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Tyrosine-protein kinase receptor (EC 2.7.10.1)

 T2CB11_RAT              Unreviewed;      1384 AA.
T2CB11; F1LN53;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
18-JUL-2018, entry version 45.
RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
Name=Insr {ECO:0000313|EMBL:AGV29469.1,
ECO:0000313|Ensembl:ENSRNOP00000049655, ECO:0000313|RGD:2917};
ORFNames=rCG_58966 {ECO:0000313|EMBL:EDL74923.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|EMBL:AGV29469.1};
[1] {ECO:0000313|Ensembl:ENSRNOP00000049655, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000049655,
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:EDL74923.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL74923.1};
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:EDL74923.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL74923.1};
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:ENSRNOP00000049655}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000049655};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
[5] {ECO:0000313|EMBL:AGV29469.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Copenhagen {ECO:0000313|EMBL:AGV29470.1}, and
Fischer 344 {ECO:0000313|EMBL:AGV29469.1};
PubMed=24023717;
Ren X., Graham J.C., Jing L., Mikheev A.M., Gao Y., Lew J.P., Xie H.,
Kim A.S., Shang X., Friedman C., Vail G., Fang M.Z., Bromberg Y.,
Zarbl H.;
"Mapping of Mcs30, a New Mammary Carcinoma Susceptibility Quantitative
Trait Locus (QTL30) on Rat Chromosome 12: Identification of Fry as a
Candidate Mcs Gene.";
PLoS ONE 8:E70930-E70930(2013).
[6] {ECO:0000313|EMBL:AGV29469.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Copenhagen {ECO:0000313|EMBL:AGV29470.1}, and
Fischer 344 {ECO:0000313|EMBL:AGV29469.1};
Ren X.F.;
Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000256|RuleBase:RU000312,
ECO:0000256|SAAS:SAAS00701269}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily.
{ECO:0000256|RuleBase:RU000312}.
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EMBL; AABR07034944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07034945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07034946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF112847; AGV29469.1; -; mRNA.
EMBL; KF112848; AGV29470.1; -; mRNA.
EMBL; CH474084; EDL74923.1; -; Genomic_DNA.
RefSeq; NP_058767.2; NM_017071.2.
UniGene; Rn.9876; -.
Ensembl; ENSRNOT00000041155; ENSRNOP00000049655; ENSRNOG00000029986.
GeneID; 24954; -.
KEGG; rno:24954; -.
CTD; 3643; -.
RGD; 2917; Insr.
eggNOG; KOG4258; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118818; -.
KO; K04527; -.
OMA; ESAGECC; -.
OrthoDB; EOG091G00GE; -.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-RNO-74713; IRS activation.
Reactome; R-RNO-74749; Signal attenuation.
Reactome; R-RNO-74751; Insulin receptor signalling cascade.
Reactome; R-RNO-74752; Signaling by Insulin receptor.
Reactome; R-RNO-77387; Insulin receptor recycling.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000029986; -.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005899; C:insulin receptor complex; IEA:Ensembl.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0031981; C:nuclear lumen; IEA:Ensembl.
GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:Ensembl.
GO; GO:0043559; F:insulin binding; IEA:Ensembl.
GO; GO:0043560; F:insulin receptor substrate binding; IEA:Ensembl.
GO; GO:0005009; F:insulin-activated receptor activity; IEA:Ensembl.
GO; GO:0031994; F:insulin-like growth factor I binding; IEA:Ensembl.
GO; GO:0031995; F:insulin-like growth factor II binding; IEA:Ensembl.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IEA:Ensembl.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0051425; F:PTB domain binding; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0008544; P:epidermis development; IEA:Ensembl.
GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0030238; P:male sex determination; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0048639; P:positive regulation of developmental growth; IEA:Ensembl.
GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
GO; GO:0051446; P:positive regulation of meiotic cell cycle; IEA:Ensembl.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0060267; P:positive regulation of respiratory burst; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
GO; GO:2000194; P:regulation of female gonad development; IEA:Ensembl.
GO; GO:0019087; P:transformation of host cell by virus; IEA:Ensembl.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.80.20.20; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
Pfam; PF00041; fn3; 1.
Pfam; PF00757; Furin-like; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000620; Insulin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 3.
SMART; SM00261; FU; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49265; SSF49265; 4.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS50853; FN3; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
1: Evidence at protein level;
ATP-binding {ECO:0000256|SAAS:SAAS00708816};
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Kinase {ECO:0000256|SAAS:SAAS00582553};
Membrane {ECO:0000256|SAAS:SAAS00602683, ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00708816};
Phosphoprotein {ECO:0000256|RuleBase:RU000312};
Proteomics identification {ECO:0000213|PeptideAtlas:T2CB11};
Receptor {ECO:0000256|RuleBase:RU000312,
ECO:0000256|SAAS:SAAS00600436, ECO:0000313|EMBL:AGV29469.1};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Repeat {ECO:0000256|SAAS:SAAS00786331};
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}.
TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 960 981 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 626 728 Fibronectin type-III.
{ECO:0000259|PROSITE:PS50853}.
DOMAIN 755 850 Fibronectin type-III.
{ECO:0000259|PROSITE:PS50853}.
DOMAIN 855 949 Fibronectin type-III.
{ECO:0000259|PROSITE:PS50853}.
DOMAIN 1025 1300 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
ACT_SITE 1161 1161 Proton acceptor.
{ECO:0000256|PIRSR:PIRSR000620-1}.
SEQUENCE 1384 AA; 156896 MW; 5FD2B0F942CBB2A9 CRC64;
MGSGRGCETT AVPLLMAVAA LLVGTAGHLY PGEVCPGMDI RNNLTRLHEL ENCSVIEGHL
QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK DLFPNLTVIR GSRLFFNYAL
VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN ELCYLATIDW SRILDSVEDN YIVLNKDDNE
ECGDVCPGTA KGKTNCPATV INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHKECL
GNCSEPDDPT KCVACRNFYL DGQCVETCPP PYYHFQDWRC VNFSFCQDLH YKCRNSRKPG
CHQYVIHNNK CIPECPSGYT MNSSNLMCTP CLGPCPKVCQ ILEGEKTIDS VTSAQELRGC
TVINGSLIIN IRGGNNLAAE LEANLGLIEE ISGFLKIRRS YALVSLSFFR KLHLIRGETL
EIGNYSFYAL DNQNLRQLWD WNKHNLTITQ GKLFFHYNPK LCLSEIHKME EVSGTKGRQE
RNDIALKTNG DQASCENELL KFSFIRTSFD KILLRWEPYW PPDFRDLLGF MLFYKEAPYQ
NVTEFDGQDA CGSNSWTVVD IDPPQRSNDP KSQTPSHPGW LMRGLKPWTQ YAIFVKTLVT
FSDERRTYGA KSDIIYVQTD ATNPSVPLDP ISVSNSSSQI ILKWKPPSDP NGNITHYLVY
WERQAEDSEL FELDYCLKGL KLPSRTWSPP FESDDSQKHN QSEYDDSASE CCSCPKTDSQ
ILKELEESSF RKTFEDYLHN VVFVPRKTSS GNGAEDTRPS RKRRSLEEVG NVTATTPTLP
DFPNISSTIA PTSHEEHRPF EKVVNKESLV ISGLRHFTGY RIELQACNQD SPEERCSVAA
YVSARTMPEA KADDIVGPVT HEIFENNVVH LMWQEPKEPN GLIVLYEVSY RRYGDEELHL
CVSRKHFALE RGCRLRGLSP GNYSVRVRAT SLAGNGSWTE PTYFYVTDYL DVPSNIAKII
IGPLIFVFLF SVVIGSIYLF LRKRQPDGPM GPLYASSNPE YLSASDVFPS SVYVPDEWEV
PREKITLLRE LGQGSFGMVY EGNAKDIIKG EVETRVAVKT VNESASLRER IEFLNEASVM
KGFTCHHVVR LLGVVSKGQP TLVVMELMAH GDLKSHLRSL RPDAENNPGR PPPTLQEMIQ
MTAEIADGMA YLNAKKFVHR DLAARNCMVA HDFTVKIGDF GMTRDIYETD YYRKGGKGLL
PVRWMSPESL KDGVFTASSD MWSFGVVLWE ITSLAEQPYQ GLSNEQVLKF VMDGGYLDPP
DNCPERLTDL MRMCWQFNPK MRPTFLEIVN LLKDDLHPSF PEVSFFYSEE NKAPESEELE
MEFEDMENVP LDRSSHCQRE EAGCREGGSS LSIKRTYDEH IPYTHMNGGK KNGRVLTLPR
SNPS


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18-272-195043 TIE1 - Goat polyclonal to TIE1; EC 2.7.10.1; Tyrosine-protein kinase receptor TIE-2; hTIE2; Tyrosine-protein kinase receptor TEK; p140 TEK; Tunica interna endothelial cell kinase; CD202b antigen Polyc 0.05 mg


 

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