ID   ANGP4_BOVIN             Reviewed;         498 AA.
AC   Q24K15;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Angiopoietin-4;
DE            Short=ANG-4;
DE   Flags: Precursor;
GN   Name=ANGPT4;
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=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce
CC       tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell
CC       survival, migration and angiogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TEK/TIE2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; BC114033; AAI14034.1; -; mRNA.
DR   RefSeq; NP_001069951.1; NM_001076483.2.
DR   AlphaFoldDB; Q24K15; -.
DR   SMR; Q24K15; -.
DR   STRING; 9913.ENSBTAP00000029073; -.
DR   PaxDb; Q24K15; -.
DR   GeneID; 617915; -.
DR   KEGG; bta:617915; -.
DR   CTD; 51378; -.
DR   eggNOG; KOG2579; Eukaryota.
DR   InParanoid; Q24K15; -.
DR   OrthoDB; 357340at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 3.90.215.10; -; 1.
DR   InterPro; IPR028845; Ang-4.
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:SF31; PTHR19143:SF31; 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; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..498
FT                   /note="Angiopoietin-4"
FT                   /id="PRO_0000278836"
FT   DOMAIN          277..497
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          51..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          85..109
FT                   /evidence="ECO:0000255"
FT   COILED          186..254
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        65..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
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;  55929 MW;  7D40424BDFA166F4 CRC64;
     MPSPPAMLLG GLLLIVASTT VAQRRGQEAA GRRRAHRVQH GQCSYTFVLP EPEPCPPEPE
     AFGGSNSLQR DSPAATLNLG DWPSQRMRQL EKMLENNTQW LQKLERYIQV NLRLELAQAQ
     QHMVQNQTAT MLELGTSLLT QTTAQTRKLT DVEAQVLNQT SRMEIQLLET SLSTNKLEKQ
     LLLQGHELHR LQGHNSALET RVQALETQQQ AELASLSGEK ERLRRLLGRQ SGALAGLERT
     LRAASSNSSL LQRQQHQLLE SVQRLVRVMA QGPASMRAAD QLFQDCAEIQ RFGANASGIY
     TIHVANVTEP RKVFCDMEAS GGGWTLIQRR ENGSVNFQRN WKDYKQGFGN PAGEHWLGNE
     VVHQLTSRAT YSLRVELQDW EGNEAYAQYE HFQLGSEAQL YRLSLSGYSG SAGRQSSLVL
     QGTNFSTRDA DNDNCLCKCA QMLSGGWWFD ACGLSNLNGI YYPARHHVRK LNGIRWHYFQ
     GPSYSLRTTR MMVRPSGI