;
RA   Thirstrup K., Carriere F., Hjorth S.A., Rasmussen P.B., Nielsen P.F.,
RA   Ladefoged C., Thim L., Boel E.;
RT   "Cloning and expression in insect cells of two pancreatic lipases and a
RT   procolipase from Myocastor coypus.";
RL   Eur. J. Biochem. 227:186-193(1995).
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:0000255|PROSITE-ProRule:PRU00674}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the pancreas.
CC   -!- SIMILARITY: Belongs to the colipase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00674}.
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DR   EMBL; X82998; CAA58119.1; -; mRNA.
DR   PIR; I48204; I48204.
DR   AlphaFoldDB; P42889; -.
DR   SMR; P42889; -.
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   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   1: Evidence at protein level;
KW   Digestion; Direct protein sequencing; Disulfide bond; Lipid degradation;
KW   Lipid metabolism; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:7851384"
FT   PROPEP          18..22
FT                   /note="Enterostatin, activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000005700"
FT   CHAIN           23..111
FT                   /note="Colipase"
FT                   /id="PRO_0000005701"
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   111 AA;  11899 MW;  7FF37DE7C169616B CRC64;
     MEKVLALVLL TLAVAYAAPD PRGLIINLDN GELCLNSAQC KSQCCQHDSP LGLARCADKA
     RENSGCSPQT IYGIYYLCPC ERGLTCDGDK SIIGAITNTN YGICQDPQSK K