ANGP2_PIG
ID ANGP2_PIG Reviewed; 496 AA.
AC Q9BDY7;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Angiopoietin-2;
DE Short=ANG-2;
DE Flags: Precursor;
GN Name=ANGPT2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11230987; DOI=10.1016/s0008-6363(00)00295-9;
RA Kim I., Moon S.O., Han C.Y., Pak Y.K., Moon S.K., Kim J.J., Koh G.Y.;
RT "The angiopoietin-tie2 system in coronary artery endothelium prevents
RT oxidized low-density lipoprotein-induced apoptosis.";
RL Cardiovasc. Res. 49:872-881(2001).
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; AF233228; AAK14993.1; -; mRNA.
DR RefSeq; NP_998973.1; NM_213808.1.
DR AlphaFoldDB; Q9BDY7; -.
DR SMR; Q9BDY7; -.
DR STRING; 9823.ENSSSCP00000016694; -.
DR PaxDb; Q9BDY7; -.
DR GeneID; 396730; -.
DR KEGG; ssc:396730; -.
DR CTD; 285; -.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; Q9BDY7; -.
DR OrthoDB; 357340at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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: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..496
FT /note="Angiopoietin-2"
FT /id="PRO_0000009115"
FT DOMAIN 275..495
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 130..255
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 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
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"
SQ SEQUENCE 496 AA; 56911 MW; 33B02BE224FE6B9D CRC64;
MWQLVFFALS CDLVLAAAYN NFRKSMDSTG KRQYQVQHGP CSYTFLLPET DNCRSPSSSY
VSNAVQRDAP LDYDDSVRRL QVLENIMENN TQWLMKLESY IQDNMKKEMV EIQQNAVQNQ
TAVMIEIGTN LLNQTAEQTR KLTDVEAQVL NQTTRLELQL LEHSLSTNKL EKQILDQTSE
INKLQDKNSF LEKKVLDMED KHIVQLQSIK EEKDQLQVLV SKQNSIIEEL EKQLVTATVN
NSVLQKQQHD LMETVHNLLT MISTSNSAKH SLVAKEEQII FRDCAEAFKS GLTTSGTYTL
TFPNSTEETK AYCDMETGGG GWTVIQRRED GSVDFQRTWK EYKMGFGSPS GEHWLGNEFV
SQVTNQKRYV LKIHLRDWEG NEAYSLYEHF YLSSEEFNYR IHLKGLTGTA GKISSISQPG
NDFSTKDADN DKCICKCSQM LTGGWWFDAC GPSNLNGMYY PQRQNTNKFN GIKWYYWKGS
GYSLKATTMM IRPADF
