ANGP2_BOVIN
ID ANGP2_BOVIN Reviewed; 496 AA.
AC O77802; A5PKF7; Q9TSK0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Angiopoietin-2;
DE Short=ANG-2;
DE Flags: Precursor;
GN Name=ANGPT2; Synonyms=ANG2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-496.
RC TISSUE=Ovary;
RX PubMed=9840613;
RA Goede V., Schmidt T., Kimmina S., Kozian D., Augustin H.G.;
RT "Analysis of blood vessel maturation processes during cyclic ovarian
RT angiogenesis.";
RL Lab. Invest. 78:1385-1394(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 340-476.
RC TISSUE=Adrenal cortex;
RX PubMed=9776732; DOI=10.1161/01.res.83.8.852;
RA Mandriota S.J., Pepper M.S.;
RT "Regulation of angiopoietin-2 mRNA levels in bovine microvascular
RT endothelial cells by cytokines and hypoxia.";
RL Circ. Res. 83:852-859(1998).
CC -!- FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and
CC modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of
CC TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic
CC inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix
CC contacts may induce endothelial cell apoptosis with consequent vascular
CC regression. In concert with VEGF, it may facilitate endothelial cell
CC migration and proliferation, thus serving as a permissive angiogenic
CC signal. Involved in the regulation of lymphangiogenesis.
CC {ECO:0000250|UniProtKB:O15123}.
CC -!- SUBUNIT: Interacts with TEK/TIE2, competing for the same binding site
CC as ANGPT1. Interacts with ITGA5. {ECO:0000250|UniProtKB:O15123}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O15123}.
CC -!- DEVELOPMENTAL STAGE: Found to be expressed throughout the ovarian
CC cycle. Overexpressed during luteolysis, this could reflect the
CC regression of capillaries that had developed pericyte contact in the
CC midstage corpus luteum.
CC -!- DOMAIN: The Fibrinogen C-terminal domain mediates interaction with the
CC TEK/TIE2 receptor. {ECO:0000250}.
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DR EMBL; BC142471; AAI42472.1; -; mRNA.
DR EMBL; AF094699; AAC62490.1; -; mRNA.
DR EMBL; AF032924; AAC78285.1; -; mRNA.
DR RefSeq; NP_001092325.1; NM_001098855.1.
DR AlphaFoldDB; O77802; -.
DR SMR; O77802; -.
DR STRING; 9913.ENSBTAP00000014656; -.
DR PaxDb; O77802; -.
DR Ensembl; ENSBTAT00000014656; ENSBTAP00000014656; ENSBTAG00000011034.
DR GeneID; 282141; -.
DR KEGG; bta:282141; -.
DR CTD; 285; -.
DR VEuPathDB; HostDB:ENSBTAG00000011034; -.
DR VGNC; VGNC:25888; ANGPT2.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158430; -.
DR HOGENOM; CLU_038628_3_1_1; -.
DR InParanoid; O77802; -.
DR OMA; KIQLKDW; -.
DR OrthoDB; 357340at2759; -.
DR TreeFam; TF336658; -.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000011034; Expressed in thyroid gland and 105 other tissues.
DR ExpressionAtlas; O77802; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0050928; P:negative regulation of positive chemotaxis; IEA:Ensembl.
DR GO; GO:0048014; P:Tie signaling pathway; IEA:Ensembl.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR028844; Ang-2.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR19143:SF199; PTHR19143:SF199; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Calcium; Coiled coil; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..496
FT /note="Angiopoietin-2"
FT /id="PRO_0000099063"
FT DOMAIN 275..495
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 167..249
FT /evidence="ECO:0000255"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15123"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15123"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15123"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15123"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 284..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 433..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 437..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CONFLICT 393
FT /note="S -> L (in Ref. 3; AAC78285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 56539 MW; 3DC10D0246E89E95 CRC64;
MWQLVFLTLS CDLAVATAHS GSRKGMDIAA GKKQYQVQHG ACSYTFLLPE TDHCRSPSSA
YVPNAVQRDA PLDYDDSVQR LQVLENIMEN NTQWLMKLEN YIQDNMKKEM VEIQQNAVQN
QTAVMIEIGT NLLNQTAEQT RKLTDVEAQV LNQTTRLELQ LLEHSLSTNK LEKQILDQTS
EISKLQDKNS FLEKKVLDME DKHIVQLRSI KEEKDQLQVL VSKQNSIIEE LEKQLVTATV
NNSVLQKQQH DLMETVNNLL TLMSTSNPSY SLLAKDEQII FRDCGEAFKS GLTTSGVYTL
TFPNSTEEIK AYCDMETGGG GWTVIQRRED GSVDFQRTWK EYKVGFGNPS GEHWLGNEFV
SQVTGQKRYV LKIHLRDWEG NEAYSLYDHF YLSNEELNYR IHLKGLTGTA GKISSISQPG
NDFSTKDADN DKCICKCSQM LTGGWWFDAC GPSNLNGMYY PQRQNTNKFN GIKWYYWKGS
GYSLKATTMM IRPADF
