ID   TIE1_BOVIN              Reviewed;        1136 AA.
AC   Q06805;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Tyrosine-protein kinase receptor Tie-1;
DE            EC=2.7.10.1;
DE   Flags: Precursor;
GN   Name=TIE1; Synonyms=TIE, TIE-1;
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 [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Endothelial cell;
RX   PubMed=8415706; DOI=10.1073/pnas.90.20.9355;
RA   Sato T.N., Qin Y., Kozak C.A., Andus K.L.;
RT   "Tie-1 and tie-2 define another class of putative receptor tyrosine kinase
RT   genes expressed in early embryonic vascular system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:9355-9358(1993).
CC   -!- FUNCTION: Transmembrane tyrosine-protein kinase that may modulate
CC       TEK/TIE2 activity and contribute to the regulation of angiogenesis.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBUNIT: Heterodimer with TEK/TIE2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in developing vascular
CC       endothelial cells. {ECO:0000269|PubMed:8415706}.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to ANGPT1, most
CC       likely by TEK/TIE2. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Tie subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; X71423; CAA50554.1; -; mRNA.
DR   PIR; S57845; S57845.
DR   RefSeq; NP_776390.1; NM_173965.2.
DR   AlphaFoldDB; Q06805; -.
DR   SMR; Q06805; -.
DR   STRING; 9913.ENSBTAP00000004917; -.
DR   PaxDb; Q06805; -.
DR   PRIDE; Q06805; -.
DR   GeneID; 280941; -.
DR   KEGG; bta:280941; -.
DR   CTD; 7075; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   InParanoid; Q06805; -.
DR   OrthoDB; 707342at2759; -.
DR   BRENDA; 2.7.10.1; 908.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
DR   GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd00063; FN3; 3.
DR   Gene3D; 2.60.40.10; -; 5.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   2: Evidence at transcript level;
KW   Angiogenesis; ATP-binding; Cell membrane; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL          1..23
FT   CHAIN           24..1136
FT                   /note="Tyrosine-protein kinase receptor Tie-1"
FT                   /id="PRO_0000024470"
FT   TOPO_DOM        24..757
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        758..782
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        783..1136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..106
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          212..254
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          256..301
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          303..343
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          370..424
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          444..543
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          546..640
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          644..737
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          837..1116
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        977
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         843..851
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         868
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1005
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        707
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        226..235
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        229..242
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        244..253
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        317..325
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        319..331
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        333..342
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1136 AA;  124953 MW;  EFF85804A041BB12 CRC64;
     MVWLEPPLLL PIFFLASHVG AAVDLTLLAD LRLTEPQRFF LTCVSGEAGA GRGSDAWGPP
     LLLEKDDRIV RTPRPWQPPH IARNGSSRVT VRGFSQPSDL VGVFSCVGGG GTRVLYVHNS
     PGAHLLPDKV THTVNKGDTA VLSARVRKEK QTDVIWKSNG SYFYTLDRHE AQDGQFLLQL
     PNVQPSSSGI YSATYLEASP LGSAFFRLIV RGCEAGRWGQ DCTKECPGCL HGGVCHDQDG
     ECVCPPGFTG TRCEQACREG RFGQSCQEQC PGTSGCRGLT FCLPDPYGCS CGSGWRGSQC
     QEACAPGRFG ADCHLQCQCQ NGGTCDRFSG CVCPSGWHGM HCEKSDRIPQ ILDMVSELEF
     NLDTMPRINC AAAGNPFPVR GSMELRKPDG TVLLSTKAIV EPDRTTAEFE VPRLALGDSG
     LWECRVSTSG GQDSRRFRIN VKVPPVPLTA PRLLAKQSRQ LVVSPLVSFS GDGPIASVRL
     HYRPQDSTMA WSTIVVDPSE NVTLMNLRPK TGYSVRVQLS RPGEGGEGAW GPPTLMTTDC
     PEPLLKPWLE GWHVEGPDRL RVSWSLPPVP GPLVGDGFLL RLWDGARGQE RRENVSSPQA
     RTALLTGLTP GTYYQLDVRL YHCTLLGPAS PAARVLLPPS GPPAPRHLHA QALSDSEIQL
     MWQRPEAAAG PISKYIVEVQ VAGGSGDPLW MDVDRPEETS TIVRGLNAST RYLFRVRASV
     QGPGDWSNVV EQSTLGNGLQ IEGPVQEIHA AEEGLDQQLV LAVVGSVSAT CLTILAALLT
     LACIRKSCLH RRRTFTYQSG SGEETILQFS SGTLTLTRRP KPQPEPLNYP VLEWEDITFE
     DLIGEGNFGQ VIRAMIKKDG LKMNAAIKML KEYASENDHR DFAGELEVLC KLGHHPNIIN
     LLGACENRGY LYIAIEYAPY GNLLDFLRKS RVLETDPAFA REHGTASTLS SRQLLRFASD
     AANGMQYLSE KQFIHRDLAA RNVLVGENLA SKIADFGLSR GEEVYVKKTM GRLPVRWMAI
     ESLNYSVYTT KSDVWSFGVL LWEIVSLGGT PYCGMTCAEL YEKLPQAYRM EQPRNCDDEV
     YELMRQCWRD RPYERPPFAQ IALQLGRMLE ARKAYVNMSL FENFTYAGID ATAEEA