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P27917 (APOC3_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein C-III

Short name=Apo-CIII
Short name=ApoC-III
Alternative name(s):
Apolipoprotein C3
Gene names
Name:APOC3
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length96 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits lipoprotein lipase and hepatic lipase and decreases the uptake of lymph chylomicrons by hepatic cells. This suggests that it delays the catabolism of triglyceride-rich particles.

Subcellular location

Secreted.

Tissue specificity

Mainly VLDL and also in HDL. Synthesized predominantly in liver and to a lesser degree in intestine.

Sequence similarities

Belongs to the apolipoprotein C3 family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
Lipid transport
Transport
   Cellular componentChylomicron
Secreted
VLDL
   DomainSignal
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Compara

cholesterol efflux

Inferred from electronic annotation. Source: Compara

cholesterol homeostasis

Inferred from electronic annotation. Source: Compara

cholesterol metabolic process

Inferred from electronic annotation. Source: Compara

chylomicron remnant clearance

Inferred from electronic annotation. Source: Compara

high-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Compara

lipoprotein metabolic process

Inferred from electronic annotation. Source: InterPro

negative regulation of cholesterol import

Inferred from electronic annotation. Source: Compara

negative regulation of fatty acid biosynthetic process

Inferred from electronic annotation. Source: Compara

negative regulation of high-density lipoprotein particle clearance

Inferred from electronic annotation. Source: Compara

negative regulation of lipoprotein lipase activity

Inferred from electronic annotation. Source: Compara

negative regulation of low-density lipoprotein particle clearance

Inferred from electronic annotation. Source: Compara

negative regulation of receptor-mediated endocytosis

Inferred from electronic annotation. Source: Compara

negative regulation of triglyceride catabolic process

Inferred from electronic annotation. Source: Compara

negative regulation of very-low-density lipoprotein particle clearance

Inferred from electronic annotation. Source: Compara

phospholipid efflux

Inferred from electronic annotation. Source: Compara

regulation of Cdc42 protein signal transduction

Inferred from electronic annotation. Source: Compara

triglyceride catabolic process

Inferred from electronic annotation. Source: Compara

triglyceride homeostasis

Inferred from electronic annotation. Source: Compara

triglyceride mobilization

Inferred from electronic annotation. Source: Compara

   Cellular_componentchylomicron

Inferred from electronic annotation. Source: UniProtKB-KW

intermediate-density lipoprotein particle

Inferred from electronic annotation. Source: Compara

spherical high-density lipoprotein particle

Inferred from electronic annotation. Source: Compara

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionlipase inhibitor activity

Inferred from electronic annotation. Source: Compara

phospholipid binding

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 9673Apolipoprotein C-III
PRO_0000002034

Regions

Region68 – 9629Lipid-binding By similarity

Sequences

Sequence LengthMass (Da)Tools
P27917 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: E4AC07F58C8A4DB2

FASTA9610,704
        10         20         30         40         50         60 
MQPRVLLVAG LLVLLACAQA IEAEDTSLLD KMQDYVKQAT RTAQDALTSV KESEVAQQAR 

        70         80         90 
GWVTDSISSL KDYWSTFKGK FTDFWDYTPK PEPSSS 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the apolipoprotein AI and CIII genes in the domestic pig."
Birchbauer A., Knipping G., Juritsch B., Aschauer H., Zechner R.
Genomics 15:643-652(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
Winteroe A.K., Fredholm M., Davies W.
Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Small intestine.
[3]"Sequences and expression of the porcine apolipoprotein A-I and C-III mRNAs."
Trieu V.N., Hasler-Rapacz J., Rapacz J., Black D.D.
Gene 123:173-179(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-96, PROTEIN SEQUENCE OF 34-58.
Tissue: Liver.
[4]Hasler-Rapacz J.O., Chaudhary R., Chowdhary B.P., Trieu V.N., Jackson K., Gustavsson I., Rapacz J.
Submitted (OCT-1995) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 24-96.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00627 Genomic DNA. Translation: AAA30993.1.
F14536 mRNA. Translation: CAA23113.1.
M84133 mRNA. No translation available.
M84134 Genomic DNA. No translation available.
PIRB46018.
RefSeqNP_001002801.1. NM_001002801.1.
UniGeneSsc.53685.
Ssc.96102.

3D structure databases

ProteinModelPortalP27917.
SMRP27917. Positions 22-96.
ModBaseSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000015993.

Proteomic databases

PaxDbP27917.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000016435; ENSSSCP00000015993; ENSSSCG00000015069.
GeneID406187.
KEGGssc:406187.

Organism-specific databases

CTD345.

Phylogenomic databases

eggNOGNOG39866.
GeneTreeENSGT00390000015395.
HOGENOMHOG000247042.
HOVERGENHBG050549.
KOK08759.
OMASLKDYWS.
OrthoDBEOG4WDDDG.

Gene expression databases

ArrayExpressP27917.

Family and domain databases

InterProIPR008403. Apo-CIII.
[Graphical view]
PANTHERPTHR14225. PTHR14225. 1 hit.
PfamPF05778. Apo-CIII. 1 hit.
[Graphical view]
ProDomPD010414. Apo-CIII. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameAPOC3_PIG
AccessionPrimary (citable) accession number: P27917
Secondary accession number(s): Q29208
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1993
Last modified: April 3, 2013
This is version 80 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