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Q9Y5C1 (ANGL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiopoietin-related protein 3
Alternative name(s):
Angiopoietin-5
Short name=ANG-5
Angiopoietin-like protein 3
Gene names
Name:ANGPTL3
Synonyms:ANGPT5
ORF Names:UNQ153/PRO179
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Interacts with C19orf80/ANGPTL8. Ref.12

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed principally in liver. Weakly expressed in kidney. Ref.1

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacylglycerol homeostasis

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

artery morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cell-matrix adhesion

Inferred from physical interaction PubMed 11877390. Source: UniProtKB

cholesterol homeostasis

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

cholesterol metabolic process

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

fatty acid metabolic process

Inferred from direct assay PubMed 12565906. Source: BHF-UCL

glycerol metabolic process

Inferred from direct assay PubMed 12565906. Source: BHF-UCL

integrin-mediated signaling pathway

Non-traceable author statement PubMed 11877390. Source: UniProtKB

lipid homeostasis

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

lipid storage

Inferred from direct assay PubMed 12565906. Source: BHF-UCL

negative regulation of lipoprotein lipase activity

Inferred from direct assay PubMed 17110602PubMed 19542565. Source: BHF-UCL

negative regulation of phospholipase activity

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

phospholipid catabolic process

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

phospholipid homeostasis

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

phospholipid metabolic process

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

positive regulation of angiogenesis

Inferred from direct assay PubMed 11877390. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay PubMed 11877390. Source: UniProtKB

positive regulation of lipid catabolic process

Inferred from direct assay PubMed 12565906. Source: BHF-UCL

response to hormone

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from direct assay PubMed 11877390. Source: BHF-UCL

triglyceride homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from direct assay PubMed 12565906. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

   Molecular_functionenzyme inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

growth factor activity

Inferred from direct assay PubMed 11877390. Source: BHF-UCL

integrin binding

Inferred from physical interaction PubMed 11877390. Source: UniProtKB

phospholipase inhibitor activity

Inferred from direct assay PubMed 17110602. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.8
Chain17 – 460444Angiopoietin-related protein 3
PRO_0000009122

Regions

Domain237 – 455219Fibrinogen C-terminal
Coiled coil85 – 210126 Potential

Amino acid modifications

Glycosylation1151N-linked (GlcNAc...) Ref.1 Ref.9
Glycosylation2961N-linked (GlcNAc...) Ref.9 Ref.10
Glycosylation3571N-linked (GlcNAc...) Ref.9
Disulfide bond246 ↔ 274 By similarity
Disulfide bond394 ↔ 408 By similarity

Natural variations

Natural variant1271L → F. Ref.13
Corresponds to variant rs72649573 [ dbSNP | Ensembl ].
VAR_067283
Natural variant4181N → Y.
Corresponds to variant rs4145257 [ dbSNP | Ensembl ].
VAR_049071

Experimental info

Sequence conflict1341L → P in BAG37708. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9Y5C1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 6279465FEEB91F56

FASTA46053,637
        10         20         30         40         50         60 
MFTIKLLLFI VPLVISSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL LQLGHGLKDF 

        70         80         90        100        110        120 
VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR RTTYKLQVKN EEVKNMSLEL 

       130        140        150        160        170        180 
NSKLESLLEE KILLQQKVKY LEEQLTNLIQ NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ 

       190        200        210        220        230        240 
TVEDQYKQLN QQHSQIKEIE NQLRRTSIQE PTEISLSSKP RAPRTTPFLQ LNEIRNVKHD 

       250        260        270        280        290        300 
GIPAECTTIY NRGEHTSGMY AIRPSNSQVF HVYCDVISGS PWTLIQHRID GSQNFNETWE 

       310        320        330        340        350        360 
NYKYGFGRLD GEFWLGLEKI YSIVKQSNYV LRIELEDWKD NKHYIEYSFY LGNHETNYTL 

       370        380        390        400        410        420 
HLVAITGNVP NAIPENKDLV FSTWDHKAKG HFNCPEGYSG GWWWHDECGE NNLNGKYNKP 

       430        440        450        460 
RAKSKPERRR GLSWKSQNGR LYSIKSTKML IHPTDSESFE 

« Hide

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
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. expand/collapse author list , 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.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. 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] [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]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. expand/collapse author list , 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
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]"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.
[10]"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.
[11]"Exome sequencing, ANGPTL3 mutations, and familial combined hypolipidemia."
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. expand/collapse author list , DePristo M.A., Daly M.J., Cohen J.C., Hobbs H.H., Altshuler D., Schonfeld G., Gabriel S.B., Yue P., Kathiresan S.
N. Engl. J. Med. 363:2220-2227(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FHBL2.
[12]"Atypical angiopoietin-like protein that regulates ANGPTL3."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:19751-19756(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C19ORF80/ANGPTL8.
[13]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS622.1.
RefSeqNP_055310.1. NM_014495.3.
UniGeneHs.209153.

3D structure databases

ProteinModelPortalQ9Y5C1.
SMRQ9Y5C1. Positions 123-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118143. 1 interaction.
IntActQ9Y5C1. 1 interaction.
STRING9606.ENSP00000360170.

PTM databases

PhosphoSiteQ9Y5C1.

Polymorphism databases

DMDM25008126.

Proteomic databases

PaxDbQ9Y5C1.
PeptideAtlasQ9Y5C1.
PRIDEQ9Y5C1.

Protocols and materials databases

DNASU27329.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371129; ENSP00000360170; ENSG00000132855.
GeneID27329.
KEGGhsa:27329.
UCSCuc001das.2. human.

Organism-specific databases

CTD27329.
GeneCardsGC01P062998.
HGNCHGNC:491. ANGPTL3.
HPAHPA038097.
MIM604774. gene.
605019. phenotype.
neXtProtNX_Q9Y5C1.
Orphanet426. Familial hypobetalipoproteinemia.
PharmGKBPA24796.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262343.
HOGENOMHOG000015386.
HOVERGENHBG001644.
InParanoidQ9Y5C1.
OMATKMLIHP.
OrthoDBEOG7X9G60.
PhylomeDBQ9Y5C1.
TreeFamTF336658.

Gene expression databases

ArrayExpressQ9Y5C1.
BgeeQ9Y5C1.
CleanExHS_ANGPTL3.
GenevestigatorQ9Y5C1.

Family and domain databases

Gene3D3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
[Graphical view]
PfamPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. SSF56496. 1 hit.
PROSITEPS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiANGPTL3.
GenomeRNAi27329.
NextBio50368.
PROQ9Y5C1.
SOURCESearch...

Entry information

Entry nameANGL3_HUMAN
AccessionPrimary (citable) accession number: Q9Y5C1
Secondary accession number(s): A0JLS0, B1ALJ0, B2RCW1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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