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O08538

- ANGP1_MOUSE

UniProt

O08538 - ANGP1_MOUSE

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Protein

Angiopoietin-1

Gene

Angpt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. receptor binding Source: MGI
  2. vascular endothelial growth factor receptor binding Source: MGI

GO - Biological processi

  1. activation of transmembrane receptor protein tyrosine kinase activity Source: Ensembl
  2. angiogenesis Source: MGI
  3. cardiac muscle tissue morphogenesis Source: DFLAT
  4. cell-substrate adhesion Source: MGI
  5. endocardium morphogenesis Source: DFLAT
  6. endoderm development Source: MGI
  7. glomerulus vasculature development Source: MGI
  8. hemopoiesis Source: MGI
  9. heparin biosynthetic process Source: Ensembl
  10. in utero embryonic development Source: MGI
  11. negative regulation of cell adhesion Source: Ensembl
  12. negative regulation of endothelial cell apoptotic process Source: Ensembl
  13. negative regulation of neuron apoptotic process Source: MGI
  14. negative regulation of vascular permeability Source: MGI
  15. patterning of blood vessels Source: DFLAT
  16. positive chemotaxis Source: Ensembl
  17. positive regulation of blood vessel endothelial cell migration Source: Ensembl
  18. positive regulation of cell adhesion Source: MGI
  19. positive regulation of endothelial cell migration Source: DFLAT
  20. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  21. positive regulation of peptidyl-serine phosphorylation Source: MGI
  22. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  23. positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  24. positive regulation of protein kinase B signaling Source: Ensembl
  25. positive regulation of protein ubiquitination Source: Ensembl
  26. positive regulation of receptor internalization Source: Ensembl
  27. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: DFLAT
  28. protein localization to cell surface Source: Ensembl
  29. regulation of satellite cell proliferation Source: Ensembl
  30. sprouting angiogenesis Source: Ensembl
  31. Tie signaling pathway Source: DFLAT
  32. transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
  33. vasculogenesis Source: DFLAT
  34. vasculogenesis involved in coronary vascular morphogenesis Source: DFLAT
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Differentiation

Enzyme and pathway databases

ReactomeiREACT_211860. Tie2 Signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiopoietin-1
Short name:
ANG-1
Gene namesi
Name:Angpt1
Synonyms:Agpt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:108448. Angpt1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. membrane raft Source: Ensembl
  4. microvillus Source: Ensembl
  5. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 498479Angiopoietin-1PRO_0000009111Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi286 ↔ 315PROSITE-ProRule annotation
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi439 ↔ 452PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO08538.
PaxDbiO08538.
PRIDEiO08538.

PTM databases

PhosphoSiteiO08538.

Expressioni

Developmental stagei

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.

Gene expression databases

BgeeiO08538.
CleanExiMM_ANGPT1.
ExpressionAtlasiO08538. baseline and differential.
GenevestigatoriO08538.

Interactioni

Subunit structurei

Homooligomer. Interacts with TEK/TIE2 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-6051N.
STRINGi10090.ENSMUSP00000022921.

Structurei

3D structure databases

ProteinModelPortaliO08538.
SMRiO08538. Positions 151-497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini277 – 497221Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili81 – 11939Sequence AnalysisAdd
BLAST
Coiled coili153 – 261109Sequence AnalysisAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG310490.
GeneTreeiENSGT00760000118809.
HOVERGENiHBG001644.
InParanoidiO08538.
KOiK05465.
OMAiTSQRQYS.
OrthoDBiEOG7X9G60.
TreeFamiTF336658.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR028843. Ang-1.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PANTHERiPTHR19143:SF156. PTHR19143:SF156. 1 hit.
PfamiPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O08538-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVFLSFAFF AAILTHIGCS NQRRNPENGG RRYNRIQHGQ CAYTFILPEH
60 70 80 90 100
DGNCRESATE QYNTNALQRD APHVEPDFSS QKLQHLEHVM ENYTQWLQKL
110 120 130 140 150
ENYIVENMKS EMAQIQQNAV QNHTATMLEI GTSLLSQTAE QTRKLTDVET
160 170 180 190 200
QVLNQTSRLE IQLLENSLST YKLEKQLLQQ TNEILKIHEK NSLLEHKILE
210 220 230 240 250
MEGKHKEELD TLKEEKENLQ GLVSRQTFII QELEKQLSRA TNNNSILQKQ
260 270 280 290 300
QLELMDTVHN LISLCTKEGV LLKGGKREEE KPFRDCADVY QAGFNKSGIY
310 320 330 340 350
TIYFNNMPEP KKVFCNMDVN GGGWTVIQHR EDGSLDFQRG WKEYKMGFGN
360 370 380 390 400
PSGEYWLGNE FIFAITSQRQ YMLRIELMDW EGNRAYSQYD RFHIGNEKQN
410 420 430 440 450
YRLYLKGHTG TAGKQSSLIL HGADFSTKDA DNDNCMCKCA LMLTGGWWFD
460 470 480 490
ACGPSNLNGM FYTAGQNHGK LNGIKWHYFK GPSYSLRSTT MMIRPLDF
Length:498
Mass (Da):57,519
Last modified:July 27, 2011 - v2
Checksum:iFC36F905A9E79074
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621I → V in AAB50558. (PubMed:8980223)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U83509 mRNA. Translation: AAB50558.1.
BC067410 mRNA. Translation: AAH67410.1.
CCDSiCCDS27450.1.
RefSeqiNP_033770.2. NM_009640.4.
UniGeneiMm.309336.

Genome annotation databases

EnsembliENSMUST00000022921; ENSMUSP00000022921; ENSMUSG00000022309.
GeneIDi11600.
KEGGimmu:11600.
UCSCiuc007vpc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U83509 mRNA. Translation: AAB50558.1 .
BC067410 mRNA. Translation: AAH67410.1 .
CCDSi CCDS27450.1.
RefSeqi NP_033770.2. NM_009640.4.
UniGenei Mm.309336.

3D structure databases

ProteinModelPortali O08538.
SMRi O08538. Positions 151-497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6051N.
STRINGi 10090.ENSMUSP00000022921.

PTM databases

PhosphoSitei O08538.

Proteomic databases

MaxQBi O08538.
PaxDbi O08538.
PRIDEi O08538.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022921 ; ENSMUSP00000022921 ; ENSMUSG00000022309 .
GeneIDi 11600.
KEGGi mmu:11600.
UCSCi uc007vpc.1. mouse.

Organism-specific databases

CTDi 284.
MGIi MGI:108448. Angpt1.

Phylogenomic databases

eggNOGi NOG310490.
GeneTreei ENSGT00760000118809.
HOVERGENi HBG001644.
InParanoidi O08538.
KOi K05465.
OMAi TSQRQYS.
OrthoDBi EOG7X9G60.
TreeFami TF336658.

Enzyme and pathway databases

Reactomei REACT_211860. Tie2 Signaling.

Miscellaneous databases

ChiTaRSi ANGPT1. mouse.
NextBioi 279116.
PROi O08538.
SOURCEi Search...

Gene expression databases

Bgeei O08538.
CleanExi MM_ANGPT1.
ExpressionAtlasi O08538. baseline and differential.
Genevestigatori O08538.

Family and domain databases

Gene3Di 3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProi IPR028843. Ang-1.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view ]
PANTHERi PTHR19143:SF156. PTHR19143:SF156. 1 hit.
Pfami PF00147. Fibrinogen_C. 1 hit.
[Graphical view ]
SMARTi SM00186. FBG. 1 hit.
[Graphical view ]
SUPFAMi SSF56496. SSF56496. 1 hit.
PROSITEi PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  4. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiANGP1_MOUSE
AccessioniPrimary (citable) accession number: O08538
Secondary accession number(s): Q6NWV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3