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P02654 (APOC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein C-I

Short name=Apo-CIB
Short name=ApoC-IB
Alternative name(s):
Apolipoprotein C1

Cleaved into the following chain:

  1. Truncated apolipoprotein C-I
    Short name=Apo-CIB'
    Short name=ApoC-IB'
Gene names
Name:APOC1
Synonyms:APOC1B
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length83 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to modulate the interaction of APOE with beta-migrating VLDL and inhibit binding of beta-VLDL to the LDL receptor-related protein. Binds free fatty acids and reduces their intracellular esterification. Ref.13

Subcellular location

Secreted.

Tissue specificity

Synthesized mainly in liver and to a minor degree in intestine. Secreted in plasma.

Miscellaneous

Apolipoprotein C-I is present in acidic (APOC1A) and basic (APOC1B) forms in P.paniscus, P.abelii and P.troglodytes and perhaps also in baboons and macaques. In human, the acidic form has become a pseudogene. Apo-CI makes up about 10% of the protein of the VLDL (very low density lipoprotein) and 2% of that of HDL (high density lipoprotein).

Sequence similarities

Belongs to the apolipoprotein C1 family.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentSecreted
VLDL
   Coding sequence diversityPolymorphism
   DomainSignal
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processcholesterol efflux

Inferred from direct assay. Source: BHF-UCL

chylomicron remnant clearance

Inferred from direct assay. Source: BHF-UCL

high-density lipoprotein particle remodeling

Traceable author statement. Source: BHF-UCL

lipoprotein metabolic process

Inferred from electronic annotation. Source: InterPro

negative regulation of cholesterol transport

Inferred from direct assay. Source: BHF-UCL

negative regulation of fatty acid biosynthetic process

Inferred from direct assay. Source: BHF-UCL

negative regulation of lipoprotein lipase activity

Inferred from direct assay. Source: BHF-UCL

negative regulation of phosphatidylcholine catabolic process

Inferred from direct assay. Source: BHF-UCL

negative regulation of receptor-mediated endocytosis

Inferred from direct assay. Source: BHF-UCL

negative regulation of very-low-density lipoprotein particle clearance

Inferred from direct assay. Source: BHF-UCL

phospholipid efflux

Inferred from direct assay. Source: BHF-UCL

positive regulation of cholesterol esterification

Traceable author statement. Source: BHF-UCL

very-low-density lipoprotein particle assembly

Traceable author statement. Source: BHF-UCL

very-low-density lipoprotein particle clearance

Inferred from genetic interaction. Source: BHF-UCL

   Cellular componentchylomicron

Traceable author statement. Source: BHF-UCL

endoplasmic reticulum

Inferred from direct assay. Source: LIFEdb

high-density lipoprotein particle

Inferred from direct assay. Source: BHF-UCL

very-low-density lipoprotein particle

Inferred from direct assay. Source: BHF-UCL

   Molecular functionfatty acid binding

Inferred from direct assay Ref.13. Source: BHF-UCL

phosphatidylcholine binding

Traceable author statement. Source: BHF-UCL

phosphatidylcholine-sterol O-acyltransferase activator activity

Traceable author statement. Source: BHF-UCL

phospholipase inhibitor activity

Inferred from direct assay. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.10 Ref.11
Chain27 – 8357Apolipoprotein C-I
PRO_0000002014
Chain29 – 8355Truncated apolipoprotein C-I By similarity
PRO_0000391843

Natural variations

Natural variant161I → M. Ref.16
Corresponds to variant rs5112 [ dbSNP | Ensembl ].
VAR_014183
Natural variant711T → S Polymorphism found only in persons of American Indian or Mexican ancestry; more susceptible to N-terminal truncation and shows greater distribution to the VLDL than the protein with T-71. Ref.17
VAR_029011

Secondary structure

....... 83
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02654 [UniParc].

Last modified October 23, 1986. Version 1.
Checksum: 4A3614626624AE6A

FASTA839,332
        10         20         30         40         50         60 
MRLFLSLPVL VVVLSIVLEG PAPAQGTPDV SSALDKLKEF GNTLEDKARE LISRIKQSEL 

        70         80 
SAKMREWFSE TFQKVKEKLK IDS 

« Hide

References

« Hide 'large scale' references
[1]"Characterisation of mRNAs encoding the precursor for human apolipoprotein CI."
Knott T.J., Robertson M.E., Priestley L.M., Urdea M., Wallis S.C., Scott J.
Nucleic Acids Res. 12:3909-3915(1984) [PubMed: 6328444] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Two copies of the human apolipoprotein C-I gene are linked closely to the apolipoprotein E gene."
Lauer S.J., Walker D., Elshourbagy N.A., Reardon C.A., Levy-Wilson B., Taylor J.M.
J. Biol. Chem. 263:7277-7286(1988) [PubMed: 2835369] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene: PEREC1."
Freitas E.M., Zhang W.J., Lalonde J.P., Tay G.K., Gaudieri S., Ashworth L.K., Van Bockxmeer F.M., Dawkins R.L.
DNA Seq. 9:89-100(1998) [PubMed: 10520737] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Nickerson D.A., Smith J.D., Fullerton S.M., Clark A.G., Stengard J.H., Salomaa V., Boerwinkle E., Sing C.F., Weiss K.M.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]Bechtel S., Schupp I., Duda A., Wellenreuther R., Mehrle A., Ruschke V., Poustka A., Wiemann S.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[9]"Isolation and characterisation of a cDNA clone for human apolipoprotein CI and assignment of the gene to chromosome 19."
Tata F., Henry I., Markham A.F., Wallis S.C., Weil D., Grzeschik K.H., Junien C., Williamson R., Humphries S.E.
Hum. Genet. 69:345-349(1985) [PubMed: 2985493] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-83.
[10]"Thf complete amino acid sequence of C-I (apoLp-Ser), an apolipoprotein from human very low density lipoproteins."
Shulman R.S., Herbert P.N., Wehrly K., Fredrickson D.S.
J. Biol. Chem. 250:182-190(1975) [PubMed: 166984] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-83.
[11]"The primary structure of apolopoprotein-serine."
Jackson R.L., Sparrow J.T., Baker H.N., Morrisett J.D., Taunton O.D., Gotto A.M. Jr.
J. Biol. Chem. 249:5308-5313(1974) [PubMed: 4369340] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-83.
[12]"Exact localization of the familial dysbetalipoproteinemia associated HpaI restriction site in the promoter region of the APOC1 gene."
Smit M.V.D., Kooij-Meijs E., Woudt L.P., Havekes L.M., Frants R.R.
Biochem. Biophys. Res. Commun. 152:1282-1288(1988) [PubMed: 2897845] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
[13]"Apolipoprotein C-I binds free fatty acids and reduces their intracellular esterification."
Westerterp M., Berbee J.F., Delsing D.J., Jong M.C., Gijbels M.J., Dahlmans V.E., Offerman E.H., Romijn J.A., Havekes L.M., Rensen P.C.
J. Lipid Res. 48:1353-1361(2007) [PubMed: 17339654] [Abstract]
Cited for: FUNCTION.
[14]"Conformation of two peptides corresponding to human apolipoprotein C-I residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy."
Rozek A., Buchko G.W., Cushley R.J.
Biochemistry 34:7401-7408(1995) [PubMed: 7779782] [Abstract]
Cited for: STRUCTURE BY NMR OF 33-50 AND 61-79.
[15]"Conformational studies of the N-terminal lipid-associating domain of human apolipoprotein C-I by CD and 1H NMR spectroscopy."
Rozek A., Buchko G.W., Kanda P., Cushley R.J.
Protein Sci. 6:1858-1868(1997) [PubMed: 9300485] [Abstract]
Cited for: STRUCTURE BY NMR OF 27-64.
[16]"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis."
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.
Nat. Genet. 22:239-247(1999) [PubMed: 10391210] [Abstract]
Cited for: VARIANT MET-16.
[17]"A functional polymorphism of apolipoprotein C1 detected by mass spectrometry."
Wroblewski M.S., Wilson-Grady J.T., Martinez M.B., Kasthuri R.S., McMillan K.R., Flood-Urdangarin C., Nelsestuen G.L.
FEBS J. 273:4707-4715(2006) [PubMed: 16981907] [Abstract]
Cited for: VARIANT SER-71, CHARACTERIZATION OF VARIANT SER-71.
+Additional computationally mapped references.

Web resources

Wikipedia

Apolipoprotein C1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00570 mRNA. Translation: CAA25235.1.
M20843 Genomic DNA. Translation: AAA51763.1.
AF050154 Genomic DNA. Translation: AAD02506.1.
AY422954 Genomic DNA. Translation: AAQ91813.1.
BT007142 mRNA. Translation: AAP35806.1.
CR456907 mRNA. Translation: CAG33188.1.
AM392727 mRNA. Translation: CAL37605.1.
BC009698 mRNA. Translation: AAH09698.1.
BC055093 mRNA. Translation: AAH55093.1.
M20902 Genomic DNA. Translation: AAA88018.1.
M27359 mRNA. Translation: AAA51762.1.
IPIIPI00021855.
PIRLPHUC1. A28057.
RefSeqNP_001636.1. NM_001645.3.
UniGeneHs.110675.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALENMR-A33-50[»]
1ALFNMR-A61-79[»]
1IOJNMR-A27-83[»]
1OPPNMR-A27-64[»]
ProteinModelPortalP02654.
SMRP02654. Positions 27-83.
ModBaseSearch...

Protein-protein interaction databases

IntActP02654. 4 interactions.
STRINGP02654.

Polymorphism databases

DMDM114016.

Proteomic databases

PeptideAtlasP02654.
PRIDEP02654.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252491; ENSP00000252491; ENSG00000130208.
GeneID341.
KEGGhsa:341.
UCSCuc002pac.1. human.

Organism-specific databases

CTD341.
GeneCardsGC19P045417.
H-InvDBHIX0015216.
HIX0137948.
HGNCHGNC:607. APOC1.
MIM107710. gene.
neXtProtNX_P02654.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG21768.
GeneTreeENSGT00390000011584.
HOGENOMHBG126847.
HOVERGENHBG050547.
InParanoidP02654.
OMANTLEDKA.
OrthoDBEOG4K0QQ3.
PhylomeDBP02654.

Gene expression databases

ArrayExpressP02654.
BgeeP02654.
CleanExHS_APOC1.
GenevestigatorP02654.

Family and domain databases

InterProIPR006781. ApoC-I.
[Graphical view]
Gene3DG3DSA:4.10.260.30. ApoC-I. 1 hit.
PANTHERPTHR16565. ApoC-I. 1 hit.
PfamPF04691. ApoC-I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio1409.
SOURCESearch...

Entry information

Entry nameAPOC1_HUMAN
AccessionPrimary (citable) accession number: P02654
Secondary accession number(s): Q6IB97
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 23, 1986
Last modified: January 25, 2012
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families