Reviewed, UniProtKB/Swiss-Prot P02655 (APOC2_HUMAN)

Names and origin

Protein names

Recommended name:
    Apolipoprotein C-II
      Short name=Apo-CII
      Short name=ApoC-II

Gene names

Name:	APOC2
Synonyms:	APC2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	101 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	Component of the very low density lipoprotein (VLDL) fraction in plasma, and is an activator of several triacylglycerol lipases. The association of APOC2 with plasma chylomicrons, VLDL, and HDL is reversible, a function of the secretion and catabolism of triglyceride-rich lipoproteins, and changes rapidly.
Subcellular location	Secreted.
Tissue specificity	Secreted in plasma.
Involvement in disease	Defects in APOC2 are the cause of hyperlipoproteinemia type 1B [MIM:207750]. It is an autosomal recessive trait characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis. Ref.20
Sequence similarities	Belongs to the apolipoprotein C2 family.

Ontologies

Keywords
Biological process	Lipid degradation Lipid transport Transport
Cellular component	Chylomicron Secreted VLDL
Coding sequence diversity	Polymorphism
Disease	Disease mutation Hyperlipidemia
Domain	Signal
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cholesterol efflux Inferred from direct assay. Source: UniProtKB cholesterol homeostasis Inferred by curator. Source: UniProtKB chylomicron remnant clearance Inferred from direct assay. Source: UniProtKB chylomicron remodeling Inferred by curator. Source: UniProtKB high-density lipoprotein particle clearance Inferred from mutant phenotype. Source: UniProtKB lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cholesterol transport Inferred from mutant phenotype. Source: UniProtKB negative regulation of lipid metabolic process Inferred from direct assay. Source: UniProtKB negative regulation of receptor-mediated endocytosis Inferred from direct assay. Source: UniProtKB negative regulation of very-low-density lipoprotein particle clearance Inferred from direct assay. Source: UniProtKB phospholipid efflux Inferred from direct assay. Source: UniProtKB positive regulation of fatty acid biosynthetic process Inferred from direct assay. Source: UniProtKB positive regulation of lipoprotein lipase activity Inferred from direct assay. Source: UniProtKB positive regulation of phospholipase activity Inferred from direct assay. Source: UniProtKB positive regulation of phospholipid catabolic process Inferred from direct assay. Source: UniProtKB positive regulation of triglyceride catabolic process Inferred from direct assay. Source: UniProtKB positive regulation of very-low-density lipoprotein particle remodeling Inferred by curator. Source: UniProtKB reverse cholesterol transport Inferred by curator. Source: UniProtKB triglyceride homeostasis Inferred from mutant phenotype. Source: UniProtKB very-low-density lipoprotein particle remodeling Traceable author statement. Source: UniProtKB
Cellular component	chylomicron Inferred from direct assay. Source: UniProtKB intermediate-density lipoprotein particle Inferred from direct assay. Source: UniProtKB low-density lipoprotein particle Inferred from direct assay. Source: UniProtKB spherical high-density lipoprotein particle Inferred from direct assay. Source: UniProtKB very-low-density lipoprotein particle Inferred from direct assay. Source: UniProtKB
Molecular function	lipase inhibitor activity Inferred from direct assay. Source: UniProtKB lipid binding Inferred from direct assay. Source: UniProtKB lipoprotein lipase activator activity Inferred from direct assay. Source: UniProtKB phospholipase activator activity Inferred from direct assay. Source: UniProtKB phospholipase binding Inferred from physical interaction. Source: UniProtKB protein heterodimerization activity Inferred from mutant phenotype. Source: UniProtKB protein homodimerization activity Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.11 Ref.12

Chain

23 – 101

79

Apolipoprotein C-II

PRO_0000002024

Regions

Region

43 – 51

9

Lipid binding

Region

55 – 78

24

Lipoprotein lipase cofactor

Natural variations

Natural variant

41

1

K → T

VAR_000639

Natural variant

48

1

W → R in hyperlipoproteinemia type 1B; variant Wakayama. Ref.20

VAR_000640

Natural variant

60

1

E → K in San Francisco; found in hyperlipidemic patients. dbSNP rs5122. Ref.17

VAR_000641

Natural variant

77

1

K → Q in Africa. dbSNP rs5126. Ref.16 Ref.21

VAR_000642

Experimental info

Sequence conflict

36

1

F → L Ref.7

Sequence conflict

36

1

F → L Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

101

Helix Strand Turn

Details...

Beta strand

28 – 31

4

Helix

37 – 57

21

Turn

58 – 61

4

Beta strand

62 – 64

3

Turn

75 – 77

3

Turn

79 – 81

3

Beta strand

86 – 88

3

Helix

92 – 94

3

Helix

97 – 99

3

Sequences

	Sequence		Length	Mass (Da)
	P02655-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 51CB86FEDB174D84	FASTA	101	11,284
	10 20 30 40 50 60 MGTRLLPALF LVLLVLGFEV QGTQQPQQDE MPSPTFLTQV KESLSSYWES AKTAAQNLYE 70 80 90 100 KTYLPAVDEK LRDLYSKSTA AMSTYTGIFT DQVLSVLKGE E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human preproapolipoprotein C-II gene. Complete nucleic acid sequence and genomic organization." Fojo S.S., Law S.W., Brewer H.B. Jr. FEBS Lett. 213:221-226(1987) [PubMed: 3030808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Human apolipoprotein C-II: complete nucleic acid sequence of preapolipoprotein C-II." Fojo S.S., Law S.W., Brewer H.B. Jr. Proc. Natl. Acad. Sci. U.S.A. 81:6354-6357(1984) [PubMed: 6593704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA abundance." Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C., Baralle F.E. Nucleic Acids Res. 12:3917-3932(1984) [PubMed: 6328445] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The human apolipoprotein C-II gene sequence contains a novel chromosome 19-specific minisatellite in its third intron." Das H.K., Jackson C.L., Miller D.A., Leff T., Breslow J.L. J. Biol. Chem. 262:4787-4793(1987) [PubMed: 3558370] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The structure of the human apolipoprotein C-II gene. Electron microscopic analysis of RNA:DNA hybrids, complete nucleotide sequence, and identification of 5' homologous sequences among apolipoprotein genes." Wei C.F., Tsao Y.K., Robberson D.L., Gotto A.M. Jr., Brown K., Chan L. J. Biol. Chem. 260:15211-15221(1985) [PubMed: 2415514] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[6]	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].
[7]	"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].
[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: Skeletal muscle.
[9]	"The isolation and characterization of cDNA clones for human apolipoprotein CII." Myklebost O., Williamson B., Markham A.F., Myklebost S.R., Rogers J., Woods D.E., Humphries S.E. J. Biol. Chem. 259:4401-4404(1984) [PubMed: 6546757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-101.
[10]	"Isolation of cDNA and genomic clones for apolipoprotein C-II." Jackson C.L., Bruns G.A.P., Breslow J.L. Methods Enzymol. 128:788-800(1986) [PubMed: 3014272] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 11-101.
[11]	"Amino acid sequence of human plasma apolipoprotein C-II from normal and hyperlipoproteinemic subjects." Hospattankar A.V., Fairwell T., Ronan R., Brewer H.B. Jr. J. Biol. Chem. 259:318-322(1984) [PubMed: 6706938] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-101.
[12]	"Primary structure of very low density apolipoprotein C-II of human plasma." Jackson R.L., Baker H.N., Gilliam E.B., Gotto A.M. Jr. Proc. Natl. Acad. Sci. U.S.A. 74:1942-1945(1977) [PubMed: 194244] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-101.
[13]	"Expression of the apolipoprotein C-II gene during myelomonocytic differentiation of human leukemic cells." Chun E.M., Park Y.J., Kang H.S., Cho H.M., Jun D.Y., Kim Y.H. J. Leukoc. Biol. 69:645-650(2001) [PubMed: 11310852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-101.
[14]	"Sequence specific 1H-NMR assignments and secondary structure of a carboxy-terminal functional fragment of apolipoprotein CII." Lycksell P.-O., Oehman A., Bengtsson-Olivecrona G., Johansson L.B.-A., Wijmenga S.S., Wernic D., Graeslund A. Eur. J. Biochem. 205:223-231(1992) [PubMed: 1555583] [Abstract] Cited for: STRUCTURE BY NMR OF 72-101.
[15]	"A refined three-dimensional solution structure of a carboxy terminal fragment of apolipoprotein CII." Oehman A., Lycksell P.-O., Graeslund A. Eur. Biophys. J. 22:351-357(1993) [PubMed: 8112221] [Abstract] Cited for: STRUCTURE BY NMR OF 72-101.
[16]	"A variant primary structure of apolipoprotein C-II in individuals of African descent." Menzel H.-J., Kane J.P., Malloy M.J., Havel R.J. J. Clin. Invest. 77:595-601(1986) [PubMed: 3944271] [Abstract] Cited for: VARIANT AFRICA GLN-77.
[17]	"Molecular cloning and characteristics of a new apolipoprotein C-II mutant identified in three unrelated individuals with hypercholesterolemia and hypertriglyceridemia." Pullinger C.R., Zysow B.R., Hennessy L.K., Frost P.H., Malloy M.J., Kanr J.P. Hum. Mol. Genet. 2:69-74(1993) [PubMed: 8490626] [Abstract] Cited for: VARIANT SAN FRANCISCO LYS-60.
[18]	"An apolipoprotein CII mutation, CII Lys-19-->Thr identified in patients with hyperlipidemia." Hegele R.A., Connelly P.W., Maguire G.F., Huff M.W., Leiter L., Wolfe B.M., Evans A.J., Little J.A. Dis. Markers 9:73-80(1991) [PubMed: 1782747] [Abstract] Cited for: VARIANT THR-41.
[19]	"The apolipoprotein C-II variant apoC-II Lys-19-->Thr is not associated with dyslipidemia in an affected kindred." Zysow B.R., Pullinger C.R., Hennessy L.K., Farese R.V. Jr., Ghassemzadeh M., Kane J.P. Clin. Genet. 45:292-297(1994) [PubMed: 7923858] [Abstract] Cited for: VARIANT THR-41.
[20]	"A missense mutation (Trp 26-->Arg) in exon 3 of the apolipoprotein CII gene in a patient with apolipoprotein CII deficiency (apo CII-Wakayama)." Inadera H., Hibino A., Kobayashi J., Kanzaki T., Shirai K., Yukawa S., Saito Y., Yoshida S. Biochem. Biophys. Res. Commun. 193:1174-1183(1993) [PubMed: 8323539] [Abstract] Cited for: VARIANT HYPERLIPOPROTEINEMIA TYPE 1B WAKAYAMA ARG-48.
[21]	"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 GLN-77.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

X05151 Genomic DNA. Translation: CAA28798.1.
X00568 mRNA. Translation: CAA25234.1.
J02698 Genomic DNA. Translation: AAA98743.1.
AY422955 Genomic DNA. Translation: AAQ91814.1.
BT006708 mRNA. Translation: AAP35354.1.
BC005348 mRNA. Translation: AAH05348.3.
M29844 mRNA. Translation: AAA51743.1.
M10612 Genomic DNA. Translation: AAB59380.1.
AF113884 mRNA. Translation: AAD28193.1.

IPI

IPI00021856.

PIR

LPHUC2. A24238.

RefSeq

NP_000474.2.

UniGene

Hs.75615

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BY6	NMR	-	A	66-101	[»]
1I5J	NMR	-	A	23-101	[»]
1O8T	NMR	-	A	23-101	[»]
1SOH	NMR	-	A	23-101	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P02655.

2-D gel databases

SWISS-2DPAGE

P02655.

DOSAC-COBS-2DPAGE

P02655.

Proteomic databases

PeptideAtlas

P02655.

PRIDE

P02655.

Genome annotation databases

Ensembl

ENST00000252490; ENSP00000252490; ENSG00000234906; Homo sapiens. [Genome view]
ENST00000419266; ENSP00000406381; ENSG00000234906; Homo sapiens. [Genome view]

GeneID

344.

KEGG

hsa:344.

UCSC

uc002pah.1. human.

Organism-specific databases

CTD

344.

GeneCards

GC19P050138.

HGNC

HGNC:609. APOC2.

MIM

207750. phenotype.
608083. gene.

Orphanet

411. Hyperlipoproteinemia type 1.
181425. Major hypertriglyceridemia.

PharmGKB

PA52.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P02655.

OMA

GFEVQGA

OrthoDB

EOG9KSS58

Enzyme and pathway databases

Reactome

REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P02655.

Bgee

P02655.

CleanEx

HS_APC2.
HS_APOC2.

Genevestigator

P02655.

GermOnline

ENSG00000130207. Homo sapiens.

Family and domain databases

InterPro

IPR008019. Apo-CII.
[Graphical view]

PANTHER

PTHR16566. Apo-CII. 1 hit.

Pfam

PF05355. Apo-CII. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

1419.

PMAP-CutDB

P02655.

SOURCE

Search...

Entry information

Entry name

APOC2_HUMAN

Accession

Primary (citable) accession number: P02655
Secondary accession number(s): Q9BS39, Q9UDE3, Q9UNK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 24, 2009
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.