ANGP2_CANLF
ID ANGP2_CANLF Reviewed; 495 AA.
AC A0A8J8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Angiopoietin-2;
DE Short=ANG-2;
DE Flags: Precursor;
GN Name=ANGPT2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16545849; DOI=10.1016/j.rvsc.2005.12.004;
RA Kato Y., Asano K., Mizutani I., Konno T., Sasaki Y., Kutara K., Teshima K.,
RA Edamura K., Kano R., Suzuki K., Shibuya H., Sato T., Hasegawa A.,
RA Tanaka S.;
RT "Gene expressions of canine angiopoietin-1 and -2 in normal tissues and
RT spontaneous tumours.";
RL Res. Vet. Sci. 81:280-286(2006).
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 -!- DOMAIN: The Fibrinogen C-terminal domain mediates interaction with the
CC TEK/TIE2 receptor. {ECO:0000250}.
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DR EMBL; AB256019; BAE93229.1; -; mRNA.
DR RefSeq; NP_001041591.1; NM_001048126.1.
DR AlphaFoldDB; A0A8J8; -.
DR SMR; A0A8J8; -.
DR STRING; 9615.ENSCAFP00000012670; -.
DR PaxDb; A0A8J8; -.
DR Ensembl; ENSCAFT00030016221; ENSCAFP00030014161; ENSCAFG00030008722.
DR Ensembl; ENSCAFT00040015200; ENSCAFP00040013168; ENSCAFG00040008101.
DR Ensembl; ENSCAFT00845039859; ENSCAFP00845031217; ENSCAFG00845022531.
DR GeneID; 607616; -.
DR KEGG; cfa:607616; -.
DR CTD; 285; -.
DR VEuPathDB; HostDB:ENSCAFG00845022531; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158430; -.
DR HOGENOM; CLU_038628_3_1_1; -.
DR InParanoid; A0A8J8; -.
DR OMA; KIQLKDW; -.
DR OrthoDB; 357340at2759; -.
DR TreeFam; TF336658; -.
DR Reactome; R-CFA-210993; Tie2 Signaling.
DR Proteomes; UP000002254; Chromosome 16.
DR Bgee; ENSCAFG00000008597; Expressed in placenta and 49 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
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; IBA:GO_Central.
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..495
FT /note="Angiopoietin-2"
FT /id="PRO_0000278835"
FT DOMAIN 274..494
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 165..247
FT /evidence="ECO:0000255"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15123"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15123"
FT BINDING 432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15123"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15123"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 283..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 432..434
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 436..449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 495 AA; 57012 MW; 8EA314E75FE2AA30 CRC64;
MWQIVFFTLS CDLVRAAAYN NFRRSMDSIG RRQYQVQHGS CSYTFLLPET DNCRSPGSYV
PNAVQRDAPL DYDDSVQRLQ VLENIMENNT QWLIKLENYI QDNMKKEMVE MQQNAVQNQT
AVMIEIGTNL LNQTAEQTRK LTDVEAQVLN QTTRLELQLL EHSLSTNKLE KQILDQTSEI
NKLQDKNSFL EKKVLDMEDK HIVQLRSIKE EKDQLQVLVS KQNSIIEELE KQLVTATVNN
SVLQKQQHDL METVHSLLTM ISPSKSPKDT FVAKEEQIIY RDCAEVFKSG LTTNGIYTLT
FPNSTEEIKA YCDMETSGGG WTVIQRREDG SVDFQRTWKE YKVGFGNPSG EHWLGNEFVF
QVTNQQPYVL KIHLKDWEGN EAYSLYEHFY LSGEELNYRI HLKGLTGTAG KISSISQPGN
DFSTKDADND KCICKCSQML TGGWWFDACG PSNLNGMYYP QRQNTNKFNG IKWYYWKGSG
YSLKGTTMMI RPADF
