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O35608 (ANGP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-2

Short name=ANG-2
Gene names
Name:Angpt2
Synonyms:Agpt2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal By similarity.

Subunit structure

Interacts with TEK/TIE2, competing for the same binding site as ANGPT1 By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed only at sites of vascular remodeling.

Domain

The Fibrinogen C-terminal domain mediates interaction with the TEK/TIE2 receptor By similarity.

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
   Cellular componentSecreted
   DomainCoiled coil
Signal
   LigandCalcium
Metal-binding
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processTie signaling pathway

Traceable author statement PubMed 20299672. Source: DFLAT

angiogenesis

Inferred from genetic interaction PubMed 16778080. Source: MGI

blood vessel morphogenesis

Inferred from mutant phenotype PubMed 15579434. Source: MGI

blood vessel remodeling

Traceable author statement PubMed 20299672. Source: DFLAT

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

endoderm development

Traceable author statement PubMed 10051567. Source: MGI

germ cell development

Inferred from electronic annotation. Source: Ensembl

glomerulus vasculature development

Inferred from electronic annotation. Source: Ensembl

hemopoiesis

Traceable author statement PubMed 20299672. Source: DFLAT

maternal process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

negative regulation of angiogenesis

Inferred from direct assay Ref.1. Source: MGI

negative regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell-substrate adhesion

Inferred from direct assay PubMed 9846489. Source: MGI

negative regulation of positive chemotaxis

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of angiogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

response to activity

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to radiation

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein tyrosine kinase signaling pathway

Traceable author statement PubMed 8384837. Source: MGI

   Cellular_componentcell projection

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

vascular endothelial growth factor receptor binding

Traceable author statement PubMed 10051567. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 496478Angiopoietin-2
PRO_0000009114

Regions

Domain275 – 495221Fibrinogen C-terminal
Coiled coil159 – 25698 Potential

Sites

Metal binding4291Calcium By similarity
Metal binding4311Calcium By similarity
Metal binding4331Calcium; via carbonyl oxygen By similarity
Metal binding4351Calcium; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation3041N-linked (GlcNAc...) Potential
Disulfide bond284 ↔ 313 By similarity
Disulfide bond433 ↔ 435 By similarity
Disulfide bond437 ↔ 450 By similarity

Experimental info

Sequence conflict3481S → N in AAB63189. Ref.1
Sequence conflict4111G → A in AAB63189. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35608 [UniParc].

Last modified April 26, 2004. Version 2.
Checksum: E7563B498A0EF331

FASTA49656,576
        10         20         30         40         50         60 
MWQIIFLTFG WDLVLASAYS NFRKSVDSTG RRQYQVQNGP CSYTFLLPET DSCRSSSSPY 

        70         80         90        100        110        120 
MSNAVQRDAP LDYDDSVQRL QVLENILENN TQWLMKLENY IQDNMKKEMV EIQQNVVQNQ 

       130        140        150        160        170        180 
TAVMIEIGTS LLNQTAAQTR KLTDVEAQVL NQTTRLELQL LQHSISTNKL EKQILDQTSE 

       190        200        210        220        230        240 
INKLQNKNSF LEQKVLDMEG KHSEQLQSMK EQKDELQVLV SKQSSVIDEL EKKLVTATVN 

       250        260        270        280        290        300 
NSLLQKQQHD LMETVNSLLT MMSSPNSKSS VAIRKEEQTT FRDCAEIFKS GLTTSGIYTL 

       310        320        330        340        350        360 
TFPNSTEEIK AYCDMDVGGG GWTVIQHRED GSVDFQRTWK EYKEGFGSPL GEYWLGNEFV 

       370        380        390        400        410        420 
SQLTGQHRYV LKIQLKDWEG NEAHSLYDHF YLAGEESNYR IHLTGLTGTA GKISSISQPG 

       430        440        450        460        470        480 
SDFSTKDSDN DKCICKCSQM LSGGWWFDAC GPSNLNGQYY PQKQNTNKFN GIKWYYWKGS 

       490 
GYSLKATTMM IRPADF 

« Hide

References

« Hide 'large scale' references
[1]"Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis."
Maisonpierre P.C., Suri C., Jones P.F., Bartunkova S., Wiegand S.J., Radziejewski C., Compton D.L., McClain J., Aldrich T.H., Papadopoulos N., Daly T.J., Davis S., Sato T.N., Yancopoulos G.D.
Science 277:55-60(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Uterus.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Head, Ovary, Spleen and Uterus.
[3]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004326 mRNA. Translation: AAB63189.1.
AK019860 mRNA. Translation: BAB31887.1.
AK048622 mRNA. Translation: BAC33396.1.
AK156132 mRNA. Translation: BAE33599.1.
BC027216 mRNA. Translation: AAH27216.1.
RefSeqNP_031452.2. NM_007426.4.
UniGeneMm.439874.

3D structure databases

ProteinModelPortalO35608.
SMRO35608. Positions 148-495.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6049N.
IntActO35608. 1 interaction.

PTM databases

PhosphoSiteO35608.

Proteomic databases

PRIDEO35608.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033846; ENSMUSP00000033846; ENSMUSG00000031465.
GeneID11601.
KEGGmmu:11601.
UCSCuc009kzu.1. mouse.

Organism-specific databases

CTD285.
MGIMGI:1202890. Angpt2.

Phylogenomic databases

eggNOGNOG298026.
GeneTreeENSGT00720000108441.
HOGENOMHOG000037128.
HOVERGENHBG001644.
InParanoidO35608.
KOK05466.
OMAIKAYCDM.
OrthoDBEOG7X9G60.
PhylomeDBO35608.
TreeFamTF336658.

Gene expression databases

ArrayExpressO35608.
BgeeO35608.
CleanExMM_ANGPT2.
GenevestigatorO35608.

Family and domain databases

Gene3D3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR028844. Ang-2.
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]
PANTHERPTHR19143:SF33. PTHR19143:SF33. 1 hit.
PfamPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. SSF56496. 1 hit.
PROSITEPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279120.
PROO35608.
SOURCESearch...

Entry information

Entry nameANGP2_MOUSE
AccessionPrimary (citable) accession number: O35608
Secondary accession number(s): Q3U1A1, Q9D2D2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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