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Database: UniProt
Entry: A0A340Y4X3_LIPVE
LinkDB: A0A340Y4X3_LIPVE
Original site: A0A340Y4X3_LIPVE 
ID   A0A340Y4X3_LIPVE        Unreviewed;      1139 AA.
AC   A0A340Y4X3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=TIE1 {ECO:0000313|RefSeq:XP_007468293.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007468293.1};
RN   [1] {ECO:0000313|RefSeq:XP_007468293.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001171};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   RefSeq; XP_007468293.1; XM_007468231.1.
DR   AlphaFoldDB; A0A340Y4X3; -.
DR   STRING; 118797.A0A340Y4X3; -.
DR   GeneID; 103079731; -.
DR   KEGG; lve:103079731; -.
DR   CTD; 7075; -.
DR   InParanoid; A0A340Y4X3; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000265300; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd05089; PTKc_Tie1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   PANTHER; PTHR24416:SF341; TYROSINE-PROTEIN KINASE RECEPTOR TIE-1; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00047; ig; 2.
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; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 1.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000313|RefSeq:XP_007468293.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_007468293.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          226..257
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          317..346
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          447..544
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          546..643
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          647..740
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          840..1119
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         871
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        247..256
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        336..345
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1139 AA;  125202 MW;  BEFEA3DD4CFA050E CRC64;
     MVWLGPPLLL PIVFLASHVG AAVDLTLLAD LRLAEPQRFF LTCVSGEAGA GRGSDAWGSP
     LLLEKDDRIV RTPRPWQPLH LARNGSRQVT LRGFSQPSDL VGVFSCVGGA GARRARVLYV
     HNSPGAHLLP GKVTHTVNKG DTAVLSAWVR KEKQTDVIWK SNGSYFYTLD WHEAQEGRFL
     LQLPNVQPSS SGIYSATYLE ASPLGSAFFR LIVRGCEAGH WGQDCTKECP GCLHGGVCHD
     QDGECVCPPG FTGTRCEQAC REGRFGQSCQ EQCPGTSGCR GLTFCLPDPY GCSCGSGWRG
     SQCQEACAPG HFGADCHLQC QCQNGGTCDR FSGCVCPSGW HGVHCEKSDR IPQILDMVSE
     LEFNLETTPR INCAAAGNPF PVRGSVELRK PDGTVLLSTK AIVEPDRTTA EFEVPRLALG
     DSGLWECRVS TSGGQDSRRF RVNVKVPPVP LTAPRLLAKQ SRQLMVSPLV SFSGDGPIAS
     VRLHYRPQDS TMAWSTIVVD PSENVTLMNL RPKTGYSVRV QLSRPGEGGE GAWGPPTLMT
     TDCPEPLLQP WLEGWHVEGP DRLRVSWSLP SVPGPLVGDG FLLRLWDGAR GQERRENVSS
     PQARTALLTG LTPGTHYQLD VRLYHCTLLG PASPAARVLL PPSGPPAPRH LHAQALSDSE
     IQLVWQRPEA PAGPISKYIV EVQVAEGSGD PLWMDVDRPE ETSTVVRGLN ASTRYLFRVR
     ASVQGPGDWS DLVEESTLSN GLQSEGPVQE VQAAEEGLDQ QLVLAVVGSV SATCLTILAA
     LLTLACIRRS CLHRRRTFTY QSGSGEETIL QFSSGTLTLT RRPKPQPEPL NYPVLEWEDI
     TFEDLIGEGN FGQVIRAMIK KDGLKMNAAI KMLKEYASEN DHRDFAGELE VLCKLGHHPN
     IINLLGACEN RGYLYIAIEY APYGNLLDFL RKSRVLETDP AFAREHGTAS TLSSRQLLRF
     ASDAANGMQY LSEKQFIHRD LAARNVLVGE NLASKIADFG LSRGEEVYVK KTMGRLPVRW
     MAIESLNYSV YTTKSDVWSF GVLLWEIVSL GGTPYCGMTC AELYEKLPQG YRMEQPRNCD
     DEVYELMRQC WRDRPYERPP FAQIALQLGR MLEARKAYVN MSLFENFTYA GIDATAEEA
//
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