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UniProtKB/Swiss-Prot entry Q9Y5C1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ANGL3_HUMAN
Primary accession number Q9Y5C1
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 68)
Name and origin of the protein
Protein name Angiopoietin-related protein 3 [Precursor]
Synonyms Angiopoietin-like 3
Angiopoietin-5
ANG-5
Gene name
Name: ANGPTL3
Synonyms: ANGPT5
ORFNames: UNQ153/PRO179
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND GLYCOSYLATION AT ASN-115.
TISSUE=Liver;
DOI=10.1006/geno.1999.6041; PubMed=10644446 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
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 [GENOMIC DNA].
SeattleSNPs program for genomic applications;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
PROTEIN SEQUENCE OF 17-31.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115; ASN-296 AND ASN-357, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF152562; AAD34156.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358273; AAQ88640.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY569015; AAS66984.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058287; AAH58287.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_055310.1; -.
UniGene Hs.209153
3D structure databases
HSSP P02671; 1FZD. [HSSP ENTRY / PDB]
ModBase Q9Y5C1.
Protein-protein interaction databases
IntAct Q9Y5C1; -.
Organism-specific databases
H-InvDB HIX0028565; -.
HGNC HGNC:491; ANGPTL3.
GenAtlas ANGPTL3.
MIM 604774; gene. [NCBI / EBI]
PharmGKB PA24796; -.
GeneCards Q9Y5C1.
Gene expression databases
ArrayExpress Q9Y5C1; -.
CleanEx HS_ANGPTL3; -.
GermOnline ENSG00000132855; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0043498; Molecular function: cell surface binding (inferred from direct assay from UniProtKB).
GO:0008083; Molecular function: growth factor activity (inferred from direct assay from UniProtKB).
GO:0005178; Molecular function: integrin binding (inferred from physical interaction from UniProtKB).
GO:0004859; Molecular function: phospholipase inhibitor activity (inferred from direct assay from UniProtKB).
GO:0055090; Biological process: acylglycerol homeostasis (inferred from direct assay from UniProtKB).
GO:0048844; Biological process: artery morphogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0007160; Biological process: cell-matrix adhesion (inferred from physical interaction from UniProtKB).
GO:0042632; Biological process: cholesterol homeostasis (inferred from direct assay from UniProtKB).
GO:0008203; Biological process: cholesterol metabolic process (inferred from direct assay from UniProtKB).
GO:0006631; Biological process: fatty acid metabolic process (inferred from direct assay from UniProtKB).
GO:0006071; Biological process: glycerol metabolic process (inferred from direct assay from UniProtKB).
GO:0007229; Biological process: integrin-mediated signaling pathway (non-traceable author statement from UniProtKB).
GO:0051005; Biological process: negative regulation of lipoprotein lipase activity (inferred from direct assay from UniProtKB).
GO:0010519; Biological process: negative regulation of phospholipase activity (inferred from direct assay from UniProtKB).
GO:0009395; Biological process: phospholipid catabolic process (inferred from direct assay from UniProtKB).
GO:0055091; Biological process: phospholipid homeostasis (inferred from direct assay from UniProtKB).
GO:0045766; Biological process: positive regulation of angiogenesis (inferred from direct assay from UniProtKB).
GO:0030335; Biological process: positive regulation of cell migration (inferred from direct assay from UniProtKB).
GO:0050996; Biological process: positive regulation of lipid catabolic process (inferred from direct assay from UniProtKB).
GO:0019915; Biological process: sequestering of lipid (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002181; Fibrinogen_a/b/g_C.
IPR014716; Fibrinogen_a/b/g_C_1.
Graphical view of domain structure.
Gene3D G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1.
Pfam PF00147; Fibrinogen_C; 1.
Pfam graphical view of domain structure.
SMART SM00186; FBG; 1.
SMART graphical view of domain structure.
PROSITE PS00514; FIBRINOGEN_C_1; FALSE_NEG.
PS51406; FIBRINOGEN_C_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9Y5C1.
Proteomic databases
PeptideAtlas Q9Y5C1; -.
Genome annotation databases
Ensembl ENSG00000132855; Homo sapiens. [Contig view]
GeneID 27329; -.
KEGG hsa:27329; -.
Phylogenomic databases
HOGENOM Q9Y5C1; -.
HOVERGEN Q9Y5C1; -.
Other
NextBio 50368; -.
SOURCE ANGPTL3; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Coiled coil; Direct protein sequencing; Glycoprotein; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    16  16      
CHAIN   17   460  444     Angiopoietin-related protein 3. PRO_0000009122
DOMAIN   237   455  219     Fibrinogen C-terminal. 
COILED   85   210  126     Potential. 
CARBOHYD   115   115        N-linked (GlcNAc...). 
CARBOHYD   296   296        N-linked (GlcNAc...). 
CARBOHYD   357   357        N-linked (GlcNAc...). 
DISULFID   246   274        By similarity. 
DISULFID   394   408        By similarity. 
Sequence information
Length: 460 AA [This is the length of the unprocessed precursor] Molecular weight: 53637 Da [This is the MW of the unprocessed precursor] CRC64: 6279465FEEB91F56 [This is a checksum on the sequence]
        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 

Q9Y5C1 in FASTA format

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