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Reviewed, UniProtKB/Swiss-Prot P02652 (APOA2_HUMAN)

Last modified November 24, 2009. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Apolipoprotein A-II
      Short name=Apo-AII
      Short name=ApoA-II
Cleaved into the following chain:
    1- Recommended name:
            Apolipoprotein A-II(1-76)
Gene names
Name: APOA2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.

Subunit structure

Homodimer; disulfide-linked. Also forms a disulfide-linked heterodimer with APOD. Interacts with HCV core protein. Interacts with APOA1BP. Ref.14 Ref.15

Subcellular location

Secreted.

Tissue specificity

Plasma; synthesized in the liver and intestine.

Sequence similarities

Belongs to the apolipoprotein A2 family.

Mass spectrometry

Molecular mass is 8701.2 Da from positions 24 - 100. Determined by MALDI. Ref.16

Molecular mass is 8823.4 Da from positions 24 - 100. Determined by MALDI. Cysteinylated ApoA-II. Ref.16

Molecular mass is 17421.3 Da from positions 24 - 100. Determined by MALDI. Homodimer. Ref.16

Molecular mass is 17293.4 Da from positions 24 - 100. Determined by MALDI. Heterodimer with apolipoprotein A-II(1-76). Ref.16

Molecular mass is 8578.3 Da from positions 24 - 99. Determined by MALDI. Ref.16

Molecular mass is 17166.2 Da from positions 24 - 99. Determined by MALDI. Homodimer. Ref.16

Ontologies

Keywords
   Biological processHost-virus interaction
Lipid transport
Transport
   Cellular componentHDL
Secreted
   DomainSignal
   PTMCleavage on pair of basic residues
Disulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcholesterol efflux

Inferred from direct assay. Source: UniProtKB

cholesterol homeostasis

Inferred from direct assay. Source: UniProtKB

diacylglycerol catabolic process

Inferred from direct assay. Source: UniProtKB

high-density lipoprotein particle assembly

Inferred from direct assay. Source: UniProtKB

high-density lipoprotein particle clearance

Inferred from direct assay. Source: UniProtKB

high-density lipoprotein particle remodeling

Inferred from direct assay. Source: UniProtKB

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

low-density lipoprotein particle remodeling

Inferred from direct assay. Source: UniProtKB

negative regulation of cholesterol import

Inferred from direct assay. Source: UniProtKB

negative regulation of cholesterol transporter activity

Inferred from direct assay. Source: UniProtKB

negative regulation of cytokine secretion during immune response

Inferred from direct assay. Source: UniProtKB

negative regulation of lipase activity

Inferred from direct assay. Source: UniProtKB

negative regulation of lipid catabolic process

Inferred from direct assay. Source: UniProtKB

negative regulation of very-low-density lipoprotein particle remodeling

Inferred from direct assay. Source: UniProtKB

phosphatidylcholine biosynthetic process

Inferred from direct assay. Source: UniProtKB

phospholipid catabolic process

Inferred from direct assay. Source: UniProtKB

phospholipid efflux

Inferred from direct assay. Source: UniProtKB

positive regulation of cholesterol esterification

Inferred from direct assay. Source: UniProtKB

positive regulation of interleukin-8 biosynthetic process

Inferred from direct assay. Source: UniProtKB

positive regulation of lipid catabolic process

Inferred from direct assay. Source: UniProtKB

protein folding

Inferred from direct assay. Source: UniProtKB

regulation of protein stability

Inferred from direct assay. Source: UniProtKB

response to glucose stimulus

Inferred from direct assay. Source: UniProtKB

reverse cholesterol transport

Inferred from direct assay. Source: UniProtKB

triglyceride metabolic process

Traceable author statement. Source: UniProtKB

triglyceride-rich lipoprotein particle remodeling

Inferred from direct assay. Source: UniProtKB

   Cellular componentchylomicron

Inferred from direct assay. Source: UniProtKB

endoplasmic reticulum lumen

Inferred from Experiment. Source: Reactome

spherical high-density lipoprotein particle

Inferred from direct assay. Source: UniProtKB

very-low-density lipoprotein particle

Inferred from direct assay. Source: UniProtKB

   Molecular functionapolipoprotein receptor binding

Inferred from physical interaction. Source: UniProtKB

cholesterol binding

Inferred from direct assay. Source: UniProtKB

high-density lipoprotein receptor binding

Inferred from physical interaction. Source: UniProtKB

lipase inhibitor activity

Inferred from direct assay. Source: UniProtKB

phosphatidylcholine binding

Inferred from direct assay. Source: UniProtKB

phosphatidylcholine-sterol O-acyltransferase activator activity

Inferred from direct assay. Source: UniProtKB

protein heterodimerization activity Ref.14

Inferred from physical interaction. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.3
Propeptide19 – 235
PRO_0000002002
Chain24 – 10077Apolipoprotein A-II
PRO_0000002003
Chain24 – 9976Apolipoprotein A-II(1-76)
PRO_0000002004

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid Ref.12
Disulfide bond29Interchain (with C-136 in APOD); in heterodimeric form Ref.14
Disulfide bond29Interchain; in homodimeric form Ref.14 Ref.5

Experimental info

Sequence conflict961Q → H in CAA28583. Ref.1

Secondary structure

............. 100
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02652-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 1247868A25EC3AF2

FASTA10011,175
        10         20         30         40         50         60 
MKLLAATVLL LTICSLEGAL VRRQAKEPCV ESLVSQYFQT VTDYGKDLME KVKSPELQAE 

        70         80         90        100 
AKSYFEKSKE QLTPLIKKAG TELVNFLSYF VELGTQPATQ 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterisation of a cDNA encoding the precursor for human apolipoprotein AII."
Knott T.J., Priestley L.M., Urdea M., Scott J.
Biochem. Biophys. Res. Commun. 120:734-740(1984) [PubMed: 6428397] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Human apolipoprotein A-II: nucleotide sequence of a cloned cDNA, and localization of its structural gene on human chromosome 1."
Moore M.N., Kao F.-T., Tsao Y.-K., Chan L.
Biochem. Biophys. Res. Commun. 123:1-7(1984) [PubMed: 6089788] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [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 A-II gene: complete nucleic acid sequence and genomic organization."
Lackner K.J., Law S.W., Brewer H.B. Jr.
Nucleic Acids Res. 13:4597-4608(1985) [PubMed: 2989800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The human apolipoprotein AII gene: structural organization and sites of expression."
Knott T.J., Wallis S.C., Robertson M.E., Priestley L.M., Urdea M., Rall L.B., Scott J.
Nucleic Acids Res. 13:6387-6398(1985) [PubMed: 2995928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Molecular cloning and sequence analysis of human apolipoprotein A-II cDNA."
Chan L., Moore M.N., Tsao Y.-K.
Methods Enzymol. 128:745-752(1986) [PubMed: 3088392] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"Sequence polymorphism at the human apolipoprotein AII gene (APOA2): unexpected deficit of variation in an African-American sample."
Fullerton S.M., Clark A.G., Weiss K.M., Taylor S.L., Stengard J.H., Salomaa V., Boerwinkle E., Nickerson D.A.
Hum. Genet. 111:75-87(2002) [PubMed: 12136239] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[9]"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].
[10]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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.
[12]"Isolation and characterization of the tryptic and cyanogen bromide peptides of apoLp-Gln-II (apoA-II), plasma high density apolipoprotein."
Lux S.E., John K.M., Ronan R., Brewer H.B. Jr.
J. Biol. Chem. 247:7519-7527(1972) [PubMed: 4344225] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-100.
[13]"Cell-free translation of human liver apolipoprotein AI and AII mRNA. Processing of primary translation products."
Stoffel W., Krueger E., Deutzmann R.
Hoppe-Seyler's Z. Physiol. Chem. 364:227-237(1983) [PubMed: 6407957] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE OF 1-29.
[14]"Structure of human apolipoprotein D: locations of the intermolecular and intramolecular disulfide links."
Yang C.-Y., Gu Z.-W., Blanco-Vaca F., Gaskell S.J., Yang M., Massey J.B., Gotto A.M. Jr., Pownall H.J.
Biochemistry 33:12451-12455(1994) [PubMed: 7918467] [Abstract]
Cited for: INTERCHAIN DISULFIDE BOND WITH APOD.
Tissue: Plasma.
[15]"Cloning and characterization of a novel apolipoprotein A-I-binding protein, AI-BP, secreted by cells of the kidney proximal tubules in response to HDL or ApoA-I."
Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A., Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G., Schmitz G.
Genomics 79:693-702(2002) [PubMed: 11991719] [Abstract]
Cited for: INTERACTION WITH APOA1BP.
[16]"Novel mass spectrometric immunoassays for the rapid structural characterization of plasma apolipoproteins."
Niederkofler E.E., Tubbs K.A., Kiernan U.A., Nedelkov D., Nelson R.W.
J. Lipid Res. 44:630-639(2003) [PubMed: 12562854] [Abstract]
Cited for: MASS SPECTROMETRY.
[17]"Structures of apolipoprotein A-II and a lipid-surrogate complex provide insights into apolipoprotein-lipid interactions."
Kumar M.S., Carson M., Hussain M.M., Murthy H.M.
Biochemistry 41:11681-11691(2002) [PubMed: 12269810] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-100.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

X04898 Genomic DNA. Translation: CAA28583.1.
X00955 mRNA. Translation: CAA25467.1.
X02905 Genomic DNA. Translation: CAA26665.1.
X02619 Genomic DNA. Translation: CAA26474.1.
M29882 mRNA. Translation: AAA51701.1.
AY100524 Genomic DNA. Translation: AAM49807.1.
AK312034 mRNA. Translation: BAG34971.1.
BT006786 mRNA. Translation: AAP35432.1.
AL590714 Genomic DNA. Translation: CAH72151.1.
BC005282 mRNA. Translation: AAH05282.1.
IPIIPI00021854.
PIRLPHUA2. A93586.
RefSeqNP_001634.1.
UniGeneHs.237658

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1L6LX-ray2.301/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/P/Q/S/T/U/V/W/X/Y/Z24-100[»]
2OU1X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L24-100[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP02652.

2-D gel databases

SWISS-2DPAGEP02652.
Siena-2DPAGEP02652.

Proteomic databases

PeptideAtlasP02652.
PRIDEP02652.

Genome annotation databases

EnsemblENST00000367990; ENSP00000356969; ENSG00000158874; Homo sapiens. [Genome view]
GeneID336.
KEGGhsa:336.
UCSCuc001fzc.1. human.

Organism-specific databases

CTD336.
GeneCardsGC01M159458.
HGNCHGNC:601. APOA2.
MIM107670. gene.
Orphanet85450. Amyloid nephropathy, familial.
PharmGKBPA24886.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP02652.
HOVERGENP02652.
OMAKAYFEKT
OrthoDBEOG9XWJHB

Enzyme and pathway databases

ReactomeREACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpressP02652.
BgeeP02652.
CleanExHS_APOA2.
GenevestigatorP02652.
GermOnlineENSG00000158874. Homo sapiens.

Family and domain databases

InterProIPR006801. ApoA-II.
[Graphical view]
PANTHERPTHR11027. ApoA-II. 1 hit.
PfamPF04711. ApoA-II. 1 hit.
[Graphical view]
ProDomPD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other Resources

NextBio1391.
PMAP-CutDBP02652.
SOURCESearch...

Entry information

Entry nameAPOA2_HUMAN
AccessionPrimary (citable) accession number: P02652
Secondary accession number(s): B2R524
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: November 24, 2009
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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 1

Human chromosome 1: entries, gene names and cross-references to MIM

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents