ID   ANGP1_PIG               Reviewed;         498 AA.
AC   Q9BDY8;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Angiopoietin-1;
DE            Short=ANG-1;
DE   Flags: Precursor;
GN   Name=ANGPT1;
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 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 {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
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DR   EMBL; AF233227; AAK14992.1; -; mRNA.
DR   RefSeq; NP_999124.1; NM_213959.1.
DR   AlphaFoldDB; Q9BDY8; -.
DR   SMR; Q9BDY8; -.
DR   STRING; 9823.ENSSSCP00000006448; -.
DR   PaxDb; Q9BDY8; -.
DR   PRIDE; Q9BDY8; -.
DR   GeneID; 397009; -.
DR   KEGG; ssc:397009; -.
DR   CTD; 284; -.
DR   eggNOG; KOG2579; Eukaryota.
DR   InParanoid; Q9BDY8; -.
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: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; 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..498
FT                   /note="Angiopoietin-1"
FT                   /id="PRO_0000278834"
FT   DOMAIN          277..497
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   COILED          158..254
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        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        286..315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        439..452
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ   SEQUENCE   498 AA;  57413 MW;  A8C1C8EF56061876 CRC64;
     MTVFLSFAFL AAILTHIGCS NQRRSPENGG RRYNRIQHGQ CAYTFILPEH DGNCRESTTD
     QYNTNALQRD APHVEQDFSS QKLQHLEHVM ENYTQWLQKI ENYIVENMKS EMAQIQQNAV
     QNHTATMLEI GTSLLSQTAE QTRKLTDVET QVLNQTSRLE IQLLENSLST YKLEKQLLQQ
     TNEILKIHEK NSLLEHKILE MEGKHKEELD TLKEEKENLQ GLVTRQTYII QELKKQLNRA
     TTNNSVLQKQ QLELMDTVHN LVNLCTKEGV LLKGGKKEEV KPFRDCADVY QAGFNKSGIY
     TIYINNMPEP KKVFCNMDLN GGGWTVIQHR EDGSLDFQRG WKEYKMGFGN PSGEYWLGNE
     FIFAITSQRQ YTLRTELMDW EGNRAYSQYD RFHIGNEKQN YRLYLKGHSG TAGKQSSLIL
     HGADFSTKDA DNDNCMCKCA LMLTGGWWFD ACGPSNLNGM FYTAGQNHGK LNGIKWHYFK
     GPSYSLRSTT MMIRPLDF