ID   TIE1_HUMAN              Reviewed;        1138 AA.
AC   P35590; B5A949; B5A950;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   24-JAN-2024, entry version 216.
DE   RecName: Full=Tyrosine-protein kinase receptor Tie-1;
DE            EC=2.7.10.1;
DE   Flags: Precursor;
GN   Name=TIE1; Synonyms=TIE;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1312667; DOI=10.1128/mcb.12.4.1698-1707.1992;
RA   Partanen J., Armstrong E., Maekelae T.P., Korhonen J., Sandberg M.,
RA   Renkonen R., Knuutila S., Huebner K., Alitalo K.;
RT   "A novel endothelial cell surface receptor tyrosine kinase with
RT   extracellular epidermal growth factor homology domains.";
RL   Mol. Cell. Biol. 12:1698-1707(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Partanen J.M.;
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND ALTERNATIVE SPLICING.
RX   PubMed=18593464; DOI=10.1186/ar2447;
RA   Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
RA   Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
RT   "Novel splice variants derived from the receptor tyrosine kinase
RT   superfamily are potential therapeutics for rheumatoid arthritis.";
RL   Arthritis Res. Ther. 10:R73-R73(2008).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 22-36.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [7]
RP   INTERACTION WITH TEK, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=15851516; DOI=10.1083/jcb.200411105;
RA   Saharinen P., Kerkela K., Ekman N., Marron M., Brindle N., Lee G.M.,
RA   Augustin H., Koh G.Y., Alitalo K.;
RT   "Multiple angiopoietin recombinant proteins activate the Tie1 receptor
RT   tyrosine kinase and promote its interaction with Tie2.";
RL   J. Cell Biol. 169:239-243(2005).
RN   [8]
RP   FUNCTION, INTERACTION WITH TEK, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=20227369; DOI=10.1016/j.molcel.2010.02.007;
RA   Seegar T.C., Eller B., Tzvetkova-Robev D., Kolev M.V., Henderson S.C.,
RA   Nikolov D.B., Barton W.A.;
RT   "Tie1-Tie2 interactions mediate functional differences between angiopoietin
RT   ligands.";
RL   Mol. Cell 37:643-655(2010).
RN   [9]
RP   INTERACTION WITH SVEP1.
RX   PubMed=37097004; DOI=10.7554/elife.82969;
RA   Hussmann M., Schulte D., Weischer S., Carlantoni C., Nakajima H.,
RA   Mochizuki N., Stainier D.Y.R., Zobel T., Koch M., Schulte-Merker S.;
RT   "Svep1 is a binding ligand of Tie1 and affects specific aspects of facial
RT   lymphatic development in a Vegfc-independent manner.";
RL   Elife 12:0-0(2023).
RN   [10]
RP   VARIANTS [LARGE SCALE ANALYSIS] MET-448; VAL-1104 AND HIS-1109.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [11]
RP   VARIANTS LMPHM11 CYS-481; LYS-1061 AND HIS-1109, AND INVOLVEMENT IN
RP   LMPHM11.
RX   PubMed=32947856; DOI=10.3390/ijms21186780;
RA   Michelini S., Ricci M., Veselenyiova D., Kenanoglu S., Kurti D.,
RA   Baglivo M., Fiorentino A., Basha S.H., Priya S., Serrani R., Krajcovic J.,
RA   Dundar M., Dautaj A., Bertelli M.;
RT   "TIE1 as a Candidate Gene for Lymphatic Malformations with or without
RT   Lymphedema.";
RL   Int. J. Mol. Sci. 21:0-0(2020).
CC   -!- FUNCTION: Transmembrane tyrosine-protein kinase that may modulate
CC       TEK/TIE2 activity and contribute to the regulation of angiogenesis.
CC       {ECO:0000269|PubMed:20227369}.
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 (PubMed:20227369). Interacts with
CC       SVEP1 (via C-terminus) (PubMed:37097004). {ECO:0000269|PubMed:20227369,
CC       ECO:0000269|PubMed:37097004}.
CC   -!- INTERACTION:
CC       P35590; Q6A162: KRT40; NbExp=3; IntAct=EBI-2256865, EBI-10171697;
CC       P35590; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2256865, EBI-10171774;
CC       P35590; Q15238: PSG5; NbExp=3; IntAct=EBI-2256865, EBI-4314891;
CC       P35590; Q93062: RBPMS; NbExp=3; IntAct=EBI-2256865, EBI-740322;
CC       P35590; Q15654: TRIP6; NbExp=3; IntAct=EBI-2256865, EBI-742327;
CC       P35590; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2256865, EBI-527853;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15851516,
CC       ECO:0000269|PubMed:20227369}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:15851516, ECO:0000269|PubMed:20227369}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P35590-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35590-2; Sequence=VSP_047609, VSP_047610;
CC       Name=3;
CC         IsoId=P35590-3; Sequence=VSP_047607, VSP_047608;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in developing vascular
CC       endothelial cells. {ECO:0000269|PubMed:20227369}.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to ANGPT1, most
CC       likely by TEK/TIE2. {ECO:0000269|PubMed:15851516}.
CC   -!- DISEASE: Lymphatic malformation 11 (LMPHM11) [MIM:619401]: A form of
CC       primary lymphedema, a disease characterized by swelling of body parts
CC       due to developmental anomalies and functional defects of the lymphatic
CC       system. Patients with lymphedema may suffer from recurrent local
CC       infections. LMPHM11 is an autosomal dominant form characterized by
CC       onset of lower extremity edema in the second or third decade of life.
CC       Some affected individuals may have subclinical lymphatic malformations.
CC       {ECO:0000269|PubMed:32947856}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Tie subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42560/TIE1";
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DR   EMBL; X60957; CAA43290.1; -; mRNA.
DR   EMBL; EU826587; ACF47623.1; -; mRNA.
DR   EMBL; EU826588; ACF47624.1; -; mRNA.
DR   EMBL; AC093420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC038239; AAH38239.1; -; mRNA.
DR   CCDS; CCDS482.1; -. [P35590-1]
DR   RefSeq; NP_005415.1; NM_005424.4. [P35590-1]
DR   PDB; 5N06; X-ray; 2.50 A; A/B=642-738.
DR   PDBsum; 5N06; -.
DR   AlphaFoldDB; P35590; -.
DR   SMR; P35590; -.
DR   BioGRID; 112931; 15.
DR   IntAct; P35590; 31.
DR   MINT; P35590; -.
DR   STRING; 9606.ENSP00000361554; -.
DR   BindingDB; P35590; -.
DR   ChEMBL; CHEMBL5274; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; P35590; -.
DR   GuidetoPHARMACOLOGY; 1841; -.
DR   GlyCosmos; P35590; 5 sites, No reported glycans.
DR   GlyGen; P35590; 6 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P35590; -.
DR   PhosphoSitePlus; P35590; -.
DR   BioMuta; TIE1; -.
DR   DMDM; 549081; -.
DR   MassIVE; P35590; -.
DR   PaxDb; 9606-ENSP00000361554; -.
DR   PeptideAtlas; P35590; -.
DR   ProteomicsDB; 55098; -. [P35590-1]
DR   ProteomicsDB; 5928; -.
DR   ProteomicsDB; 5929; -.
DR   Antibodypedia; 32289; 776 antibodies from 39 providers.
DR   DNASU; 7075; -.
DR   Ensembl; ENST00000372476.8; ENSP00000361554.3; ENSG00000066056.14. [P35590-1]
DR   Ensembl; ENST00000538015.1; ENSP00000440063.1; ENSG00000066056.14. [P35590-2]
DR   GeneID; 7075; -.
DR   KEGG; hsa:7075; -.
DR   MANE-Select; ENST00000372476.8; ENSP00000361554.3; NM_005424.5; NP_005415.1.
DR   UCSC; uc001ciu.4; human. [P35590-1]
DR   AGR; HGNC:11809; -.
DR   CTD; 7075; -.
DR   DisGeNET; 7075; -.
DR   GeneCards; TIE1; -.
DR   HGNC; HGNC:11809; TIE1.
DR   HPA; ENSG00000066056; Low tissue specificity.
DR   MalaCards; TIE1; -.
DR   MIM; 600222; gene.
DR   MIM; 619401; phenotype.
DR   neXtProt; NX_P35590; -.
DR   OpenTargets; ENSG00000066056; -.
DR   PharmGKB; PA36516; -.
DR   VEuPathDB; HostDB:ENSG00000066056; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   GeneTree; ENSGT00940000157693; -.
DR   HOGENOM; CLU_008888_0_0_1; -.
DR   InParanoid; P35590; -.
DR   OMA; AKVWWRL; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; P35590; -.
DR   TreeFam; TF317568; -.
DR   BRENDA; 2.7.10.1; 2681.
DR   PathwayCommons; P35590; -.
DR   SignaLink; P35590; -.
DR   SIGNOR; P35590; -.
DR   BioGRID-ORCS; 7075; 20 hits in 1182 CRISPR screens.
DR   ChiTaRS; TIE1; human.
DR   GenomeRNAi; 7075; -.
DR   Pharos; P35590; Tchem.
DR   PRO; PR:P35590; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P35590; Protein.
DR   Bgee; ENSG00000066056; Expressed in omental fat pad and 148 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
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:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060854; P:branching involved in lymph vessel morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0060836; P:lymphatic endothelial cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045026; P:plasma membrane fusion; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
DR   GO; GO:0001936; P:regulation of endothelial cell proliferation; ISS:BHF-UCL.
DR   GO; GO:1901201; P:regulation of extracellular matrix assembly; ISS:BHF-UCL.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0048771; P:tissue remodeling; ISS:BHF-UCL.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
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; 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.
DR   Genevisible; P35590; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Angiogenesis; ATP-binding;
KW   Cell membrane; Direct protein sequencing; 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..21
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           22..1138
FT                   /note="Tyrosine-protein kinase receptor Tie-1"
FT                   /id="PRO_0000024471"
FT   TOPO_DOM        22..759
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        760..784
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        785..1138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..105
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          214..256
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          258..303
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          305..345
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          372..426
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          446..545
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          548..642
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          646..739
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          839..1118
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        979
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         845..853
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         870
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1007
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        596
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        709
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        228..237
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        231..244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        246..255
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        315..327
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        321..333
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        335..344
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VAR_SEQ         305..317
FT                   /note="ACAPGHFGADCRL -> VHQGHCGAREDHS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:18593464"
FT                   /id="VSP_047607"
FT   VAR_SEQ         318..1138
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:18593464"
FT                   /id="VSP_047608"
FT   VAR_SEQ         348..379
FT                   /note="DRIPQILNMASELEFNLETMPRINCAAAGNPF -> GWRDWVDTSTEKQNTD
FT                   EGRFGGHVSAPVGAPG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:18593464"
FT                   /id="VSP_047609"
FT   VAR_SEQ         380..1138
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:18593464"
FT                   /id="VSP_047610"
FT   VARIANT         448
FT                   /note="V -> M (in dbSNP:rs56302794)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041852"
FT   VARIANT         481
FT                   /note="R -> C (in LMPHM11; uncertain significance;
FT                   dbSNP:rs139244400)"
FT                   /evidence="ECO:0000269|PubMed:32947856"
FT                   /id="VAR_085888"
FT   VARIANT         1061
FT                   /note="E -> K (in LMPHM11; uncertain significance;
FT                   dbSNP:rs760492428)"
FT                   /evidence="ECO:0000269|PubMed:32947856"
FT                   /id="VAR_085889"
FT   VARIANT         1104
FT                   /note="A -> V (in dbSNP:rs35573981)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041853"
FT   VARIANT         1109
FT                   /note="R -> H (in LMPHM11; uncertain significance;
FT                   dbSNP:rs34993202)"
FT                   /evidence="ECO:0000269|PubMed:17344846,
FT                   ECO:0000269|PubMed:32947856"
FT                   /id="VAR_041854"
FT   STRAND          648..656
FT                   /evidence="ECO:0007829|PDB:5N06"
FT   STRAND          659..665
FT                   /evidence="ECO:0007829|PDB:5N06"
FT   STRAND          676..682
FT                   /evidence="ECO:0007829|PDB:5N06"
FT   STRAND          691..695
FT                   /evidence="ECO:0007829|PDB:5N06"
FT   STRAND          701..707
FT                   /evidence="ECO:0007829|PDB:5N06"
FT   STRAND          714..728
FT                   /evidence="ECO:0007829|PDB:5N06"
SQ   SEQUENCE   1138 AA;  125090 MW;  3B42BE33678C58A1 CRC64;
     MVWRVPPFLL PILFLASHVG AAVDLTLLAN LRLTDPQRFF LTCVSGEAGA GRGSDAWGPP
     LLLEKDDRIV RTPPGPPLRL ARNGSHQVTL RGFSKPSDLV GVFSCVGGAG ARRTRVIYVH
     NSPGAHLLPD KVTHTVNKGD TAVLSARVHK EKQTDVIWKS NGSYFYTLDW HEAQDGRFLL
     QLPNVQPPSS GIYSATYLEA SPLGSAFFRL IVRGCGAGRW GPGCTKECPG CLHGGVCHDH
     DGECVCPPGF TGTRCEQACR EGRFGQSCQE QCPGISGCRG LTFCLPDPYG CSCGSGWRGS
     QCQEACAPGH FGADCRLQCQ CQNGGTCDRF SGCVCPSGWH GVHCEKSDRI PQILNMASEL
     EFNLETMPRI NCAAAGNPFP VRGSIELRKP DGTVLLSTKA IVEPEKTTAE FEVPRLVLAD
     SGFWECRVST SGGQDSRRFK VNVKVPPVPL AAPRLLTKQS RQLVVSPLVS FSGDGPISTV
     RLHYRPQDST MDWSTIVVDP SENVTLMNLR PKTGYSVRVQ LSRPGEGGEG AWGPPTLMTT
     DCPEPLLQPW LEGWHVEGTD RLRVSWSLPL VPGPLVGDGF LLRLWDGTRG QERRENVSSP
     QARTALLTGL TPGTHYQLDV QLYHCTLLGP ASPPAHVLLP PSGPPAPRHL HAQALSDSEI
     QLTWKHPEAL PGPISKYVVE VQVAGGAGDP LWIDVDRPEE TSTIIRGLNA STRYLFRMRA
     SIQGLGDWSN TVEESTLGNG LQAEGPVQES RAAEEGLDQQ LILAVVGSVS ATCLTILAAL
     LTLVCIRRSC LHRRRTFTYQ SGSGEETILQ FSSGTLTLTR RPKLQPEPLS YPVLEWEDIT
     FEDLIGEGNF GQVIRAMIKK DGLKMNAAIK MLKEYASEND HRDFAGELEV LCKLGHHPNI
     INLLGACKNR GYLYIAIEYA PYGNLLDFLR KSRVLETDPA FAREHGTAST LSSRQLLRFA
     SDAANGMQYL SEKQFIHRDL AARNVLVGEN LASKIADFGL SRGEEVYVKK TMGRLPVRWM
     AIESLNYSVY TTKSDVWSFG VLLWEIVSLG GTPYCGMTCA ELYEKLPQGY RMEQPRNCDD
     EVYELMRQCW RDRPYERPPF AQIALQLGRM LEARKAYVNM SLFENFTYAG IDATAEEA
//