APOA2_HUMAN
ID APOA2_HUMAN Reviewed; 100 AA.
AC P02652; B2R524;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Apolipoprotein A-II;
DE Short=Apo-AII;
DE Short=ApoA-II;
DE AltName: Full=Apolipoprotein A2;
DE Contains:
DE RecName: Full=Proapolipoprotein A-II;
DE Short=ProapoA-II;
DE Contains:
DE RecName: Full=Truncated apolipoprotein A-II;
DE AltName: Full=Apolipoprotein A-II(1-76);
DE Flags: Precursor;
GN Name=APOA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6428397; DOI=10.1016/s0006-291x(84)80168-0;
RA Knott T.J., Priestley L.M., Urdea M., Scott J.;
RT "Isolation and characterisation of a cDNA encoding the precursor for human
RT apolipoprotein AII.";
RL Biochem. Biophys. Res. Commun. 120:734-740(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6089788; DOI=10.1016/0006-291x(84)90371-1;
RA Moore M.N., Kao F.-T., Tsao Y.-K., Chan L.;
RT "Human apolipoprotein A-II: nucleotide sequence of a cloned cDNA, and
RT localization of its structural gene on human chromosome 1.";
RL Biochem. Biophys. Res. Commun. 123:1-7(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6328445; DOI=10.1093/nar/12.9.3917;
RA Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C.,
RA Baralle F.E.;
RT "Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA
RT abundance.";
RL Nucleic Acids Res. 12:3917-3932(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2989800; DOI=10.1093/nar/13.12.4597;
RA Lackner K.J., Law S.W., Brewer H.B. Jr.;
RT "The human apolipoprotein A-II gene: complete nucleic acid sequence and
RT genomic organization.";
RL Nucleic Acids Res. 13:4597-4608(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2995928; DOI=10.1093/nar/13.17.6387;
RA Knott T.J., Wallis S.C., Robertson M.E., Priestley L.M., Urdea M.,
RA Rall L.B., Scott J.;
RT "The human apolipoprotein AII gene: structural organization and sites of
RT expression.";
RL Nucleic Acids Res. 13:6387-6398(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3088392; DOI=10.1016/0076-6879(86)28103-3;
RA Chan L., Moore M.N., Tsao Y.-K.;
RT "Molecular cloning and sequence analysis of human apolipoprotein A-II
RT cDNA.";
RL Methods Enzymol. 128:745-752(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12136239; DOI=10.1007/s00439-002-0763-x;
RA Fullerton S.M., Clark A.G., Weiss K.M., Taylor S.L., Stengard J.H.,
RA Salomaa V., Boerwinkle E., Nickerson D.A.;
RT "Sequence polymorphism at the human apolipoprotein AII gene (APOA2):
RT unexpected deficit of variation in an African-American sample.";
RL Hum. Genet. 111:75-87(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP PROTEIN SEQUENCE OF 24-100, AND PYROGLUTAMATE FORMATION AT GLN-24.
RX PubMed=4344225; DOI=10.1016/s0021-9258(19)44556-0;
RA Lux S.E., John K.M., Ronan R., Brewer H.B. Jr.;
RT "Isolation and characterization of the tryptic and cyanogen bromide
RT peptides of apoLp-Gln-II (apoA-II), plasma high density apolipoprotein.";
RL J. Biol. Chem. 247:7519-7527(1972).
RN [13]
RP PROTEIN SEQUENCE OF 25-37, MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR
RP LOCATION, AND PYROGLUTAMATE FORMATION AT GLN-24.
RX PubMed=24116940; DOI=10.1089/adt.2013.511;
RA Su M., Qi Y., Wang M., Chang W., Peng S., Xu T., Wang D.;
RT "Expression and purification of recombinant human apolipoprotein A-II in
RT Pichia pastoris.";
RL Assay Drug Dev. Technol. 11:501-507(2013).
RN [14]
RP PARTIAL PROTEIN SEQUENCE OF 1-29.
RX PubMed=6407957; DOI=10.1515/bchm2.1983.364.1.227;
RA Stoffel W., Krueger E., Deutzmann R.;
RT "Cell-free translation of human liver apolipoprotein AI and AII mRNA.
RT Processing of primary translation products.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:227-237(1983).
RN [15]
RP POLYMORPHISM.
RX PubMed=2107739;
RA Deeb S.S., Takata K., Peng R.L., Kajiyama G., Albers J.J.;
RT "A splice-junction mutation responsible for familial apolipoprotein A-II
RT deficiency.";
RL Am. J. Hum. Genet. 46:822-827(1990).
RN [16]
RP INTERCHAIN DISULFIDE BOND WITH APOD, AND INTERACTION WITH APOD.
RC TISSUE=Plasma;
RX PubMed=7918467; DOI=10.1021/bi00207a011;
RA Yang C.-Y., Gu Z.-W., Blanco-Vaca F., Gaskell S.J., Yang M., Massey J.B.,
RA Gotto A.M. Jr., Pownall H.J.;
RT "Structure of human apolipoprotein D: locations of the intermolecular and
RT intramolecular disulfide links.";
RL Biochemistry 33:12451-12455(1994).
RN [17]
RP INTERACTION WITH HEPATITIS C VIRUS/HCV CORE PROTEIN (MICROBIAL INFECTION).
RX PubMed=10498661; DOI=10.1002/hep.510300429;
RA Sabile A., Perlemuter G., Bono F., Kohara K., Demaugre F., Kohara M.,
RA Matsuura Y., Miyamura T., Brechot C., Barba G.;
RT "Hepatitis C virus core protein binds to apolipoprotein AII and its
RT secretion is modulated by fibrates.";
RL Hepatology 30:1064-1076(1999).
RN [18]
RP RETRACTED PAPER.
RX PubMed=12269810; DOI=10.1021/bi026069w;
RA Kumar M.S., Carson M., Hussain M.M., Murthy H.M.;
RT "Structures of apolipoprotein A-II and a lipid-surrogate complex provide
RT insights into apolipoprotein-lipid interactions.";
RL Biochemistry 41:11681-11691(2002).
RN [19]
RP RETRACTION NOTICE OF PUBMED:12269810.
RX PubMed=30278611; DOI=10.1021/acs.biochem.8b00956;
RA Kumar M.S., Carson M., Hussain M.M., Murthy H.M.K.;
RL Biochemistry 57:6044-6044(2018).
RN [20]
RP INTERACTION WITH NAXE.
RX PubMed=11991719; DOI=10.1006/geno.2002.6761;
RA Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A.,
RA Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G., Schmitz G.;
RT "Cloning and characterization of a novel apolipoprotein A-I-binding
RT protein, AI-BP, secreted by cells of the kidney proximal tubules in
RT response to HDL or ApoA-I.";
RL Genomics 79:693-702(2002).
RN [21]
RP MASS SPECTROMETRY, AND OXIDATION AT MET-49.
RX PubMed=12576517; DOI=10.1194/jlr.m200256-jlr200;
RA Pankhurst G., Wang X.L., Wilcken D.E., Baernthaler G., Panzenboeck U.,
RA Raftery M., Stocker R.;
RT "Characterization of specifically oxidized apolipoproteins in mildly
RT oxidized high density lipoprotein.";
RL J. Lipid Res. 44:349-355(2003).
RN [22]
RP MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=12562854; DOI=10.1194/jlr.d200034-jlr200;
RA Niederkofler E.E., Tubbs K.A., Kiernan U.A., Nedelkov D., Nelson R.W.;
RT "Novel mass spectrometric immunoassays for the rapid structural
RT characterization of plasma apolipoproteins.";
RL J. Lipid Res. 44:630-639(2003).
RN [23]
RP INTERACTION WITH NDRG1.
RX PubMed=15922294; DOI=10.1016/j.bbrc.2005.05.050;
RA Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C., Watts G.F.,
RA Kremensky I., Kalaydjieva L.;
RT "NDRG1 interacts with APO A-I and A-II and is a functional candidate for
RT the HDL-C QTL on 8q24.";
RL Biochem. Biophys. Res. Commun. 332:982-992(2005).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Serum;
RX PubMed=19824718; DOI=10.1021/pr900603n;
RA Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A., Liotta L.A.,
RA Petricoin E.F. III;
RT "An initial characterization of the serum phosphoproteome.";
RL J. Proteome Res. 8:5523-5531(2009).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP PHOSPHORYLATION AT SER-54 AND SER-68.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
CC -!- FUNCTION: May stabilize HDL (high density lipoprotein) structure by its
CC association with lipids, and affect the HDL metabolism.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked. Also forms a disulfide-
CC linked heterodimer with APOD (PubMed:7918467). Interacts with NAXE and
CC NDRG1. {ECO:0000269|PubMed:11991719, ECO:0000269|PubMed:12562854,
CC ECO:0000269|PubMed:15922294, ECO:0000269|PubMed:24116940,
CC ECO:0000269|PubMed:7918467}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV core protein.
CC {ECO:0000269|PubMed:10498661}.
CC -!- INTERACTION:
CC P02652; Q13520: AQP6; NbExp=3; IntAct=EBI-1171525, EBI-13059134;
CC P02652; Q8NEC5: CATSPER1; NbExp=7; IntAct=EBI-1171525, EBI-744545;
CC P02652; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-1171525, EBI-752069;
CC P02652; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-1171525, EBI-2680384;
CC P02652; O00258: GET1; NbExp=3; IntAct=EBI-1171525, EBI-18908258;
CC P02652; P48165: GJA8; NbExp=3; IntAct=EBI-1171525, EBI-17458373;
CC P02652; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-1171525, EBI-18053395;
CC P02652; P43628: KIR2DL3; NbExp=3; IntAct=EBI-1171525, EBI-8632435;
CC P02652; P15941-11: MUC1; NbExp=3; IntAct=EBI-1171525, EBI-17263240;
CC P02652; Q96RD7: PANX1; NbExp=3; IntAct=EBI-1171525, EBI-7037612;
CC P02652; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-1171525, EBI-716063;
CC P02652; P30825: SLC7A1; NbExp=3; IntAct=EBI-1171525, EBI-4289564;
CC P02652; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-1171525, EBI-17280858;
CC P02652; P27105: STOM; NbExp=3; IntAct=EBI-1171525, EBI-1211440;
CC P02652; Q9NWC5: TMEM45A; NbExp=3; IntAct=EBI-1171525, EBI-10823938;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24116940}.
CC -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver and intestine.
CC -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC {ECO:0000269|PubMed:26091039}.
CC -!- PTM: Apolipoprotein A-II is O-glycosylated.
CC {ECO:0000269|PubMed:23234360}.
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=17252;
CC Method=Electrospray; Note=Homodimer, without methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:12576517};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=17269;
CC Method=Electrospray; Note=Homodimer, with 1 methionine sulfoxide,
CC oxidation at Met-49.; Evidence={ECO:0000269|PubMed:12576517};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=8701.2; Method=MALDI;
CC Note=Monomer.; Evidence={ECO:0000269|PubMed:12562854};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=8823.4; Method=MALDI;
CC Note=Cysteinylated ApoA-II monomer.;
CC Evidence={ECO:0000269|PubMed:12562854};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=17421.3; Method=MALDI;
CC Note=Homodimer.; Evidence={ECO:0000269|PubMed:12562854};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=17293.4; Method=MALDI;
CC Note=Heterodimer with truncated apolipoprotein A-II.;
CC Evidence={ECO:0000269|PubMed:12562854};
CC -!- MASS SPECTROMETRY: [Truncated apolipoprotein A-II]: Mass=8578.3;
CC Method=MALDI; Note=Monomer.; Evidence={ECO:0000269|PubMed:12562854};
CC -!- MASS SPECTROMETRY: [Truncated apolipoprotein A-II]: Mass=17166.2;
CC Method=MALDI; Note=Homodimer.; Evidence={ECO:0000269|PubMed:12562854};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=17380; Method=MALDI;
CC Note=Homodimer.; Evidence={ECO:0000269|PubMed:24116940};
CC -!- POLYMORPHISM: A homozygous transition at position 1 of intron 3 of
CC APOA2 results in deficiency of apolipoprotein A-II, without significant
CC influence either on lipid and lipoprotein profiles or on the occurrence
CC of coronary artery disease [MIM:107670]. {ECO:0000269|PubMed:2107739}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A2 family. {ECO:0000305}.
CC -!- CAUTION: A paper describing the crystal structure of this protein has
CC been retracted due to evidence of fabricated data (see also US Office
CC of Research Integrity Notice 2018-07782). {ECO:0000305|PubMed:12269810,
CC ECO:0000305|PubMed:30278611}.
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DR EMBL; X04898; CAA28583.1; -; Genomic_DNA.
DR EMBL; X00955; CAA25467.1; -; mRNA.
DR EMBL; X02905; CAA26665.1; -; Genomic_DNA.
DR EMBL; X02619; CAA26474.1; -; Genomic_DNA.
DR EMBL; M29882; AAA51701.1; -; mRNA.
DR EMBL; AY100524; AAM49807.1; -; Genomic_DNA.
DR EMBL; AK312034; BAG34971.1; -; mRNA.
DR EMBL; BT006786; AAP35432.1; -; mRNA.
DR EMBL; AL590714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005282; AAH05282.1; -; mRNA.
DR CCDS; CCDS1226.1; -.
DR PIR; A93586; LPHUA2.
DR RefSeq; NP_001634.1; NM_001643.1.
DR AlphaFoldDB; P02652; -.
DR SMR; P02652; -.
DR BioGRID; 106833; 97.
DR IntAct; P02652; 27.
DR MINT; P02652; -.
DR STRING; 9606.ENSP00000356969; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB11886; Infigratinib.
DR DrugBank; DB00877; Sirolimus.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR CarbonylDB; P02652; -.
DR GlyGen; P02652; 3 sites, 3 O-linked glycans (3 sites).
DR iPTMnet; P02652; -.
DR PhosphoSitePlus; P02652; -.
DR BioMuta; APOA2; -.
DR DMDM; 114000; -.
DR SWISS-2DPAGE; P02652; -.
DR CPTAC; non-CPTAC-1073; -.
DR CPTAC; non-CPTAC-1074; -.
DR jPOST; P02652; -.
DR MassIVE; P02652; -.
DR MaxQB; P02652; -.
DR PaxDb; P02652; -.
DR PeptideAtlas; P02652; -.
DR PRIDE; P02652; -.
DR ProteomicsDB; 51538; -.
DR TopDownProteomics; P02652; -.
DR Antibodypedia; 20506; 512 antibodies from 39 providers.
DR DNASU; 336; -.
DR Ensembl; ENST00000367990.7; ENSP00000356969.3; ENSG00000158874.11.
DR GeneID; 336; -.
DR KEGG; hsa:336; -.
DR MANE-Select; ENST00000367990.7; ENSP00000356969.3; NM_001643.2; NP_001634.1.
DR UCSC; uc001fzc.2; human.
DR CTD; 336; -.
DR DisGeNET; 336; -.
DR GeneCards; APOA2; -.
DR HGNC; HGNC:601; APOA2.
DR HPA; ENSG00000158874; Tissue enriched (liver).
DR MalaCards; APOA2; -.
DR MIM; 107670; gene+phenotype.
DR neXtProt; NX_P02652; -.
DR OpenTargets; ENSG00000158874; -.
DR Orphanet; 238269; AApoAII amyloidosis.
DR PharmGKB; PA24886; -.
DR VEuPathDB; HostDB:ENSG00000158874; -.
DR eggNOG; ENOG502SVYZ; Eukaryota.
DR GeneTree; ENSGT00390000003306; -.
DR InParanoid; P02652; -.
DR OMA; LTICSFE; -.
DR OrthoDB; 1612564at2759; -.
DR PhylomeDB; P02652; -.
DR TreeFam; TF338165; -.
DR PathwayCommons; P02652; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-8963888; Chylomicron assembly.
DR Reactome; R-HSA-8963901; Chylomicron remodeling.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; P02652; -.
DR BioGRID-ORCS; 336; 13 hits in 1066 CRISPR screens.
DR ChiTaRS; APOA2; human.
DR EvolutionaryTrace; P02652; -.
DR GeneWiki; APOA2; -.
DR GenomeRNAi; 336; -.
DR Pharos; P02652; Tbio.
DR PRO; PR:P02652; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P02652; protein.
DR Bgee; ENSG00000158874; Expressed in right lobe of liver and 98 other tissues.
DR ExpressionAtlas; P02652; baseline and differential.
DR Genevisible; P02652; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; TAS:Reactome.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0034190; F:apolipoprotein receptor binding; IPI:BHF-UCL.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IBA:GO_Central.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IPI:BHF-UCL.
DR GO; GO:0055102; F:lipase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
DR GO; GO:0005319; F:lipid transporter activity; IDA:BHF-UCL.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IDA:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL.
DR GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR GO; GO:0046340; P:diacylglycerol catabolic process; IDA:BHF-UCL.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IDA:BHF-UCL.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IDA:BHF-UCL.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR GO; GO:0060621; P:negative regulation of cholesterol import; IDA:BHF-UCL.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0060695; P:negative regulation of cholesterol transporter activity; IDA:BHF-UCL.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IDA:BHF-UCL.
DR GO; GO:0060192; P:negative regulation of lipase activity; IDA:BHF-UCL.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR GO; GO:0018206; P:peptidyl-methionine modification; IDA:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IDA:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
DR GO; GO:0018158; P:protein oxidation; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IDA:BHF-UCL.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IDA:BHF-UCL.
DR GO; GO:0006641; P:triglyceride metabolic process; TAS:BHF-UCL.
DR GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; IDA:BHF-UCL.
DR InterPro; IPR006801; ApoA-II.
DR InterPro; IPR036172; ApoA-II_sf.
DR PANTHER; PTHR11027; PTHR11027; 1.
DR Pfam; PF04711; ApoA-II; 1.
DR SUPFAM; SSF82936; SSF82936; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; HDL; Host-virus interaction; Lipid transport;
KW Oxidation; Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:6328445"
FT CHAIN 19..100
FT /note="Proapolipoprotein A-II"
FT /id="PRO_0000425351"
FT CHAIN 24..100
FT /note="Apolipoprotein A-II"
FT /evidence="ECO:0000269|PubMed:4344225"
FT /id="PRO_0000002003"
FT CHAIN 24..99
FT /note="Truncated apolipoprotein A-II"
FT /evidence="ECO:0000305|PubMed:12562854"
FT /id="PRO_0000002004"
FT REGION 32..43
FT /note="O-glycosylated at one site"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:24116940,
FT ECO:0000269|PubMed:4344225"
FT MOD_RES 49
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:12576517"
FT MOD_RES 54
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 68
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:19824718"
FT DISULFID 29
FT /note="Interchain (with C-136 in APOD); in heterodimeric
FT form"
FT /evidence="ECO:0000305|PubMed:7918467"
FT CONFLICT 96
FT /note="Q -> H (in Ref. 1; CAA28583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 100 AA; 11175 MW; 1247868A25EC3AF2 CRC64;
MKLLAATVLL LTICSLEGAL VRRQAKEPCV ESLVSQYFQT VTDYGKDLME KVKSPELQAE
AKSYFEKSKE QLTPLIKKAG TELVNFLSYF VELGTQPATQ
