ANGP1_RAT
ID ANGP1_RAT Reviewed; 497 AA.
AC O35460; Q8K4Q4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Angiopoietin-1;
DE Short=ANG-1;
DE Flags: Precursor;
GN Name=Angpt1;
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 [MRNA].
RC STRAIN=Wistar; TISSUE=Placenta;
RX PubMed=12458684; DOI=10.1023/a:1020921818105;
RA Iizasa H., Bae S.H., Asashima T., Kitano T., Matsunaga N., Terasaki T.,
RA Kang Y.S., Nakashima E.;
RT "Augmented expression of the tight junction protein occludin in brain
RT endothelial cell line TR-bBB by rat angiopoietin-1 expressed in
RT baculovirus-infected sf plus insect cells.";
RL Pharm. Res. 19:1757-1760(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 91-200.
RC STRAIN=Sprague-Dawley; TISSUE=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 and activates TIE2 receptor by inducing its tyrosine
CC phosphorylation. Implicated in endothelial developmental processes
CC later and distinct from that of VEGF. Appears to play a crucial role in
CC mediating reciprocal interactions between the endothelium and
CC surrounding matrix and mesenchyme. Mediates blood vessel
CC maturation/stability. It may play an important role in the heart early
CC development.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; AB080023; BAC10290.1; -; mRNA.
DR EMBL; AF030376; AAC78246.1; -; mRNA.
DR RefSeq; NP_445998.1; NM_053546.1.
DR AlphaFoldDB; O35460; -.
DR SMR; O35460; -.
DR STRING; 10116.ENSRNOP00000007979; -.
DR GlyGen; O35460; 5 sites.
DR iPTMnet; O35460; -.
DR PhosphoSitePlus; O35460; -.
DR PaxDb; O35460; -.
DR GeneID; 89807; -.
DR KEGG; rno:89807; -.
DR UCSC; RGD:628896; rat.
DR CTD; 284; -.
DR RGD; 628896; Angpt1.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; O35460; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; O35460; -.
DR Reactome; R-RNO-210993; Tie2 Signaling.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR PRO; PR:O35460; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:RGD.
DR GO; GO:0072012; P:glomerulus vasculature development; IMP:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0030210; P:heparin biosynthetic process; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:RGD.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; ISO:RGD.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0043116; P:negative regulation of vascular permeability; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IMP:RGD.
DR GO; GO:0050918; P:positive chemotaxis; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:2000446; P:regulation of macrophage migration inhibitory factor signaling pathway; ISO:RGD.
DR GO; GO:0043393; P:regulation of protein binding; ISO:RGD.
DR GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; ISO:RGD.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0033552; P:response to vitamin B3; IEP:RGD.
DR GO; GO:0002040; P:sprouting angiogenesis; ISO:RGD.
DR GO; GO:0048014; P:Tie signaling pathway; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:RGD.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR028843; Ang-1.
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:SF156; PTHR19143:SF156; 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; Coiled coil; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..497
FT /note="Angiopoietin-1"
FT /id="PRO_0000009112"
FT DOMAIN 276..496
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 81..119
FT /evidence="ECO:0000255"
FT COILED 153..261
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 285..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 438..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CONFLICT 98
FT /note="Q -> E (in Ref. 2; AAC78246)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="E -> K (in Ref. 2; AAC78246)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="E -> K (in Ref. 2; AAC78246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 57461 MW; 08E66AEBEFD868AE CRC64;
MTVFLSFAFF AAILTHIGCS NQRRSPENGG RRYNRIQHGQ CAYTFILPEH DGNCRESATE
QYNTNALQRD APHVETDFSS QKLQHLEHVM ENYTQWLQKL ENYIVENMKS EMAQIQQNAV
QNHTATMLEI GTSLLSQTAE QTRKLTDVET QVLNQTSRLE IQLLENSLST YELEKQLLQQ
TNEILKIQEK NSLLEHKILE MEGKHKEELD TLKEEKENLQ GLVTRQTFII QELEKQLSRA
TSNNSVLQKQ QLELMDTVHN LVSLCTKEVL LKGGKREEEK PFRDCADVYQ AGFNKSGIYT
IYFNNMPEPK KVFCNMDVNE GGWTVIQHRE DGSLDFQRGW KEYKMGFGNP SGEYWLGNEF
IFAITSQRQY MLRIELMDWE GNRAYSQYDR FHIGNQKQNY RLYLKGHTGT AGKQSSLILH
GADFSTKDAD NDNCMCKCAL MLTGGWWFDA CGPSNLNGMF YTAGQNHGKL NGIKWHYFKG
PSYSLRSTTM MIRPLDF
