ANGP1_BOVIN
ID ANGP1_BOVIN Reviewed; 497 AA.
AC O18920; Q08DP8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Angiopoietin-1;
DE Short=ANG-1;
DE Flags: Precursor;
GN Name=ANGPT1; Synonyms=ANG1;
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 (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-481.
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 91-200.
RC TISSUE=Liver;
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: Found to be expressed throughout the ovarian
CC cycle.
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DR EMBL; BC123628; AAI23629.1; -; mRNA.
DR EMBL; AF093573; AAC61872.1; -; mRNA.
DR EMBL; AF032923; AAC78245.1; -; mRNA.
DR RefSeq; NP_001070265.1; NM_001076797.1.
DR AlphaFoldDB; O18920; -.
DR SMR; O18920; -.
DR STRING; 9913.ENSBTAP00000018675; -.
DR Ensembl; ENSBTAT00000018675; ENSBTAP00000018675; ENSBTAG00000014051.
DR GeneID; 282140; -.
DR KEGG; bta:282140; -.
DR CTD; 284; -.
DR VEuPathDB; HostDB:ENSBTAG00000014051; -.
DR VGNC; VGNC:53848; ANGPT1.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158117; -.
DR InParanoid; O18920; -.
DR OMA; QAFSQYD; -.
DR OrthoDB; 357340at2759; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000014051; Expressed in adenohypophysis and 91 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0050918; P:positive chemotaxis; IEA:Ensembl.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IEA:Ensembl.
DR GO; GO:0002040; P:sprouting angiogenesis; 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; 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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..497
FT /note="Angiopoietin-1"
FT /id="PRO_0000009109"
FT DOMAIN 276..496
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
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 276..277
FT /note="KE -> RK (in Ref. 2; AAC61872)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="N -> D (in Ref. 2; AAC61872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 57429 MW; 083AD44D7EC81002 CRC64;
MTVFLSFAFL AAILTHIGCS NQRRSPENGG RRYNRIQHGQ CAYTFILPEH DGNCRESTTD
QYNTNALQRD APHVEQDFSS QKLQHLEHVM ENYTQWLQKI ENYIVENMKS EMAQIQQNAV
QNHTATMLEI GTSLLSQTAE QTRKLTDVET QVLNQTSRLE IQLLENSLST YKLEKQLLQQ
TNEILKIHEK NSLLEHKIFE MEGKHKEELD TLKEEKENLQ GLVTRQTYII QELEKQLNRA
TTNNSVLQKQ QLELMDTVHN LVNLCTKEVL LKGGKKEEEK PFRDCADVYQ AGFNKSGIYT
IYINNMPEPK KVFCNMDLNG GGWTVIQHRE DGSLDFQRGW KEYKMGFGNP SGEYWLGNEF
IFAITSQRQY TLRIELLDWE GNRAYSQYDR FHIGNEKQNY RLYLKGHTGT AGKQSSLILH
GADFSTKDAD NDNCMCKCAL MLTGGWWFDA CGPSNLNGMF YTAGQNHGKL NGIKWHYFKG
PSYSLRSTTM MIRPLDF
