ANGP2_RAT
ID ANGP2_RAT Reviewed; 496 AA.
AC O35462; B1WBY0; Q548N5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Angiopoietin-2;
DE Short=ANG-2;
DE Flags: Precursor;
GN Name=Angpt2; Synonyms=Agpt2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 340-476.
RC STRAIN=Sprague-Dawley; TISSUE=Heart, and Placenta;
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 -!- DOMAIN: The Fibrinogen C-terminal domain mediates interaction with the
CC TEK/TIE2 receptor. {ECO:0000250}.
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DR EMBL; CH473970; EDM08957.1; -; Genomic_DNA.
DR EMBL; BC161931; AAI61931.1; -; mRNA.
DR EMBL; AF030378; AAC78247.1; -; mRNA.
DR EMBL; AF311728; AAG34114.1; -; mRNA.
DR RefSeq; NP_604449.1; NM_134454.1.
DR AlphaFoldDB; O35462; -.
DR SMR; O35462; -.
DR STRING; 10116.ENSRNOP00000022774; -.
DR GlyGen; O35462; 6 sites.
DR iPTMnet; O35462; -.
DR PhosphoSitePlus; O35462; -.
DR PaxDb; O35462; -.
DR PRIDE; O35462; -.
DR Ensembl; ENSRNOT00000022774; ENSRNOP00000022774; ENSRNOG00000016696.
DR GeneID; 89805; -.
DR KEGG; rno:89805; -.
DR UCSC; RGD:621861; rat.
DR CTD; 285; -.
DR RGD; 621861; Angpt2.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158430; -.
DR HOGENOM; CLU_038628_3_1_1; -.
DR InParanoid; O35462; -.
DR OMA; KIQLKDW; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; O35462; -.
DR TreeFam; TF336658; -.
DR Reactome; R-RNO-210993; Tie2 Signaling.
DR PRO; PR:O35462; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Proteomes; UP000234681; Chromosome 16.
DR Bgee; ENSRNOG00000016696; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; O35462; RN.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEP:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0007281; P:germ cell development; IEP:RGD.
DR GO; GO:0072012; P:glomerulus vasculature development; IMP:UniProtKB.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:RGD.
DR GO; GO:0050928; P:negative regulation of positive chemotaxis; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0048014; P:Tie signaling pathway; ISO:RGD.
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_0000099064"
FT DOMAIN 280..496
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 159..256
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; 56518 MW; C6F3532A89564C06 CRC64;
MWQIVFLTFG CDLVLASAYN NFRKSVDSTG RRQYQVQNGP CSYTFLLPET DSCRSSSSPY
MSNAVQRDAP LDYDDSVQRL QVLENILENN TQWLMKLENY IQDNMKKEMV EIQQNVVQNQ
TAVMIEIGTS LLNQTAAQTR KLTDVEAQVL NQTTRLELQL LQHSISTNKL EKQILDQTSE
INKLQDKNSF LEKKVLDMED KHSVQLQSMK EQKDQLQVLV SKQSSVIDEL EKKLVTATVN
NSVLQKQQHD LMETVNSLLT MMSSPDYKSS VAVPKEEKTT FRDCAEIFKS GLTTSGIYTL
TFPNSTEEVK AYCDMDMGGG GWTVIQHRED GSVDFQRTWK EYKEGFGSPL GEYWLGNEFV
SQLTSGHRYV LKIQLKDWEG SEAHSLYEHF YLSGEESNYR IHLTGLTGTA GKISSISQPG
SDFSTKDSDN DKCICKCSQM LTGGWWFDAC GPSNLNGQYY PQKQNTNKFN GIKWYYWKGS
GYSLKATTMM IRPADF
