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Protein

Angiopoietin-related protein 3

Gene

ANGPTL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity1 Publication10 Publications
ANGPTL3(17-221): In vitro inhibits LPL activity; not effective on GPIHBP1-stabilized LPL.1 Publication
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).By similarity2 Publications

GO - Molecular functioni

  • enzyme inhibitor activity Source: UniProtKB
  • growth factor activity Source: BHF-UCL
  • heparin binding Source: UniProtKB-KW
  • integrin binding Source: UniProtKB
  • phospholipase inhibitor activity Source: BHF-UCL

GO - Biological processi

  • acylglycerol homeostasis Source: BHF-UCL
  • angiogenesis Source: UniProtKB-KW
  • artery morphogenesis Source: BHF-UCL
  • cell-matrix adhesion Source: UniProtKB
  • cholesterol homeostasis Source: BHF-UCL
  • cholesterol metabolic process Source: BHF-UCL
  • fatty acid metabolic process Source: BHF-UCL
  • glycerol metabolic process Source: BHF-UCL
  • integrin-mediated signaling pathway Source: UniProtKB
  • lipid homeostasis Source: BHF-UCL
  • lipid storage Source: BHF-UCL
  • negative regulation of lipoprotein lipase activity Source: BHF-UCL
  • negative regulation of phospholipase activity Source: BHF-UCL
  • phospholipid catabolic process Source: BHF-UCL
  • phospholipid homeostasis Source: BHF-UCL
  • phospholipid metabolic process Source: BHF-UCL
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of lipid catabolic process Source: BHF-UCL
  • response to hormone Source: Ensembl
  • signal transduction Source: BHF-UCL
  • triglyceride homeostasis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Cell adhesion, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Angiopoietin-related protein 3
Alternative name(s):
Angiopoietin-5
Short name:
ANG-5
Angiopoietin-like protein 3
Cleaved into the following 2 chains:
Gene namesi
Name:ANGPTL3
Synonyms:ANGPT5
ORF Names:UNQ153/PRO179
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:491. ANGPTL3.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • early endosome Source: Ensembl
  • extracellular space Source: BHF-UCL
  • Golgi apparatus Source: Ensembl
  • lamellipodium Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Secreted

Pathology & Biotechi

Involvement in diseasei

Hypobetalipoproteinemia, familial, 2 (FHBL2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:605019

May be involved in atherosclerosis. Plasma levels are closely associated with arterial wall thickness.

May be involved in nephrotic syndrome.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 632HK → IN: Abolishes effect on plasma triglyceride level; when associated with N-65. 1 Publication
Mutagenesisi63 – 631K → N: Abolishes inhibitory effect on LIPG/EL phospholipase activity; when associated with N-65. 1 Publication
Mutagenesisi65 – 651K → N: Abolishes effect on plasma triglyceride level; when associated with 62-I-N-63. 1 Publication
Mutagenesisi65 – 651K → N: Abolishes inhibitory effect on LIPG/EL phospholipase activity; when associated with N-63. 1 Publication
Mutagenesisi204 – 2052RR → 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. 1 Publication
Mutagenesisi221 – 2211R → 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. 1 Publication
Mutagenesisi224 – 2241R → 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. 1 Publication
Mutagenesisi235 – 2351R → 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. 1 Publication

Organism-specific databases

MalaCardsiANGPTL3.
MIMi605019. phenotype.
Orphaneti426. Familial hypobetalipoproteinemia.
PharmGKBiPA24796.

Polymorphism and mutation databases

DMDMi25008126.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Chaini17 – 460444Angiopoietin-related protein 3PRO_0000009122Add
BLAST
Chaini17 – 224208ANGPTL3(17-224)1 PublicationPRO_0000435903Add
BLAST
Chaini17 – 221205ANGPTL3(17-221)1 PublicationPRO_0000435904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi115 – 1151N-linked (GlcNAc...)2 Publications
Glycosylationi226 – 2261O-linked (GlcNAc) Probable1 Publication
Disulfide bondi246 ↔ 274PROSITE-ProRule annotation
Glycosylationi296 – 2961N-linked (GlcNAc...)2 Publications
Glycosylationi357 – 3571N-linked (GlcNAc...)1 Publication
Disulfide bondi394 ↔ 408PROSITE-ProRule annotation

Post-translational modificationi

O-glycosylated at Thr-226 by GALNT2; blocks processing and activation by proprotein convertases.2 Publications
In part proteolytically cleaved by proprotein convertases; proposed to be involved in activation.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y5C1.
PeptideAtlasiQ9Y5C1.
PRIDEiQ9Y5C1.

PTM databases

iPTMnetiQ9Y5C1.
PhosphoSiteiQ9Y5C1.

Expressioni

Tissue specificityi

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).3 Publications

Inductioni

Down-regulated by insulin.1 Publication

Gene expression databases

BgeeiQ9Y5C1.
CleanExiHS_ANGPTL3.
GenevisibleiQ9Y5C1. HS.

Organism-specific databases

HPAiHPA038097.

Interactioni

Subunit structurei

Interacts with ANGPTL8. Interacts with ITGB3 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • growth factor activity Source: BHF-UCL
  • integrin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi118143. 5 interactions.
IntActiQ9Y5C1. 3 interactions.
STRINGi9606.ENSP00000360170.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5C1.
SMRiQ9Y5C1. Positions 123-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini237 – 455219Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 207191Sufficient to inhibit LIPG/EL phospholipase activity1 PublicationAdd
BLAST
Regioni17 – 165149Sufficient to inhibit LPL lipase activity1 PublicationAdd
BLAST
Regioni32 – 5625Required for inhibition of LPL lipase activity1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili85 – 210126Sequence analysisAdd
BLAST

Domaini

The fibrinogen C-terminal domain is sufficient to mediate endothelial cell adhesion.1 Publication

Sequence similaritiesi

Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000015386.
HOVERGENiHBG001644.
InParanoidiQ9Y5C1.
OMAiFSTWDHK.
OrthoDBiEOG7X9G60.
PhylomeDBiQ9Y5C1.
TreeFamiTF336658.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
[Graphical view]
PfamiPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y5C1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTIKLLLFI VPLVISSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL
60 70 80 90 100
LQLGHGLKDF VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR
110 120 130 140 150
RTTYKLQVKN EEVKNMSLEL NSKLESLLEE KILLQQKVKY LEEQLTNLIQ
160 170 180 190 200
NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ TVEDQYKQLN QQHSQIKEIE
210 220 230 240 250
NQLRRTSIQE PTEISLSSKP RAPRTTPFLQ LNEIRNVKHD GIPAECTTIY
260 270 280 290 300
NRGEHTSGMY AIRPSNSQVF HVYCDVISGS PWTLIQHRID GSQNFNETWE
310 320 330 340 350
NYKYGFGRLD GEFWLGLEKI YSIVKQSNYV LRIELEDWKD NKHYIEYSFY
360 370 380 390 400
LGNHETNYTL HLVAITGNVP NAIPENKDLV FSTWDHKAKG HFNCPEGYSG
410 420 430 440 450
GWWWHDECGE NNLNGKYNKP RAKSKPERRR GLSWKSQNGR LYSIKSTKML
460
IHPTDSESFE
Length:460
Mass (Da):53,637
Last modified:November 1, 1999 - v1
Checksum:i6279465FEEB91F56
GO

Sequence cautioni

The sequence AAH07059.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341L → P in BAG37708 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631K → T Associated with low plasma triglyceride level, fails to suppress LPL activity in vitro. 1 Publication
VAR_075670
Natural varianti91 – 911E → G Associated with low plasma triglyceride level, fails to suppress LPL activity in vitro. 1 Publication
VAR_075671
Natural varianti127 – 1271L → F.1 Publication
Corresponds to variant rs72649573 [ dbSNP | Ensembl ].
VAR_067283
Natural varianti164 – 1641L → F Associated with low plasma triglyceride level, fails to suppress LPL activity in vitro. 1 Publication
VAR_075672
Natural varianti173 – 1731N → S Associated with low plasma triglyceride level, fails to suppress LPL activity in vitro, no effect on protein secretion. 2 Publications
VAR_075673
Natural varianti259 – 2591M → T Common allele in African americans, associated with low plasma triglyceride level, fails to suppress LPL activity in vitro. 1 Publication
VAR_075674
Natural varianti288 – 2881R → Q Abolishes protein secretion, associated with low plasma triglyceride level. 1 Publication
VAR_075675
Natural varianti288 – 2881Missing Abolishes protein secretion, associated with low plasma triglyceride level. 1 Publication
VAR_075676
Natural varianti292 – 2921S → P Abolishes protein secretion, associated with low plasma triglyceride level. 1 Publication
VAR_075677
Natural varianti344 – 3441Y → S Abolishes protein secretion, associated with low plasma triglyceride level. 1 Publication
VAR_075678
Natural varianti375 – 3751E → K Abolishes protein secretion, associated with low plasma triglyceride level. 2 Publications
VAR_075679
Natural varianti417 – 4171Y → C Abolishes protein secretion, associated with low plasma triglyceride level. 1 Publication
VAR_075680
Natural varianti418 – 4181N → Y.
Corresponds to variant rs4145257 [ dbSNP | Ensembl ].
VAR_049071

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152562 mRNA. Translation: AAD34156.1.
AY358273 mRNA. Translation: AAQ88640.1.
AK315304 mRNA. Translation: BAG37708.1.
AY569015 Genomic DNA. Translation: AAS66984.1.
FJ515851 Genomic DNA. Translation: ACS13743.1.
CH471059 Genomic DNA. Translation: EAX06583.1.
BC007059 mRNA. Translation: AAH07059.1. Sequence problems.
BC058287 mRNA. Translation: AAH58287.1.
CCDSiCCDS622.1.
RefSeqiNP_055310.1. NM_014495.3.
UniGeneiHs.209153.

Genome annotation databases

EnsembliENST00000371129; ENSP00000360170; ENSG00000132855.
GeneIDi27329.
KEGGihsa:27329.
UCSCiuc001das.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152562 mRNA. Translation: AAD34156.1.
AY358273 mRNA. Translation: AAQ88640.1.
AK315304 mRNA. Translation: BAG37708.1.
AY569015 Genomic DNA. Translation: AAS66984.1.
FJ515851 Genomic DNA. Translation: ACS13743.1.
CH471059 Genomic DNA. Translation: EAX06583.1.
BC007059 mRNA. Translation: AAH07059.1. Sequence problems.
BC058287 mRNA. Translation: AAH58287.1.
CCDSiCCDS622.1.
RefSeqiNP_055310.1. NM_014495.3.
UniGeneiHs.209153.

3D structure databases

ProteinModelPortaliQ9Y5C1.
SMRiQ9Y5C1. Positions 123-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118143. 5 interactions.
IntActiQ9Y5C1. 3 interactions.
STRINGi9606.ENSP00000360170.

PTM databases

iPTMnetiQ9Y5C1.
PhosphoSiteiQ9Y5C1.

Polymorphism and mutation databases

DMDMi25008126.

Proteomic databases

PaxDbiQ9Y5C1.
PeptideAtlasiQ9Y5C1.
PRIDEiQ9Y5C1.

Protocols and materials databases

DNASUi27329.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371129; ENSP00000360170; ENSG00000132855.
GeneIDi27329.
KEGGihsa:27329.
UCSCiuc001das.3. human.

Organism-specific databases

CTDi27329.
GeneCardsiANGPTL3.
HGNCiHGNC:491. ANGPTL3.
HPAiHPA038097.
MalaCardsiANGPTL3.
MIMi604774. gene.
605019. phenotype.
neXtProtiNX_Q9Y5C1.
Orphaneti426. Familial hypobetalipoproteinemia.
PharmGKBiPA24796.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000015386.
HOVERGENiHBG001644.
InParanoidiQ9Y5C1.
OMAiFSTWDHK.
OrthoDBiEOG7X9G60.
PhylomeDBiQ9Y5C1.
TreeFamiTF336658.

Miscellaneous databases

GeneWikiiANGPTL3.
GenomeRNAii27329.
PROiQ9Y5C1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5C1.
CleanExiHS_ANGPTL3.
GenevisibleiQ9Y5C1. HS.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
[Graphical view]
PfamiPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a mammalian angiopoietin-related protein expressed specifically in liver."
    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.
    Genomics 62:477-482(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-115.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. SeattleSNPs variation discovery resource
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver and Skeletal muscle.
  8. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-31.
  9. "ANGPTL3 stimulates endothelial cell adhesion and migration via integrin alpha vbeta 3 and induces blood vessel formation in vivo."
    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.
    J. Biol. Chem. 277:17281-17290(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, DOMAIN.
  10. "ANGPTL3 decreases very low density lipoprotein triglyceride clearance by inhibition of lipoprotein lipase."
    Shimizugawa T., Ono M., Shimamura M., Yoshida K., Ando Y., Koishi R., Ueda K., Inaba T., Minekura H., Kohama T., Furukawa H.
    J. Biol. Chem. 277:33742-33748(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: FUNCTION.
  12. "Angiopoietin-like protein 3, a hepatic secretory factor, activates lipolysis in adipocytes."
    Shimamura M., Matsuda M., Kobayashi S., Ando Y., Ono M., Koishi R., Furukawa H., Makishima M., Shimomura I.
    Biochem. Biophys. Res. Commun. 301:604-609(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  13. "Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo."
    Ono M., Shimizugawa T., Shimamura M., Yoshida K., Noji-Sakikawa C., Ando Y., Koishi R., Furukawa H.
    J. Biol. Chem. 278:41804-41809(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC CLEAVAGE, FUNCTION, MUTAGENESIS OF 62-HIS-LYS-63; LYS-65; 204-ARG-ARG-205; ARG-221; ARG-224 AND ARG-235.
  14. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115; ASN-296 AND ASN-357.
    Tissue: Plasma.
  15. Cited for: FUNCTION.
  16. "Association between plasma angiopoietin-like protein 3 and arterial wall thickness in healthy subjects."
    Hatsuda S., Shoji T., Shinohara K., Kimoto E., Mori K., Fukumoto S., Koyama H., Emoto M., Nishizawa Y.
    J. Vasc. Res. 44:61-66(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN ATHEROSCLEROSIS.
  17. "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."
    Li Y., Sun L., Xu H., Fang Z., Yao W., Guo W., Rao J., Zha X.
    Acta Biochim. Biophys. Sin. 40:459-465(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "The angiopoietin-like proteins ANGPTL3 and ANGPTL4 inhibit lipoprotein lipase activity through distinct mechanisms."
    Shan L., Yu X.C., Liu Z., Hu Y., Sturgis L.T., Miranda M.L., Liu Q.
    J. Biol. Chem. 284:1419-1424(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "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)."
    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.
    J. Biol. Chem. 284:13735-13745(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4."
    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.
    J. Lipid Res. 50:2421-2429(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ANGPTL3(17-221)).
  21. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296.
    Tissue: Liver.
  22. "Angiopoietin-like protein 3 inhibits lipoprotein lipase activity through enhancing its cleavage by proprotein convertases."
    Liu J., Afroza H., Rader D.J., Jin W.
    J. Biol. Chem. 285:27561-27570(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "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."
    Schjoldager K.T., Vester-Christensen M.B., Bennett E.P., Levery S.B., Schwientek T., Yin W., Blixt O., Clausen H.
    J. Biol. Chem. 285:36293-36303(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-226.
  24. Cited for: INVOLVEMENT IN FHBL2.
  25. "Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 109:9893-9898(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  26. Cited for: INTERACTION WITH ANGPTL8.
  27. "Angptl3 deficiency is associated with increased insulin sensitivity, lipoprotein lipase activity, and decreased serum free fatty acids."
    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.
    Arterioscler. Thromb. Vasc. Biol. 33:1706-1713(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. "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."
    Tikka A., Soronen J., Laurila P.P., Metso J., Ehnholm C., Jauhiainen M.
    Biosci. Rep. 34:E00160-E00160(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  29. Cited for: TISSUE SPECIFICITY, INDUCTION.
  30. "Genetic variation in APOB, PCSK9, and ANGPTL3 in carriers of pathogenic autosomal dominant hypercholesterolemic mutations with unexpected low LDL-Cl Levels."
    Huijgen R., Sjouke B., Vis K., de Randamie J.S., Defesche J.C., Kastelein J.J., Hovingh G.K., Fouchier S.W.
    Hum. Mutat. 33:448-455(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PHE-127.
  31. "Rare loss-of-function mutations in ANGPTL family members contribute to plasma triglyceride levels in humans."
    Romeo S., Yin W., Kozlitina J., Pennacchio L.A., Boerwinkle E., Hobbs H.H., Cohen J.C.
    J. Clin. Invest. 119:70-79(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-63; GLY-91; PHE-164; SER-173; THR-259; GLN-288; PRO-292; LYS-375 AND CYS-417, CHARACTERIZATION OF VARIANTS THR-63; GLY-91; PHE-164; SER-173; THR-259; ARG-GLN; PRO-292; LYS-375 AND CYS-417.
  32. "Clinical and genetic analysis of a family diagnosed with familial hypobetalipoproteinemia in which the proband was diagnosed with diabetes mellitus."
    Wang X., Wang D., Shan Z.
    Atherosclerosis 239:552-556(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-344, CHARACTERIZATION OF VARIANTS SER-173; SER-344 AND LYS-375.
  33. "A novel role of angiopoietin-like-3 associated with podocyte injury."
    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.
    Pediatr. Res. 77:732-739(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, POSSIBLE INVOLVEMENT IN NEPHROTIC SYNDROME.

Entry informationi

Entry nameiANGL3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5C1
Secondary accession number(s): A0JLS0, B1ALJ0, B2RCW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.2 Publications

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.