ID   ANGP1_CANLF             Reviewed;         497 AA.
AC   Q60FC1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Angiopoietin-1;
DE            Short=ANG-1;
DE   Flags: Precursor;
GN   Name=ANGPT1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16545849; DOI=10.1016/j.rvsc.2005.12.004;
RA   Kato Y., Asano K., Mizutani I., Konno T., Sasaki Y., Kutara K., Teshima K.,
RA   Edamura K., Kano R., Suzuki K., Shibuya H., Sato T., Hasegawa A.,
RA   Tanaka S.;
RT   "Gene expressions of canine angiopoietin-1 and -2 in normal tissues and
RT   spontaneous tumours.";
RL   Res. Vet. Sci. 81:280-286(2006).
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; AB192412; BAD54826.1; -; mRNA.
DR   RefSeq; NP_001005754.1; NM_001005754.2.
DR   AlphaFoldDB; Q60FC1; -.
DR   SMR; Q60FC1; -.
DR   STRING; 9615.ENSCAFP00000066685; -.
DR   PaxDb; Q60FC1; -.
DR   GeneID; 403656; -.
DR   KEGG; cfa:403656; -.
DR   CTD; 284; -.
DR   eggNOG; KOG2579; Eukaryota.
DR   InParanoid; Q60FC1; -.
DR   OrthoDB; 357340at2759; -.
DR   Proteomes; UP000002254; 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..497
FT                   /note="Angiopoietin-1"
FT                   /id="PRO_0000041839"
FT   DOMAIN          276..496
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   COILED          158..256
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"
SQ   SEQUENCE   497 AA;  57415 MW;  061AFC2B03E8F081 CRC64;
     MTVFLSFAFL AAILTHIGCS NQRRSPENGG RRYNRIQHGQ CAYTFILPEH DGNCRESTTD
     QYNTNALQRD APHVGPDFSS QKLQHLEHVM ENYTQWLQKI ENYIVENMKS EMAQIQQNAV
     QNHTATMLEI GTSLLSQTAE QTRKLTDVET QVLNQTSRLE IQLLENSLST YKLEKQLLQQ
     TNEILKIHEK NSLLEHKILE MEGKHKEEWD TLKEERENLQ VLVTRQTYII QELEKQLNRA
     TNNNSVLQKQ QLELMDTVHN LVNLCTKEVL LKGGKKEEEK PFRDCADVYQ AGFNKSGIYT
     IYINNMPEPK KVFCNMDVNG GGWTVIQHRE DGSLDFQRGW KEYKMGFGNP SGEYWLGNEF
     IFAITSQRQY TLRIELMDCE GNRAYSQYDR FHIGNEKQNY RLYLKCHTGT AGKQSSLILH
     GADFSTKDAD NDNCMCKCAL MLTGGWWFDA CGPSNLNGMF YTAGQNHGKL NGIKWHYFKG
     PSYSLRSTTM MIRPLDF