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O08538 (ANGP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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-1
Short name=ANG-1
Gene names
Name:Angpt1
Synonyms:Agpt
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme By similarity.

Subunit structure

Homooligomer. Interacts with TEK/TIE2 By similarity.

Subcellular location

Secreted.

Developmental stage

Early in development, at E9 to E11, it is found most prominently in the heart myocardium surrounding the endocardium. Later, it becomes more widely distributed, most often in the mesenchyme surrounding developing vessels, in close association with endothelial cells.

Disruption phenotype

Embryonically lethal. Embryos die at about 12.5 dpc, due to important developmental defects of the endocardium and myocardium, plus generalized defects in vascular development. Ref.3

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
   Cellular componentSecreted
   DomainCoiled coil
Signal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processTie receptor signaling pathway

Traceable author statement. Source: DFLAT

anti-apoptosis

Inferred from direct assay. Source: MGI

cardiac muscle tissue morphogenesis

Traceable author statement. Source: DFLAT

cell-substrate adhesion

Inferred from direct assay. Source: MGI

endocardium morphogenesis

Traceable author statement. Source: DFLAT

endoderm development

Traceable author statement. Source: MGI

glomerulus vasculature development

Inferred from direct assay. Source: MGI

hemopoiesis

Inferred from direct assay. Source: MGI

in utero embryonic development

Inferred from mutant phenotype. Source: MGI

negative regulation of vascular permeability

Inferred from direct assay. Source: MGI

patterning of blood vessels

Traceable author statement. Source: DFLAT

positive regulation of cell adhesion

Inferred from direct assay. Source: MGI

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay. Source: MGI

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.1. Source: MGI

positive regulation of phosphatidylinositol 3-kinase cascade

Inferred from direct assay. Source: MGI

positive regulation of vascular endothelial growth factor receptor signaling pathway

Traceable author statement. Source: DFLAT

vasculogenesis involved in coronary vascular morphogenesis

Traceable author statement. Source: DFLAT

   Molecular functionvascular endothelial growth factor receptor binding

Traceable author statement. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 498479Angiopoietin-1
PRO_0000009111

Regions

Domain277 – 497221Fibrinogen C-terminal
Coiled coil81 – 11939 Potential
Coiled coil153 – 261109 Potential

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation2431N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Potential
Disulfide bond286 ↔ 315 By similarity
Disulfide bond439 ↔ 452 By similarity

Experimental info

Sequence conflict2621I → V in AAB50558. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08538 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: FC36F905A9E79074

FASTA49857,519
        10         20         30         40         50         60 
MTVFLSFAFF AAILTHIGCS NQRRNPENGG RRYNRIQHGQ CAYTFILPEH DGNCRESATE 

        70         80         90        100        110        120 
QYNTNALQRD APHVEPDFSS QKLQHLEHVM ENYTQWLQKL ENYIVENMKS EMAQIQQNAV 

       130        140        150        160        170        180 
QNHTATMLEI GTSLLSQTAE QTRKLTDVET QVLNQTSRLE IQLLENSLST YKLEKQLLQQ 

       190        200        210        220        230        240 
TNEILKIHEK NSLLEHKILE MEGKHKEELD TLKEEKENLQ GLVSRQTFII QELEKQLSRA 

       250        260        270        280        290        300 
TNNNSILQKQ QLELMDTVHN LISLCTKEGV LLKGGKREEE KPFRDCADVY QAGFNKSGIY 

       310        320        330        340        350        360 
TIYFNNMPEP KKVFCNMDVN GGGWTVIQHR EDGSLDFQRG WKEYKMGFGN PSGEYWLGNE 

       370        380        390        400        410        420 
FIFAITSQRQ YMLRIELMDW EGNRAYSQYD RFHIGNEKQN YRLYLKGHTG TAGKQSSLIL 

       430        440        450        460        470        480 
HGADFSTKDA DNDNCMCKCA LMLTGGWWFD ACGPSNLNGM FYTAGQNHGK LNGIKWHYFK 

       490 
GPSYSLRSTT MMIRPLDF

« Hide

References

« Hide 'large scale' references
[1]"Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-trap expression cloning."
Davis S., Aldrich T.H., Jones P.F., Acheson A., Compton D.L., Jain V., Ryan T.E., Bruno J., Radziejewski C., Maisonpierre P.C., Yancopoulos G.D.
Cell 87:1161-1169(1996) [PubMed: 8980223] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[3]"Requisite role of angiopoietin-1, a ligand for the TIE2 receptor, during embryonic angiogenesis."
Suri C., Jones P.F., Patan S., Bartunkova S., Maisonpierre P.C., Davis S., Sato T.N., Yancopoulos G.D.
Cell 87:1171-1180(1996) [PubMed: 8980224] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U83509 mRNA. Translation: AAB50558.1.
BC067410 mRNA. Translation: AAH67410.1.
IPIIPI00114350.
RefSeqNP_033770.2. NM_009640.3.
UniGeneMm.309336.

3D structure databases

ProteinModelPortalO08538.
SMRO08538. Positions 283-497.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6051N.
STRINGO08538.

PTM databases

PhosphoSiteO08538.

Proteomic databases

PRIDEO08538.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022921; ENSMUSP00000022921; ENSMUSG00000022309.
GeneID11600.
KEGGmmu:11600.

Organism-specific databases

CTD284.
MGIMGI:108448. Angpt1.

Phylogenomic databases

eggNOGroNOG05832.
HOVERGENHBG001644.
InParanoidO08538.
OrthoDBEOG4ZGPC8.

Gene expression databases

ArrayExpressO08538.
BgeeO08538.
CleanExMM_ANGPT1.
GenevestigatorO08538.
GermOnlineENSMUSG00000022309. Mus musculus.

Family and domain databases

InterProIPR002181. Fibrinogen_a/b/g_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR020837. Fibrinogen_CS.
[Graphical view]
Gene3DG3DSA:3.90.215.10. Fibrinogen_a/b/g_C_1. 1 hit.
G3DSA:4.10.530.10. Fibrinogen_a/b/g_C_2. 1 hit.
KOK05465.
PfamPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. Fibrinogen_a/b/g_C. 1 hit.
PROSITEPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameANGP1_MOUSE
AccessionPrimary (citable) accession number: O08538
Secondary accession number(s): Q6NWV7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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