Reviewed, UniProtKB/Swiss-Prot P02703 (COL_PIG)

Names and origin

Protein names

Recommended name:
    Colipase
Alternative name(s):
    Procolipase II

Gene names

Name:

CLPS

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	112 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase. Enterostatin has a biological activity as a satiety signal.
Subunit structure	Forms a 1:1 stoichiometric complex with pancreatic lipase.
Subcellular location	Secreted.
Tissue specificity	Expressed by the pancreas.
Sequence similarities	Belongs to the colipase family.

Ontologies

Keywords
Biological process	Digestion Lipid degradation
Cellular component	Secreted
Domain	Signal
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	digestion Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	enzyme activator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.3

Propeptide

18 – 22

5

Enterostatin, activation peptide Ref.4

PRO_0000005702

Chain

23 – 112

90

Colipase

PRO_0000005703

Amino acid modifications

Disulfide bond

34 ↔ 45

Ref.5 Ref.8

Disulfide bond

40 ↔ 56

Ref.5 Ref.8

Disulfide bond

44 ↔ 78

Ref.5 Ref.8

Disulfide bond

66 ↔ 86

Ref.5 Ref.8

Disulfide bond

80 ↔ 104

Ref.5 Ref.8

Experimental info

Sequence conflict

54

1

Missing AA sequence Ref.4

Sequence conflict

67

1

Missing AA sequence Ref.4

Sequence conflict

106

1

D → N AA sequence Ref.3

Sequence conflict

106

1

D → N AA sequence Ref.4

Sequence conflict

111 – 112

2

SD → DS AA sequence Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

112

Helix Strand Turn

Details...

Helix

37 – 39

3

Beta strand

40 – 43

4

Beta strand

48 – 52

5

Beta strand

64 – 67

4

Beta strand

71 – 77

7

Beta strand

84 – 88

5

Helix

92 – 97

6

Beta strand

101 – 106

6

Sequences

	Sequence		Length	Mass (Da)
	P02703-1 [UniParc]. Last modified October 25, 2002. Version 3. Checksum: AE0AE89956E5A846	FASTA	112	12,140
	10 20 30 40 50 60 MEKVLALLLV TLTVAYAVPD PRGIIINLDE GELCLNSAQC KSNCCQHDTI LSLSRCALKA 70 80 90 100 110 RENSECSAFT LYGVYYKCPC ERGLTCEGDK SLVGSITNTN FGICHDVGRS SD

References

[1]	"Cloning, sequencing and functional expression of a cDNA encoding porcine pancreatic preprocarboxypeptidase A1." Darnis S., Juge N., Marino C., Aviles F.X., Puigserver A., Chaix J.-C., Guo X.-J. Eur. J. Biochem. 259:719-725(1999) [PubMed: 10092856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pancreas.
[2]	"Polymorphism of Sus scrofa gene encoding pancreatic colipase." Pan G., Liu Y.G., Xiong Y.Z. Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The primary sequence of human pancreatic colipase." Sternby B., Engstroem A., Hellman U., Vihert A.M., Sternby N.-H., Borgstroem B. Biochim. Biophys. Acta 784:75-80(1984) [PubMed: 6691986] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-112.
[4]	"The primary structure of porcine colipase II. I. The amino acid sequence." Charles M., Erlanson C., Bianchetta J.D., Joffre J., Guidoni A.A., Rovery M. Biochim. Biophys. Acta 359:186-197(1974) [PubMed: 4858821] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-108.
[5]	"The primary structure of porcine colipase II. II. The disulfide bridges." Erlanson C., Charles M., Astier M., Desnuelle P. Biochim. Biophys. Acta 359:198-203(1974) [PubMed: 4603223] [Abstract] Cited for: DISULFIDE BONDS.
[6]	"Structure of the pancreatic lipase-procolipase complex." van Tilbeurgh H., Sarda L., Verger R., Cambillau C. Nature 359:159-162(1992) [PubMed: 1522902] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-112 IN COMPLEX WITH PNLIP.
[7]	"Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography." van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R., Cambillau C. Nature 362:814-820(1993) [PubMed: 8479519] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP.
[8]	"Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase." Egloff M.-P., Sarda L., Verger R., Cambillau C., van Tilbeurgh H. Protein Sci. 4:44-57(1995) [PubMed: 7773176] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP, DISULFIDE BONDS.
[9]	"Lipase activation by nonionic detergents. The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex." Hermoso J., Pignol D., Kerfelec B., Crenon I., Chapus C., Fontecilla-Camps J.-C. J. Biol. Chem. 271:18007-18016(1996) [PubMed: 8663362] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP.
[10]	"Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR." Breg J.N., Sarda L., Cozzone P.J., Rugani N., Boelens R., Kaptein R. Eur. J. Biochem. 227:663-672(1995) [PubMed: 7867624] [Abstract] Cited for: STRUCTURE BY NMR OF 18-110, SEQUENCE REVISION TO 54.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF148567 mRNA. Translation: AAF67823.1.
DQ073448 Genomic DNA. Translation: AAZ22441.1.

PIR

XLPG2. A03162.

RefSeq

NP_999368.1.

UniGene

Ssc.514

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ETH	X-ray	2.80	B/D	18-110	[»]
1LPA	X-ray	3.04	A	18-110	[»]
1LPB	X-ray	2.46	A	18-110	[»]
1N8S	X-ray	3.04	C	18-110	[»]
1PCN	NMR	-	A	18-110	[»]
1PCO	NMR	-	A	18-110	[»]

ModBase

Search...

Genome annotation databases

GeneID

397407.

KEGG

ssc:397407.

Phylogenomic databases

HOVERGEN

P02703.

Family and domain databases

InterPro

IPR001981. Colipase.
IPR017914. Colipase_C.
IPR017915. Colipase_CS.
IPR017913. Colipase_N.
IPR018100. Colipase_subgroup.
[Graphical view]

Pfam

PF01114. Colipase. 1 hit.
PF02740. Colipase_C. 1 hit.
[Graphical view]

PRINTS

PR00128. COLIPASE.

SMART

SM00023. COLIPASE. 1 hit.
[Graphical view]

PROSITE

PS00121. COLIPASE_1. 1 hit.
PS51342. COLIPASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

COL_PIG

Accession

Primary (citable) accession number: P02703
Secondary accession number(s): Q3I5G6, Q9N1T6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 25, 2002
Last modified:	June 16, 2009
This is version 74 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)