ID   COL_XENTR               Reviewed;         117 AA.
AC   A9JSD6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Colipase;
DE   Flags: Precursor;
GN   Name=clps;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Nigerian; TISSUE=Pancreas;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|PROSITE-ProRule:PRU00674}.
CC   -!- SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase.
CC       {ECO:0000255|PROSITE-ProRule:PRU00674}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00674}.
CC   -!- SIMILARITY: Belongs to the colipase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00674}.
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DR   EMBL; BC156015; AAI56016.1; -; mRNA.
DR   RefSeq; NP_001107327.1; NM_001113855.1.
DR   AlphaFoldDB; A9JSD6; -.
DR   SMR; A9JSD6; -.
DR   STRING; 8364.ENSXETP00000062838; -.
DR   PaxDb; A9JSD6; -.
DR   GeneID; 100135140; -.
DR   KEGG; xtr:100135140; -.
DR   CTD; 1208; -.
DR   Xenbase; XB-GENE-982642; clps.
DR   eggNOG; ENOG502S4NY; Eukaryota.
DR   HOGENOM; CLU_165591_0_0_1; -.
DR   InParanoid; A9JSD6; -.
DR   OMA; NSIQCKS; -.
DR   OrthoDB; 1504784at2759; -.
DR   PhylomeDB; A9JSD6; -.
DR   TreeFam; TF336178; -.
DR   Reactome; R-XTR-192456; Digestion of dietary lipid.
DR   Reactome; R-XTR-975634; Retinoid metabolism and transport.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; 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   3: Inferred from homology;
KW   Digestion; Disulfide bond; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..117
FT                   /note="Colipase"
FT                   /id="PRO_0000337012"
FT   DISULFID        39..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        45..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        49..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        71..91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT   DISULFID        85..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
SQ   SEQUENCE   117 AA;  12717 MW;  5B8C290C1BA3006F CRC64;
     MNIFNILLPI VVLLLVFGLT AAIPDEKGLI FNLDNGELCL QTAQCKSGCC HRNSGVSLAR
     CAPKAAETQK CSPLHIYGTY YFCPCESGLT CEVDRSIVGS ITNTDYGYCE DQNNTTI