COL_PIG
ID COL_PIG Reviewed; 112 AA.
AC P02703; Q3I5G6; Q9N1T6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Colipase;
DE AltName: Full=Procolipase II;
DE Flags: Precursor;
GN Name=CLPS;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=10092856; DOI=10.1046/j.1432-1327.1999.00091.x;
RA Darnis S., Juge N., Marino C., Aviles F.X., Puigserver A., Chaix J.-C.,
RA Guo X.-J.;
RT "Cloning, sequencing and functional expression of a cDNA encoding porcine
RT pancreatic preprocarboxypeptidase A1.";
RL Eur. J. Biochem. 259:719-725(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pan G., Liu Y.G., Xiong Y.Z.;
RT "Polymorphism of Sus scrofa gene encoding pancreatic colipase.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 18-112.
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 [4]
RP PROTEIN SEQUENCE OF 23-108.
RX PubMed=4858821; DOI=10.1016/0005-2795(74)90142-1;
RA Charles M., Erlanson C., Bianchetta J.D., Joffre J., Guidoni A.A.,
RA Rovery M.;
RT "The primary structure of porcine colipase II. I. The amino acid
RT sequence.";
RL Biochim. Biophys. Acta 359:186-197(1974).
RN [5]
RP DISULFIDE BONDS.
RX PubMed=4603223; DOI=10.1016/0005-2795(74)90143-3;
RA Erlanson C., Charles M., Astier M., Desnuelle P.;
RT "The primary structure of porcine colipase II. II. The disulfide bridges.";
RL Biochim. Biophys. Acta 359:198-203(1974).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-112 IN COMPLEX WITH PNLIP.
RX PubMed=1522902; DOI=10.1038/359159a0;
RA van Tilbeurgh H., Sarda L., Verger R., Cambillau C.;
RT "Structure of the pancreatic lipase-procolipase complex.";
RL Nature 359:159-162(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP.
RX PubMed=8479519; DOI=10.1038/362814a0;
RA van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R.,
RA Cambillau C.;
RT "Interfacial activation of the lipase-procolipase complex by mixed micelles
RT revealed by X-ray crystallography.";
RL Nature 362:814-820(1993).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP, AND
RP DISULFIDE BONDS.
RX PubMed=7773176; DOI=10.1002/pro.5560040107;
RA Egloff M.-P., Sarda L., Verger R., Cambillau C., van Tilbeurgh H.;
RT "Crystallographic study of the structure of colipase and of the interaction
RT with pancreatic lipase.";
RL Protein Sci. 4:44-57(1995).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP.
RX PubMed=8663362; DOI=10.1074/jbc.271.30.18007;
RA Hermoso J., Pignol D., Kerfelec B., Crenon I., Chapus C.,
RA Fontecilla-Camps J.-C.;
RT "Lipase activation by nonionic detergents. The crystal structure of the
RT porcine lipase-colipase-tetraethylene glycol monooctyl ether complex.";
RL J. Biol. Chem. 271:18007-18016(1996).
RN [10]
RP STRUCTURE BY NMR OF 18-110, AND SEQUENCE REVISION TO 54.
RX PubMed=7867624; DOI=10.1111/j.1432-1033.1995.tb20186.x;
RA Breg J.N., Sarda L., Cozzone P.J., Rugani N., Boelens R., Kaptein R.;
RT "Solution structure of porcine pancreatic procolipase as determined from 1H
RT homonuclear two-dimensional and three-dimensional NMR.";
RL Eur. J. Biochem. 227:663-672(1995).
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, ECO:0000269|PubMed:1522902,
CC ECO:0000269|PubMed:7773176, ECO:0000269|PubMed:8479519,
CC ECO:0000269|PubMed:8663362}.
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; AF148567; AAF67823.1; -; mRNA.
DR EMBL; DQ073448; AAZ22441.1; -; Genomic_DNA.
DR PIR; A03162; XLPG2.
DR RefSeq; NP_999368.1; NM_214203.1.
DR RefSeq; XP_013833274.1; XM_013977820.1.
DR RefSeq; XP_013833275.1; XM_013977821.1.
DR RefSeq; XP_013833276.1; XM_013977822.1.
DR PDB; 1ETH; X-ray; 2.80 A; B/D=18-110.
DR PDB; 1LPA; X-ray; 3.04 A; A=18-110.
DR PDB; 1LPB; X-ray; 2.46 A; A=18-110.
DR PDB; 1N8S; X-ray; 3.04 A; C=18-110.
DR PDB; 1PCN; NMR; -; A=18-110.
DR PDB; 1PCO; NMR; -; A=18-110.
DR PDBsum; 1ETH; -.
DR PDBsum; 1LPA; -.
DR PDBsum; 1LPB; -.
DR PDBsum; 1N8S; -.
DR PDBsum; 1PCN; -.
DR PDBsum; 1PCO; -.
DR AlphaFoldDB; P02703; -.
DR SMR; P02703; -.
DR CORUM; P02703; -.
DR MINT; P02703; -.
DR STRING; 9823.ENSSSCP00000001686; -.
DR PaxDb; P02703; -.
DR PRIDE; P02703; -.
DR Ensembl; ENSSSCT00000001730; ENSSSCP00000001686; ENSSSCG00000001552.
DR Ensembl; ENSSSCT00005055798; ENSSSCP00005034371; ENSSSCG00005034951.
DR Ensembl; ENSSSCT00015055872; ENSSSCP00015022451; ENSSSCG00015041628.
DR Ensembl; ENSSSCT00025057466; ENSSSCP00025024313; ENSSSCG00025042417.
DR Ensembl; ENSSSCT00030103441; ENSSSCP00030047770; ENSSSCG00030073834.
DR Ensembl; ENSSSCT00035023368; ENSSSCP00035008701; ENSSSCG00035018119.
DR Ensembl; ENSSSCT00040013803; ENSSSCP00040005296; ENSSSCG00040010604.
DR Ensembl; ENSSSCT00045061123; ENSSSCP00045042936; ENSSSCG00045035599.
DR Ensembl; ENSSSCT00050083332; ENSSSCP00050035785; ENSSSCG00050061146.
DR Ensembl; ENSSSCT00055024958; ENSSSCP00055019814; ENSSSCG00055012669.
DR Ensembl; ENSSSCT00060107621; ENSSSCP00060047727; ENSSSCG00060078045.
DR Ensembl; ENSSSCT00065052211; ENSSSCP00065022705; ENSSSCG00065038190.
DR Ensembl; ENSSSCT00070009061; ENSSSCP00070007439; ENSSSCG00070004798.
DR GeneID; 397407; -.
DR KEGG; ssc:397407; -.
DR CTD; 1208; -.
DR VGNC; VGNC:103927; CLPS.
DR eggNOG; ENOG502S4NY; Eukaryota.
DR GeneTree; ENSGT00390000012644; -.
DR HOGENOM; CLU_165591_0_0_1; -.
DR InParanoid; P02703; -.
DR OMA; NSIQCKS; -.
DR OrthoDB; 1504784at2759; -.
DR TreeFam; TF336178; -.
DR EvolutionaryTrace; P02703; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Chromosome 7.
DR Bgee; ENSSSCG00000001552; Expressed in oocyte and 7 other tissues.
DR ExpressionAtlas; P02703; baseline.
DR Genevisible; P02703; SS.
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 1: Evidence at protein level;
KW 3D-structure; Digestion; Direct protein sequencing; Disulfide bond;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:6691986"
FT PROPEP 18..22
FT /note="Enterostatin, activation peptide"
FT /evidence="ECO:0000269|PubMed:4858821"
FT /id="PRO_0000005702"
FT CHAIN 23..112
FT /note="Colipase"
FT /id="PRO_0000005703"
FT DISULFID 34..45
FT DISULFID 40..56
FT DISULFID 44..78
FT DISULFID 66..86
FT DISULFID 80..104
FT CONFLICT 54
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="D -> N (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..112
FT /note="SD -> DS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1ETH"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1PCN"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1LPB"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:1LPB"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1LPB"
SQ SEQUENCE 112 AA; 12140 MW; AE0AE89956E5A846 CRC64;
MEKVLALLLV TLTVAYAVPD PRGIIINLDE GELCLNSAQC KSNCCQHDTI LSLSRCALKA
RENSECSAFT LYGVYYKCPC ERGLTCEGDK SLVGSITNTN FGICHDVGRS SD
