ID   COL_CHICK               Reviewed;          34 AA.
AC   P11148;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   10-FEB-2021, entry version 88.
DE   RecName: Full=Colipase;
DE   Flags: Fragment;
GN   Name=CLPS;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=6547861; DOI=10.1016/0300-9084(84)90025-7;
RA   Bosc-Bierne I., Rathelot J., Bechis G., Delori P., Sarda L.;
RT   "Evidence for the existence of procolipase in chicken pancreas and
RT   pancreatic juice.";
RL   Biochimie 66:413-416(1984).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=7213802; DOI=10.1016/0005-2795(81)90187-2;
RA   Bosc-Bierne I., Rathelot J., Canioni P., Julien R., Bechis G., Gregorie J.,
RA   Rochat H., Sarda L.;
RT   "Isolation and partial structural characterization of chicken pancreatic
RT   colipase.";
RL   Biochim. Biophys. Acta 667:225-232(1981).
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.
CC   -!- SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase.
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   PIR; A05330; A05330.
DR   STRING; 9031.ENSGALP00000001320; -.
DR   eggNOG; ENOG502S4NY; Eukaryota.
DR   InParanoid; P11148; -.
DR   Proteomes; UP000000539; 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   InterPro; IPR001981; Colipase.
DR   InterPro; IPR017913; Colipase_N.
DR   Pfam; PF01114; Colipase; 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; Reference proteome; Secreted.
FT   CHAIN           1..>34
FT                   /note="Colipase"
FT                   /id="PRO_0000144831"
FT   DISULFID        12..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        18..34
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   UNSURE          12
FT   NON_TER         34
SQ   SEQUENCE   34 AA;  3591 MW;  4A646B55FCB83BEB CRC64;
     GLIFNLDTGE LCLQSAQCKS ECCQEDSGLS LAXC