ID   COL_RABIT               Reviewed;         107 AA.
AC   P42890;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Colipase;
DE   Flags: Precursor;
GN   Name=CLPS;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=8344444; DOI=10.1016/0020-711x(93)90244-9;
RA   Colwell N.S., Aleman-Gomez J.A., Sasser T.L., Kumar V.B.;
RT   "Cloning and characterization of rabbit pancreatic colipase.";
RL   Int. J. Biochem. 25:885-890(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}.
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DR   EMBL; L06329; AAA02911.1; -; mRNA.
DR   RefSeq; NP_001075712.1; NM_001082243.1.
DR   AlphaFoldDB; P42890; -.
DR   SMR; P42890; -.
DR   STRING; 9986.ENSOCUP00000024363; -.
DR   GeneID; 100009061; -.
DR   KEGG; ocu:100009061; -.
DR   CTD; 1208; -.
DR   eggNOG; ENOG502S4NY; Eukaryota.
DR   InParanoid; P42890; -.
DR   OrthoDB; 1504784at2759; -.
DR   Proteomes; UP000001811; 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   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                   /evidence="ECO:0000255"
FT   PROPEP          18..22
FT                   /note="Enterostatin, activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000005704"
FT   CHAIN           23..107
FT                   /note="Colipase"
FT                   /id="PRO_0000005705"
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   107 AA;  11271 MW;  825BA1AEB1422390 CRC64;
     MEKVLVLLLV ALSVAYAAPG PRGIVINLEE GELCLNSAQC KSGCCHHSSA LSLARCAPKA
     SENSECSPQT IYGVYYKCPC ERGLTCEGDK SIVGSITNTN FGVCLDV