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Angiopoietin-related protein 3 (Angiopoietin-5) (ANG-5) (Angiopoietin-like protein 3) [Cleaved into: ANGPTL3(17-221); ANGPTL3(17-224)]

 ANGL3_HUMAN             Reviewed;         460 AA.
Q9Y5C1; A0JLS0; B1ALJ0; B2RCW1;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
30-AUG-2017, entry version 156.
RecName: Full=Angiopoietin-related protein 3;
AltName: Full=Angiopoietin-5;
Short=ANG-5;
AltName: Full=Angiopoietin-like protein 3;
Contains:
RecName: Full=ANGPTL3(17-221);
Contains:
RecName: Full=ANGPTL3(17-224);
Flags: Precursor;
Name=ANGPTL3; Synonyms=ANGPT5; ORFNames=UNQ153/PRO179;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND GLYCOSYLATION AT
ASN-115.
TISSUE=Liver;
PubMed=10644446; DOI=10.1006/geno.1999.6041;
Conklin D., Gilbertson D., Taft D.W., Maurer M.F., Whitmore T.E.,
Smith D.L., Walker K.M., Chen L.H., Wattler S., Nehls M., Lewis K.B.;
"Identification of a mammalian angiopoietin-related protein expressed
specifically in liver.";
Genomics 62:477-482(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, and Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 17-31.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[9]
FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=11877390; DOI=10.1074/jbc.M109768200;
Camenisch G., Pisabarro M.T., Sherman D., Kowalski J., Nagel M.,
Hass P., Xie M.H., Gurney A., Bodary S., Liang X.H., Clark K.,
Beresini M., Ferrara N., Gerber H.P.;
"ANGPTL3 stimulates endothelial cell adhesion and migration via
integrin alpha vbeta 3 and induces blood vessel formation in vivo.";
J. Biol. Chem. 277:17281-17290(2002).
[10]
FUNCTION.
PubMed=12097324; DOI=10.1074/jbc.M203215200;
Shimizugawa T., Ono M., Shimamura M., Yoshida K., Ando Y., Koishi R.,
Ueda K., Inaba T., Minekura H., Kohama T., Furukawa H.;
"ANGPTL3 decreases very low density lipoprotein triglyceride clearance
by inhibition of lipoprotein lipase.";
J. Biol. Chem. 277:33742-33748(2002).
[11]
FUNCTION.
PubMed=11788823; DOI=10.1038/ng814;
Koishi R., Ando Y., Ono M., Shimamura M., Yasumo H., Fujiwara T.,
Horikoshi H., Furukawa H.;
"Angptl3 regulates lipid metabolism in mice.";
Nat. Genet. 30:151-157(2002).
[12]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12565906; DOI=10.1016/S0006-291X(02)03058-9;
Shimamura M., Matsuda M., Kobayashi S., Ando Y., Ono M., Koishi R.,
Furukawa H., Makishima M., Shimomura I.;
"Angiopoietin-like protein 3, a hepatic secretory factor, activates
lipolysis in adipocytes.";
Biochem. Biophys. Res. Commun. 301:604-609(2003).
[13]
PROTEOLYTIC CLEAVAGE, FUNCTION, AND MUTAGENESIS OF 62-HIS-LYS-63;
LYS-65; 204-ARG-ARG-205; ARG-221; ARG-224 AND ARG-235.
PubMed=12909640; DOI=10.1074/jbc.M302861200;
Ono M., Shimizugawa T., Shimamura M., Yoshida K., Noji-Sakikawa C.,
Ando Y., Koishi R., Furukawa H.;
"Protein region important for regulation of lipid metabolism in
angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in
vivo.";
J. Biol. Chem. 278:41804-41809(2003).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115; ASN-296 AND ASN-357.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[15]
FUNCTION.
PubMed=17110602; DOI=10.1161/01.ATV.0000252827.51626.89;
Shimamura M., Matsuda M., Yasumo H., Okazaki M., Fujimoto K., Kono K.,
Shimizugawa T., Ando Y., Koishi R., Kohama T., Sakai N., Kotani K.,
Komuro R., Ishida T., Hirata K., Yamashita S., Furukawa H.,
Shimomura I.;
"Angiopoietin-like protein3 regulates plasma HDL cholesterol through
suppression of endothelial lipase.";
Arterioscler. Thromb. Vasc. Biol. 27:366-372(2007).
[16]
POSSIBLE INVOLVEMENT IN ATHEROSCLEROSIS.
PubMed=17191020; DOI=10.1159/000098153;
Hatsuda S., Shoji T., Shinohara K., Kimoto E., Mori K., Fukumoto S.,
Koyama H., Emoto M., Nishizawa Y.;
"Association between plasma angiopoietin-like protein 3 and arterial
wall thickness in healthy subjects.";
J. Vasc. Res. 44:61-66(2007).
[17]
FUNCTION.
PubMed=18535744; DOI=10.1111/j.1745-7270.2008.00421.x;
Li Y., Sun L., Xu H., Fang Z., Yao W., Guo W., Rao J., Zha X.;
"Angiopoietin-like protein 3 modulates barrier properties of human
glomerular endothelial cells through a possible signaling pathway
involving phosphatidylinositol-3 kinase/protein kinase B and integrin
alphaVbeta3.";
Acta Biochim. Biophys. Sin. 40:459-465(2008).
[18]
FUNCTION.
PubMed=19028676; DOI=10.1074/jbc.M808477200;
Shan L., Yu X.C., Liu Z., Hu Y., Sturgis L.T., Miranda M.L., Liu Q.;
"The angiopoietin-like proteins ANGPTL3 and ANGPTL4 inhibit
lipoprotein lipase activity through distinct mechanisms.";
J. Biol. Chem. 284:1419-1424(2009).
[19]
FUNCTION.
PubMed=19318355; DOI=10.1074/jbc.M807899200;
Lee E.C., Desai U., Gololobov G., Hong S., Feng X., Yu X.C., Gay J.,
Wilganowski N., Gao C., Du L.L., Chen J., Hu Y., Zhao S.,
Kirkpatrick L., Schneider M., Zambrowicz B.P., Landes G., Powell D.R.,
Sonnenburg W.K.;
"Identification of a new functional domain in angiopoietin-like 3
(ANGPTL3) and angiopoietin-like 4 (ANGPTL4) involved in binding and
inhibition of lipoprotein lipase (LPL).";
J. Biol. Chem. 284:13735-13745(2009).
[20]
FUNCTION (ANGPTL3(17-221)).
PubMed=19542565; DOI=10.1194/jlr.M900145-JLR200;
Sonnenburg W.K., Yu D., Lee E.C., Xiong W., Gololobov G., Key B.,
Gay J., Wilganowski N., Hu Y., Zhao S., Schneider M., Ding Z.M.,
Zambrowicz B.P., Landes G., Powell D.R., Desai U.;
"GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by
angiopoietin-like 3 and angiopoietin-like 4.";
J. Lipid Res. 50:2421-2429(2009).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[22]
FUNCTION.
PubMed=20581395; DOI=10.1074/jbc.M110.144279;
Liu J., Afroza H., Rader D.J., Jin W.;
"Angiopoietin-like protein 3 inhibits lipoprotein lipase activity
through enhancing its cleavage by proprotein convertases.";
J. Biol. Chem. 285:27561-27570(2010).
[23]
GLYCOSYLATION AT THR-226.
PubMed=20837471; DOI=10.1074/jbc.M110.156950;
Schjoldager K.T., Vester-Christensen M.B., Bennett E.P., Levery S.B.,
Schwientek T., Yin W., Blixt O., Clausen H.;
"O-glycosylation modulates proprotein convertase activation of
angiopoietin-like protein 3: possible role of polypeptide GalNAc-
transferase-2 in regulation of concentrations of plasma lipids.";
J. Biol. Chem. 285:36293-36303(2010).
[24]
INVOLVEMENT IN FHBL2.
PubMed=20942659; DOI=10.1056/NEJMoa1002926;
Musunuru K., Pirruccello J.P., Do R., Peloso G.M., Guiducci C.,
Sougnez C., Garimella K.V., Fisher S., Abreu J., Barry A.J.,
Fennell T., Banks E., Ambrogio L., Cibulskis K., Kernytsky A.,
Gonzalez E., Rudzicz N., Engert J.C., DePristo M.A., Daly M.J.,
Cohen J.C., Hobbs H.H., Altshuler D., Schonfeld G., Gabriel S.B.,
Yue P., Kathiresan S.;
"Exome sequencing, ANGPTL3 mutations, and familial combined
hypolipidemia.";
N. Engl. J. Med. 363:2220-2227(2010).
[25]
GLYCOSYLATION.
PubMed=22566642; DOI=10.1073/pnas.1203563109;
Schjoldager K.T., Vakhrushev S.Y., Kong Y., Steentoft C.,
Nudelman A.S., Pedersen N.B., Wandall H.H., Mandel U., Bennett E.P.,
Levery S.B., Clausen H.;
"Probing isoform-specific functions of polypeptide GalNAc-transferases
using zinc finger nuclease glycoengineered SimpleCells.";
Proc. Natl. Acad. Sci. U.S.A. 109:9893-9898(2012).
[26]
INTERACTION WITH ANGPTL8.
PubMed=23150577; DOI=10.1073/pnas.1217552109;
Quagliarini F., Wang Y., Kozlitina J., Grishin N.V., Hyde R.,
Boerwinkle E., Valenzuela D.M., Murphy A.J., Cohen J.C., Hobbs H.H.;
"Atypical angiopoietin-like protein that regulates ANGPTL3.";
Proc. Natl. Acad. Sci. U.S.A. 109:19751-19756(2012).
[27]
FUNCTION.
PubMed=23661675; DOI=10.1161/ATVBAHA.113.301397;
Robciuc M.R., Maranghi M., Lahikainen A., Rader D., Bensadoun A.,
Oeoerni K., Ooerni K., Metso J., Minicocci I., Ciociola E., Ceci F.,
Montali A., Arca M., Ehnholm C., Jauhiainen M.;
"Angptl3 deficiency is associated with increased insulin sensitivity,
lipoprotein lipase activity, and decreased serum free fatty acids.";
Arterioscler. Thromb. Vasc. Biol. 33:1706-1713(2013).
[28]
FUNCTION.
PubMed=25495645; DOI=10.1042/BSR20140115;
Tikka A., Soronen J., Laurila P.P., Metso J., Ehnholm C.,
Jauhiainen M.;
"Silencing of ANGPTL 3 (angiopoietin-like protein 3) in human
hepatocytes results in decreased expression of gluconeogenic genes and
reduced triacylglycerol-rich VLDL secretion upon insulin
stimulation.";
Biosci. Rep. 34:E00160-E00160(2014).
[29]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=26204133; DOI=10.1210/jc.2015-1254;
Nidhina Haridas P.A., Soronen J., Saedevirta S., Mysore R.,
Quagliarini F., Pasternack A., Metso J., Perttilae J., Leivonen M.,
Smas C.M., Fischer-Posovszky P., Wabitsch M., Ehnholm C., Ritvos O.,
Jauhiainen M., Olkkonen V.M., Yki-Jaervinen H.;
"Regulation of Angiopoietin-Like Proteins (ANGPTLs) 3 and 8 by
Insulin.";
J. Clin. Endocrinol. Metab. 100:E1299-E1307(2015).
[30]
VARIANT PHE-127.
PubMed=22095935; DOI=10.1002/humu.21660;
Huijgen R., Sjouke B., Vis K., de Randamie J.S., Defesche J.C.,
Kastelein J.J., Hovingh G.K., Fouchier S.W.;
"Genetic variation in APOB, PCSK9, and ANGPTL3 in carriers of
pathogenic autosomal dominant hypercholesterolemic mutations with
unexpected low LDL-Cl Levels.";
Hum. Mutat. 33:448-455(2012).
[31]
VARIANTS THR-63; GLY-91; PHE-164; SER-173; THR-259; GLN-288; PRO-292;
LYS-375 AND CYS-417, AND CHARACTERIZATION OF VARIANTS THR-63; GLY-91;
PHE-164; SER-173; THR-259; ARG-GLN; PRO-292; LYS-375 AND CYS-417.
PubMed=19075393; DOI=10.1172/JCI37118;
Romeo S., Yin W., Kozlitina J., Pennacchio L.A., Boerwinkle E.,
Hobbs H.H., Cohen J.C.;
"Rare loss-of-function mutations in ANGPTL family members contribute
to plasma triglyceride levels in humans.";
J. Clin. Invest. 119:70-79(2009).
[32]
VARIANT SER-344, AND CHARACTERIZATION OF VARIANTS SER-173; SER-344 AND
LYS-375.
PubMed=25733326; DOI=10.1016/j.atherosclerosis.2015.02.031;
Wang X., Wang D., Shan Z.;
"Clinical and genetic analysis of a family diagnosed with familial
hypobetalipoproteinemia in which the proband was diagnosed with
diabetes mellitus.";
Atherosclerosis 239:552-556(2015).
[33]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND POSSIBLE INVOLVEMENT IN
NEPHROTIC SYNDROME.
PubMed=25710887; DOI=10.1038/pr.2015.38;
Liu J., Gao X., Zhai Y., Shen Q., Sun L., Feng C., Rao J., Liu H.,
Zha X., Guo M., Ma D., Zhang Z., Li R., Xu H.;
"A novel role of angiopoietin-like-3 associated with podocyte
injury.";
Pediatr. Res. 77:732-739(2015).
-!- FUNCTION: Acts in part as a hepatokine that is involved in
regulation of lipid and glucose metabolism (PubMed:11788823,
PubMed:12909640, PubMed:23661675, PubMed:25495645). Proposed to
play a role in the trafficking of energy substrates to either
storage or oxidative tissues in response to food intake (By
similarity). Has a stimulatory effect on plasma triglycerides
(TG), which is achieved by suppressing plasma TG clearance via
inhibition of LPL activity. The inhibition of LPL activity appears
to be an indirect mechanism involving recruitment of proprotein
convertases PCSK6 and FURIN to LPL leading to cleavage and
dissociation of LPL from the cell surface; the function does not
require ANGPTL3 proteolytic cleavage but seems to be mediated by
the N-terminal domain, and is not inhibited by GPIHBP1
(PubMed:12097324, PubMed:19318355, PubMed:20581395). Can inhibit
endothelial lipase, causing increased plasma levels of high
density lipoprotein (HDL) cholesterol and phospholipids
(PubMed:17110602, PubMed:19028676). Can bind to adipocytes to
activate lipolysis, releasing free fatty acids and glycerol
(PubMed:12565906). Suppresses LPL specifically in oxidative
tissues which is required to route very low density lipoprotein
(VLDL)-TG to white adipose tissue (WAT) for storage in response to
food; the function may involve cooperation with circulating,
liver-derived ANGPTL8 and ANGPTL4 expression in WAT (By
similarity). Contributes to lower plasma levels of low density
lipoprotein (LDL)-cholesterol by a mechanism that is independent
of the canonical pathway implicating APOE and LDLR. May stimulate
hypothalamic LPL activity (By similarity).
{ECO:0000250|UniProtKB:Q9R182, ECO:0000269|PubMed:11788823,
ECO:0000269|PubMed:12097324, ECO:0000269|PubMed:12565906,
ECO:0000269|PubMed:12909640, ECO:0000269|PubMed:17110602,
ECO:0000269|PubMed:19028676, ECO:0000269|PubMed:19318355,
ECO:0000269|PubMed:20581395, ECO:0000269|PubMed:23661675,
ECO:0000269|PubMed:25495645, ECO:0000305|PubMed:20581395}.
-!- FUNCTION: ANGPTL3(17-221): In vitro inhibits LPL activity; not
effective on GPIHBP1-stabilized LPL.
{ECO:0000269|PubMed:19542565}.
-!- FUNCTION: Involved in angiogenesis. Binds to endothelial cells via
integrin alpha-V/beta-3 (ITGAV:ITGB3), activates FAK, MAPK and Akt
signaling pathways and induces cell adhesion and cell migration
(PubMed:11877390). Secreted from podocytes, may modulate
properties of glomerular endothelial cells involving integrin
alpha-V/beta-3 and Akt signaling (PubMed:18535744). May increase
the motility of podocytes. May induce actin filament
rearrangements in podocytes implicating integrin alpha-V/beta-3
and Rac1 activation. Binds to hematopoietic stem cells (HSC) and
is involved in the regulation of HSC activity probably implicating
down-regulation of IKZF1/IKAROS (By similarity).
{ECO:0000250|UniProtKB:Q9R182, ECO:0000269|PubMed:11877390,
ECO:0000269|PubMed:18535744}.
-!- SUBUNIT: Interacts with ANGPTL8. Interacts with ITGB3 (By
similarity). {ECO:0000250|UniProtKB:Q9R182,
ECO:0000269|PubMed:23150577}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250,
ECO:0000305|PubMed:11877390}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:Q9R182}. Note=Colocalized with HSPG2 and
activated ITGB3 on podocytes. {ECO:0000250|UniProtKB:Q9R182}.
-!- TISSUE SPECIFICITY: Expressed principally in liver. Weakly
expressed in kidney. Binds to adipocytes. Increased expression and
colocalization with activated ITGB3 in glomeruli of patients with
nephrotic syndrome showing effaced podocyte foot processes (at
protein level). {ECO:0000269|PubMed:10644446,
ECO:0000269|PubMed:25710887, ECO:0000269|PubMed:26204133}.
-!- INDUCTION: Down-regulated by insulin.
{ECO:0000269|PubMed:26204133}.
-!- DOMAIN: The fibrinogen C-terminal domain is sufficient to mediate
endothelial cell adhesion. {ECO:0000269|PubMed:11877390}.
-!- PTM: O-glycosylated at Thr-226 by GALNT2; blocks processing and
activation by proprotein convertases.
{ECO:0000269|PubMed:20837471, ECO:0000269|PubMed:22566642}.
-!- PTM: In part proteolytically cleaved by proprotein convertases;
proposed to be involved in activation.
{ECO:0000269|PubMed:12909640, ECO:0000269|PubMed:20837471}.
-!- DISEASE: Hypobetalipoproteinemia, familial, 2 (FHBL2)
[MIM:605019]: A disorder of lipid metabolism characterized by less
than 5th percentile age- and sex-specific levels of low density
lipoproteins, and dietary fat malabsorption. Affected individuals
present with combined hypolipidemia, consisting of extremely low
plasma levels of LDL cholesterol, HDL cholesterol, and
triglycerides. {ECO:0000269|PubMed:20942659}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Note=May be involved in atherosclerosis. Plasma levels
are closely associated with arterial wall thickness.
{ECO:0000305|PubMed:17191020}.
-!- DISEASE: Note=May be involved in nephrotic syndrome.
{ECO:0000305|PubMed:25710887}.
-!- MISCELLANEOUS: Was suggested to inhibit LPL through a direct
mechanism; however, the necessary concentration to achieve in
vitro inhibition is at least 30-fold higher than ANGPTL3 plasma
concentration. {ECO:0000305|PubMed:19028676,
ECO:0000305|PubMed:20581395}.
-!- SEQUENCE CAUTION:
Sequence=AAH07059.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AF152562; AAD34156.1; -; mRNA.
EMBL; AY358273; AAQ88640.1; -; mRNA.
EMBL; AK315304; BAG37708.1; -; mRNA.
EMBL; AY569015; AAS66984.1; -; Genomic_DNA.
EMBL; FJ515851; ACS13743.1; -; Genomic_DNA.
EMBL; CH471059; EAX06583.1; -; Genomic_DNA.
EMBL; BC007059; AAH07059.1; ALT_SEQ; mRNA.
EMBL; BC058287; AAH58287.1; -; mRNA.
CCDS; CCDS622.1; -.
RefSeq; NP_055310.1; NM_014495.3.
UniGene; Hs.209153; -.
ProteinModelPortal; Q9Y5C1; -.
BioGrid; 118143; 5.
IntAct; Q9Y5C1; 3.
STRING; 9606.ENSP00000360170; -.
iPTMnet; Q9Y5C1; -.
PhosphoSitePlus; Q9Y5C1; -.
DMDM; 25008126; -.
EPD; Q9Y5C1; -.
PaxDb; Q9Y5C1; -.
PeptideAtlas; Q9Y5C1; -.
PRIDE; Q9Y5C1; -.
DNASU; 27329; -.
Ensembl; ENST00000371129; ENSP00000360170; ENSG00000132855.
GeneID; 27329; -.
KEGG; hsa:27329; -.
UCSC; uc001das.3; human.
CTD; 27329; -.
DisGeNET; 27329; -.
GeneCards; ANGPTL3; -.
HGNC; HGNC:491; ANGPTL3.
HPA; HPA038097; -.
MalaCards; ANGPTL3; -.
MIM; 604774; gene.
MIM; 605019; phenotype.
neXtProt; NX_Q9Y5C1; -.
OpenTargets; ENSG00000132855; -.
Orphanet; 426; Familial hypobetalipoproteinemia.
PharmGKB; PA24796; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GeneTree; ENSGT00890000139379; -.
HOGENOM; HOG000015386; -.
HOVERGEN; HBG001644; -.
InParanoid; Q9Y5C1; -.
OMA; FVHKTKG; -.
OrthoDB; EOG091G03M1; -.
PhylomeDB; Q9Y5C1; -.
TreeFam; TF336658; -.
Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
GeneWiki; ANGPTL3; -.
GenomeRNAi; 27329; -.
PRO; PR:Q9Y5C1; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000132855; -.
CleanEx; HS_ANGPTL3; -.
Genevisible; Q9Y5C1; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0004859; F:phospholipase inhibitor activity; IDA:BHF-UCL.
GO; GO:0055090; P:acylglycerol homeostasis; IDA:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IPI:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO; GO:0006631; P:fatty acid metabolic process; IDA:BHF-UCL.
GO; GO:0006071; P:glycerol metabolic process; IDA:BHF-UCL.
GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0055088; P:lipid homeostasis; IDA:BHF-UCL.
GO; GO:0019915; P:lipid storage; IDA:BHF-UCL.
GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IDA:BHF-UCL.
GO; GO:0010519; P:negative regulation of phospholipase activity; IDA:BHF-UCL.
GO; GO:0009395; P:phospholipid catabolic process; IDA:BHF-UCL.
GO; GO:0055091; P:phospholipid homeostasis; IDA:BHF-UCL.
GO; GO:0006644; P:phospholipid metabolic process; IDA:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:BHF-UCL.
GO; GO:0051004; P:regulation of lipoprotein lipase activity; TAS:Reactome.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
GO; GO:0070328; P:triglyceride homeostasis; IGI:MGI.
CDD; cd00087; FReD; 1.
Gene3D; 3.90.215.10; -; 1.
Gene3D; 4.10.530.10; -; 1.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
Pfam; PF00147; Fibrinogen_C; 1.
SMART; SM00186; FBG; 1.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
1: Evidence at protein level;
Angiogenesis; Cell adhesion; Cell projection; Coiled coil;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Heparin-binding; Lipid metabolism; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 16 {ECO:0000269|PubMed:15340161}.
CHAIN 17 460 Angiopoietin-related protein 3.
/FTId=PRO_0000009122.
CHAIN 17 224 ANGPTL3(17-224).
{ECO:0000305|PubMed:12909640}.
/FTId=PRO_0000435903.
CHAIN 17 221 ANGPTL3(17-221).
{ECO:0000305|PubMed:12909640}.
/FTId=PRO_0000435904.
DOMAIN 237 455 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
REGION 17 207 Sufficient to inhibit LIPG/EL
phospholipase activity.
{ECO:0000269|PubMed:17110602}.
REGION 17 165 Sufficient to inhibit LPL lipase
activity. {ECO:0000269|PubMed:12909640}.
REGION 32 56 Required for inhibition of LPL lipase
activity. {ECO:0000269|PubMed:19318355}.
COILED 85 210 {ECO:0000255}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10644446,
ECO:0000269|PubMed:16335952}.
CARBOHYD 226 226 O-linked (GalNAc) threonine.
{ECO:0000269|PubMed:20837471}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 357 357 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 246 274 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 394 408 {ECO:0000255|PROSITE-ProRule:PRU00739}.
VARIANT 63 63 K -> T (associated with low plasma
triglyceride level; fails to suppress LPL
activity in vitro; dbSNP:rs146749211).
{ECO:0000269|PubMed:19075393}.
/FTId=VAR_075670.
VARIANT 91 91 E -> G (associated with low plasma
triglyceride level; fails to suppress LPL
activity in vitro; dbSNP:rs139334976).
{ECO:0000269|PubMed:19075393}.
/FTId=VAR_075671.
VARIANT 127 127 L -> F (in dbSNP:rs72649573).
{ECO:0000269|PubMed:22095935}.
/FTId=VAR_067283.
VARIANT 164 164 L -> F (associated with low plasma
triglyceride level; fails to suppress LPL
activity in vitro; dbSNP:rs775976787).
{ECO:0000269|PubMed:19075393}.
/FTId=VAR_075672.
VARIANT 173 173 N -> S (associated with low plasma
triglyceride level; fails to suppress LPL
activity in vitro; no effect on protein
secretion; dbSNP:rs149624466).
{ECO:0000269|PubMed:19075393,
ECO:0000269|PubMed:25733326}.
/FTId=VAR_075673.
VARIANT 259 259 M -> T (common allele in African
americans; associated with low plasma
triglyceride level; fails to suppress LPL
activity in vitro; dbSNP:rs77871363).
{ECO:0000269|PubMed:19075393}.
/FTId=VAR_075674.
VARIANT 288 288 R -> Q (abolishes protein secretion;
associated with low plasma triglyceride
level; dbSNP:rs763904695).
{ECO:0000269|PubMed:19075393}.
/FTId=VAR_075675.
VARIANT 288 288 Missing (abolishes protein secretion;
associated with low plasma triglyceride
level). {ECO:0000269|PubMed:19075393}.
/FTId=VAR_075676.
VARIANT 292 292 S -> P (abolishes protein secretion;
associated with low plasma triglyceride
level; dbSNP:rs138899888).
{ECO:0000269|PubMed:19075393}.
/FTId=VAR_075677.
VARIANT 344 344 Y -> S (abolishes protein secretion;
associated with low plasma triglyceride
level). {ECO:0000269|PubMed:25733326}.
/FTId=VAR_075678.
VARIANT 375 375 E -> K (abolishes protein secretion;
associated with low plasma triglyceride
level; dbSNP:rs768802285).
{ECO:0000269|PubMed:19075393,
ECO:0000269|PubMed:25733326}.
/FTId=VAR_075679.
VARIANT 417 417 Y -> C (abolishes protein secretion;
associated with low plasma triglyceride
level; dbSNP:rs376210525).
{ECO:0000269|PubMed:19075393}.
/FTId=VAR_075680.
VARIANT 418 418 N -> Y (in dbSNP:rs4145257).
/FTId=VAR_049071.
MUTAGEN 62 63 HK->IN: Abolishes effect on plasma
triglyceride level; when associated with
N-65. {ECO:0000269|PubMed:12909640}.
MUTAGEN 63 63 K->N: Abolishes inhibitory effect on
LIPG/EL phospholipase activity; when
associated with N-65.
{ECO:0000269|PubMed:17110602}.
MUTAGEN 65 65 K->N: Abolishes effect on plasma
triglyceride level; when associated with
62-I-N-63. {ECO:0000269|PubMed:12909640}.
MUTAGEN 65 65 K->N: Abolishes inhibitory effect on
LIPG/EL phospholipase activity; when
associated with N-63.
{ECO:0000269|PubMed:17110602}.
MUTAGEN 204 205 RR->TT: Abolishes proteolytical cleavage
and effect on plasma triglyceride levels,
keeps in vitro inactivation of LPL
activity; when associated with S-221; S-
224 and S-235.
{ECO:0000269|PubMed:12909640}.
MUTAGEN 221 221 R->ST: Abolishes proteolytical cleavage
and effect on plasma triglyceride levels,
keeps in vitro inactivation of LPL
activity; when associated with 204-T-T-
205; S-224 and S-235.
{ECO:0000269|PubMed:12909640}.
MUTAGEN 224 224 R->S: Abolishes proteolytical cleavage
and effect on plasma triglyceride levels,
keeps in vitro inactivation of LPL
activity; when associated with 204-T-T-
205; S-221 and S-235.
{ECO:0000269|PubMed:12909640}.
MUTAGEN 235 235 R->T: Abolishes proteolytical cleavage
and effect on plasma triglyceride levels,
keeps in vitro inactivation of LPL
activity; when associated with 204-T-T-
205; S-221 and S-224.
{ECO:0000269|PubMed:12909640}.
CONFLICT 134 134 L -> P (in Ref. 3; BAG37708).
{ECO:0000305}.
SEQUENCE 460 AA; 53637 MW; 6279465FEEB91F56 CRC64;
MFTIKLLLFI VPLVISSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL LQLGHGLKDF
VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR RTTYKLQVKN EEVKNMSLEL
NSKLESLLEE KILLQQKVKY LEEQLTNLIQ NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ
TVEDQYKQLN QQHSQIKEIE NQLRRTSIQE PTEISLSSKP RAPRTTPFLQ LNEIRNVKHD
GIPAECTTIY NRGEHTSGMY AIRPSNSQVF HVYCDVISGS PWTLIQHRID GSQNFNETWE
NYKYGFGRLD GEFWLGLEKI YSIVKQSNYV LRIELEDWKD NKHYIEYSFY LGNHETNYTL
HLVAITGNVP NAIPENKDLV FSTWDHKAKG HFNCPEGYSG GWWWHDECGE NNLNGKYNKP
RAKSKPERRR GLSWKSQNGR LYSIKSTKML IHPTDSESFE


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