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Endothelial-specific receptor tyrosine kinase (TEK receptor tyrosine kinase)

 D3ZCD0_RAT              Unreviewed;      1120 AA.
D3ZCD0;
20-APR-2010, integrated into UniProtKB/TrEMBL.
20-APR-2010, sequence version 1.
22-NOV-2017, entry version 79.
SubName: Full=Endothelial-specific receptor tyrosine kinase {ECO:0000313|EMBL:EDL97760.1};
SubName: Full=TEK receptor tyrosine kinase {ECO:0000313|Ensembl:ENSRNOP00000036086};
Name=Tek {ECO:0000313|EMBL:EDL97760.1,
ECO:0000313|Ensembl:ENSRNOP00000036086, ECO:0000313|RGD:620980};
ORFNames=rCG_53516 {ECO:0000313|EMBL:EDL97760.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000036086, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000036086, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000036086,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|EMBL:EDL97760.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL97760.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[3] {ECO:0000313|EMBL:EDL97760.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL97760.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|Ensembl:ENSRNOP00000036086}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000036086};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000256|SAAS:SAAS00701269}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000256|SAAS:SAAS00941529}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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EMBL; AABR07049285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07049286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07073130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC133043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473998; EDL97760.1; -; Genomic_DNA.
RefSeq; NP_001099207.1; NM_001105737.1.
UniGene; Rn.9159; -.
STRING; 10116.ENSRNOP00000036086; -.
Ensembl; ENSRNOT00000032248; ENSRNOP00000036086; ENSRNOG00000008587.
GeneID; 89804; -.
KEGG; rno:89804; -.
CTD; 7010; -.
RGD; 620980; Tek.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00810000125384; -.
KO; K05121; -.
OMA; AIEYAPH; -.
OrthoDB; EOG091G00RL; -.
Reactome; R-RNO-210993; Tie2 Signaling.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000008587; -.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
GO; GO:0009925; C:basal plasma membrane; ISO:RGD.
GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005911; C:cell-cell junction; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
GO; GO:0045121; C:membrane raft; ISO:RGD.
GO; GO:0005815; C:microtubule organizing center; IEA:Ensembl.
GO; GO:0005902; C:microvillus; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; IPI:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:RGD.
GO; GO:0004872; F:receptor activity; ISO:RGD.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; TAS:RGD.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; ISO:RGD.
GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
GO; GO:0001958; P:endochondral ossification; IEP:RGD.
GO; GO:0001935; P:endothelial cell proliferation; ISO:RGD.
GO; GO:0072012; P:glomerulus vasculature development; IMP:UniProtKB.
GO; GO:0007507; P:heart development; ISO:RGD.
GO; GO:0060347; P:heart trabecula formation; ISO:RGD.
GO; GO:0030097; P:hemopoiesis; ISO:RGD.
GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:RGD.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; ISO:RGD.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:RGD.
GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:RGD.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:RGD.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
GO; GO:0051259; P:protein oligomerization; ISO:RGD.
GO; GO:0045765; P:regulation of angiogenesis; ISO:RGD.
GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; ISO:RGD.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; ISO:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IDA:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; ISO:RGD.
GO; GO:0002040; P:sprouting angiogenesis; ISO:RGD.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
GO; GO:0048014; P:Tie signaling pathway; ISO:RGD.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:RGD.
GO; GO:0001570; P:vasculogenesis; ISO:RGD.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR018941; Tyr_kin_Tie2_Ig-like_dom-1_N.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF00041; fn3; 3.
Pfam; PF10430; Ig_Tie2_1; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00181; EGF; 2.
SMART; SM00060; FN3; 3.
SMART; SM00220; S_TKc; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF49265; SSF49265; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50853; FN3; 3.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
ATP-binding {ECO:0000256|SAAS:SAAS00708816};
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
Immunoglobulin domain {ECO:0000256|SAAS:SAAS00941986};
Kinase {ECO:0000256|SAAS:SAAS00582553};
Membrane {ECO:0000256|SAAS:SAAS00602683, ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00708816};
Proteomics identification {ECO:0000213|PeptideAtlas:D3ZCD0};
Receptor {ECO:0000256|SAAS:SAAS00600436, ECO:0000313|EMBL:EDL97760.1};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Signal {ECO:0000256|SAM:SignalP};
Transferase {ECO:0000256|SAAS:SAAS00582553};
Transmembrane {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Tyrosine-protein kinase {ECO:0000256|SAAS:SAAS00582553}.
SIGNAL 1 22 {ECO:0000256|SAM:SignalP}.
CHAIN 23 1120 {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5011204976.
TRANSMEM 742 766 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 221 252 EGF-like. {ECO:0000259|PROSITE:PS50026}.
DOMAIN 350 440 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 444 539 Fibronectin type-III.
{ECO:0000259|PROSITE:PS50853}.
DOMAIN 543 635 Fibronectin type-III.
{ECO:0000259|PROSITE:PS50853}.
DOMAIN 640 733 Fibronectin type-III.
{ECO:0000259|PROSITE:PS50853}.
DOMAIN 820 1092 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
DISULFID 242 251 {ECO:0000256|PROSITE-ProRule:PRU00076}.
SEQUENCE 1120 AA; 125800 MW; C1B9DDD44D58372D CRC64;
MDSLAGLVLC GVSLLLYGLV EGAMDLILIN SLPLVSDAET SLTCIASGWH PHEPITIGRD
FEALMNQHQD PLEVTQDVTR EWAKKVVWKR EKASKINGAY FCEGRVRGQA IRIRTMKMRQ
QASFLPATLT MTVDRGDNVN ISFKKVLIKE EDAVIYKNGS FIHSVPRHEV PDILEVHLPH
AQPQDAGVYS ARYIGGNLFT SAFTRLIVRR CEAQKWGPDC NRPCTTCKNN GVCHEDTGEC
ICPPGFMGRT CEKACEPHTF GRTCKERCSG SEGCKSYVFC LPDPYGCSCA TGWRGLQCNE
ACPYGHYGPD CKLRCHCTNE EMCDRFQGCL CSQGWQGLQC EKEGRPRMTP QIEDLPDHIE
VNSGKFNPIC KASGWPLPTS EEMTLVKPDG TVLQPNDFNH TDHFSVAIFT VNRILPPDSG
VWVCSVNTVA GMVEKPFNIS VKVLPEPLHA PNVIDTGHNF AIINISSEPY FGDGPIKSKK
LFYKPVNQAW KYIQVMNEIV TLNYLEPRTD YELCVQLVRP GEGGEGHPGP VRRFTTASIG
LPPPRGLSLL PKSQTALNLT WQPIFTSSED EFYVEVERWS QQTRSDQQNI KVPGNLTSVL
LNNLLPREQY SVRARVNTKA QGEWSEELRA WTLSDILPPQ PENIKITNIT DYTALVSWTI
VDGYSISSII IRYKVQGKNE DQHIDVKIKN ATITQYQLKG LEPETTYHVD IFAENNIGSS
NPAFSQEIRT LPAPKDLGGG KMLLIAILGS AGMTCITVLL AFLIMLQLKR ANVQRRMAQA
FQNVREEPAV QFNSGTLALN RKAKNNPDPT IYPVLDWNDI KFQDVIGEGN FGQVLKARIK
KDGLRMDAAI KRMKEYASKD DHRDFAGELE VLCKLGHHPN IINLLGACEH RGYLYLAIEY
APHGNLLDFL RKSRVLETDP AFAIANSTAS TLSSQQLLHF AADVARGMDY LSQKQFIHRD
LAARNILVGE NYIAKIADFG LSRGQEVYVK KTMGRLPVRW MAIESLNYSV YTTNSDVWSY
GVLLWEIVSL GGTPYCGMTC AELYEKLPQG YRLEKPLNCD DEVYDLMRQC WREKPYERPS
FAQILVSLNR MLEERKTYVN TTLYEKFTYA GIDCSAEEAA


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