ID   COLA_HORSE              Reviewed;         106 AA.
AC   P02704;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Colipase A;
DE   Flags: Precursor; Fragment;
GN   Name=CLPS1;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=8049250; DOI=10.1016/0005-2760(94)00096-4;
RA   Crenon I., Granon S., Chapus C., Kerfelec B.;
RT   "Molecular cloning and expression of two horse pancreatic cDNA encoding
RT   colipase A and B.";
RL   Biochim. Biophys. Acta 1213:357-360(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 12-106.
RC   TISSUE=Pancreas;
RX   PubMed=6691986; DOI=10.1016/0167-4838(84)90175-4;
RA   Sternby B., Engstroem A., Hellman U., Vihert A.M., Sternby N.-H.,
RA   Borgstroem B.;
RT   "The primary sequence of human pancreatic colipase.";
RL   Biochim. Biophys. Acta 784:75-80(1984).
RN   [3]
RP   PROTEIN SEQUENCE OF 12-106, AND TAURODEOXYCHOLATE-BINDING.
RX   PubMed=7075593; DOI=10.1111/j.1432-1033.1982.tb19774.x;
RA   Pierrot M., Astier J.-P., Astier M., Charles M., Drenth J.;
RT   "Pancreatic colipase: crystallographic and biochemical aspects.";
RL   Eur. J. Biochem. 123:347-354(1982).
RN   [4]
RP   PROTEIN SEQUENCE OF 12-66.
RX   PubMed=7417313; DOI=10.1016/0006-291x(80)91607-1;
RA   Julien R., Bechis G., Gregoire J., Rathelot J., Rochat H., Sarda L.;
RT   "Evidence for the existence of two isocolipases in horse pancreas.";
RL   Biochem. Biophys. Res. Commun. 95:1245-1252(1980).
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   -!- FUNCTION: Enterostatin has a biological activity as a satiety signal.
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   EMBL; X74503; CAA52611.1; -; mRNA.
DR   PIR; A03164; XLHOA.
DR   AlphaFoldDB; P02704; -.
DR   SMR; P02704; -.
DR   InParanoid; P02704; -.
DR   Proteomes; UP000002281; 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   1: Evidence at protein level;
KW   Digestion; Direct protein sequencing; Disulfide bond; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Secreted; Signal.
FT   SIGNAL          <1..11
FT                   /evidence="ECO:0000269|PubMed:6691986,
FT                   ECO:0000269|PubMed:7075593, ECO:0000269|PubMed:7417313"
FT   PROPEP          12..16
FT                   /note="Enterostatin, activation peptide"
FT                   /id="PRO_0000005692"
FT   CHAIN           17..106
FT                   /note="Colipase A"
FT                   /id="PRO_0000005693"
FT   BINDING         63
FT                   /ligand="taurodeoxycholate"
FT                   /ligand_id="ChEBI:CHEBI:36261"
FT                   /evidence="ECO:0000305|PubMed:7075593"
FT   DISULFID        28..39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        34..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        38..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        60..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        74..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   CONFLICT        33
FT                   /note="Q -> E (in Ref. 2; AA sequence and 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="S -> E (in Ref. 2; AA sequence, 3; AA sequence and
FT                   4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="D -> N (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="R -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="E -> ER (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   106 AA;  11388 MW;  C0DC26747D94810C CRC64;
     LLLVALAVAY AVPDPRGVII NLEAGEICLN SAQCKSECCH QESSLSLARC AAKASENSEC
     SAWTLYGVYY KCPCERGLTC QVDKTLVGSI MNTNFGICFD AARSEE