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P11148 (COL_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length34 AA.
Sequence statusFragment.
Protein existenceEvidence 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.

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 processDigestion
Lipid degradation
Lipid metabolism
   Cellular componentSecreted
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionenzyme activator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›34›34Colipase
PRO_0000144831

Amino acid modifications

Disulfide bond12 ↔ 23 By similarity
Disulfide bond18 ↔ 34 By similarity

Experimental info

Sequence uncertainty121
Non-terminal residue341

Sequences

Sequence LengthMass (Da)Tools
P11148 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: 4A646B55FCB83BEB

FASTA343,591
        10         20         30 
GLIFNLDTGE LCLQSAQCKS ECCQEDSGLS LAXC 

« Hide

References

[1]"Evidence for the existence of procolipase in chicken pancreas and pancreatic juice."
Bosc-Bierne I., Rathelot J., Bechis G., Delori P., Sarda L.
Biochimie 66:413-416(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Pancreas.
[2]"Isolation and partial structural characterization of chicken pancreatic colipase."
Bosc-Bierne I., Rathelot J., Canioni P., Julien R., Bechis G., Gregorie J., Rochat H., Sarda L.
Biochim. Biophys. Acta 667:225-232(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Pancreas.

Cross-references

Sequence databases

PIRA05330.
UniGeneGga.6607.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000001320.

Proteomic databases

PaxDbP11148.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG42456.
HOGENOMHOG000059253.
InParanoidP11148.

Family and domain databases

InterProIPR001981. Colipase.
IPR017913. Colipase_N.
[Graphical view]
PfamPF01114. Colipase. 1 hit.
[Graphical view]
PROSITEPS51342. COLIPASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOL_CHICK
AccessionPrimary (citable) accession number: P11148
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families