COL_BOVIN
ID COL_BOVIN Reviewed; 112 AA.
AC A0JNQ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Colipase;
DE Flags: Precursor;
GN Name=CLPS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pancreas;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-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: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 {ECO:0000255|PROSITE-ProRule:PRU00674}.
CC -!- SIMILARITY: Belongs to the colipase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00674}.
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DR EMBL; BC126854; AAI26855.1; -; mRNA.
DR EMBL; BC142041; AAI42042.1; -; mRNA.
DR RefSeq; NP_001071435.1; NM_001077967.2.
DR AlphaFoldDB; A0JNQ7; -.
DR SMR; A0JNQ7; -.
DR STRING; 9913.ENSBTAP00000022391; -.
DR PaxDb; A0JNQ7; -.
DR Ensembl; ENSBTAT00000022391; ENSBTAP00000022391; ENSBTAG00000016833.
DR GeneID; 525923; -.
DR KEGG; bta:525923; -.
DR CTD; 1208; -.
DR VEuPathDB; HostDB:ENSBTAG00000016833; -.
DR VGNC; VGNC:53963; CLPS.
DR eggNOG; ENOG502S4NY; Eukaryota.
DR GeneTree; ENSGT00390000012644; -.
DR HOGENOM; CLU_165591_0_0_1; -.
DR InParanoid; A0JNQ7; -.
DR OMA; NSIQCKS; -.
DR OrthoDB; 1504784at2759; -.
DR TreeFam; TF336178; -.
DR Reactome; R-BTA-192456; Digestion of dietary lipid.
DR Reactome; R-BTA-975634; Retinoid metabolism and transport.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000016833; Expressed in urinary bladder and 13 other tissues.
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:0009617; P:response to bacterium; IEA:Ensembl.
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 3: Inferred from homology;
KW Digestion; Disulfide bond; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT PROPEP 18..22
FT /note="Enterostatin, activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000314946"
FT CHAIN 23..112
FT /note="Colipase"
FT /id="PRO_0000314947"
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 112 AA; 12051 MW; 949B4F9BB9250BC0 CRC64;
MEKVLILLLV ALAVAYAVPD PRGIIINLDE GELCLNSAQC TSKCCHREDG LSLARCAPKA
SENSECSAFT LYGIYYKCPC ERGLTCNVDK TIVGSITNTN FGVCLDLGRA TE
