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Proto-oncogene tyrosine-protein kinase ROS (EC 2.7.10.1) (Proto-oncogene c-Ros) (Proto-oncogene c-Ros-1) (Receptor tyrosine kinase c-ros oncogene 1) (c-Ros receptor tyrosine kinase)

 ROS1_CHICK              Reviewed;        2311 AA.
P08941;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 3.
28-FEB-2018, entry version 142.
RecName: Full=Proto-oncogene tyrosine-protein kinase ROS;
EC=2.7.10.1;
AltName: Full=Proto-oncogene c-Ros;
AltName: Full=Proto-oncogene c-Ros-1;
AltName: Full=Receptor tyrosine kinase c-ros oncogene 1;
AltName: Full=c-Ros receptor tyrosine kinase;
Flags: Precursor;
Name=ROS1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=1900358;
Chen J.M., Heller D., Poon B., Kang L., Wang L.-H.;
"The proto-oncogene c-ros codes for a transmembrane tyrosine protein
kinase sharing sequence and structural homology with sevenless protein
of Drosophila melanogaster.";
Oncogene 6:257-264(1991).
[2]
NUCLEOTIDE SEQUENCE OF 1805-1867.
PubMed=3023956; DOI=10.1128/MCB.6.8.3000;
Matsushime H., Wang L.-H., Shibuya M.;
"Human c-ros-1 gene homologous to the v-ros sequence of UR2 sarcoma
virus encodes for a transmembrane receptorlike molecule.";
Mol. Cell. Biol. 6:3000-3004(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1868-2292.
PubMed=3023892; DOI=10.1128/MCB.6.5.1478;
Neckameyer W.S., Shibuya M., Hsu M.-T., Wang L.-H.;
"Proto-oncogene c-ros codes for a molecule with structural features
common to those of growth factor receptors and displays tissue
specific and developmentally regulated expression.";
Mol. Cell. Biol. 6:1478-1486(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 2010-2311.
TISSUE=Kidney;
PubMed=3325887;
Podell S.B., Sefton B.M.;
"Chicken proto-oncogene c-ros cDNA clones: identification of a c-ros
RNA transcript and deduction of the amino acid sequence of the
carboxyl terminus of the c-ros product.";
Oncogene 2:9-14(1987).
[5]
FUNCTION IN CELL PROLIFERATION, AND SUBCELLULAR LOCATION.
PubMed=8657124; DOI=10.1128/MCB.16.4.1509;
Xiong Q., Chan J.L., Zong C.S., Wang L.H.;
"Two chimeric receptors of epidermal growth factor receptor and c-Ros
that differ in their transmembrane domains have opposite effects on
cell growth.";
Mol. Cell. Biol. 16:1509-1518(1996).
[6]
FUNCTION IN STAT3 ACTIVATION.
PubMed=9774423; DOI=10.1074/jbc.273.43.28065;
Zong C.S., Zeng L., Jiang Y., Sadowski H.B., Wang L.H.;
"Stat3 plays an important role in oncogenic Ros- and insulin-like
growth factor I receptor-induced anchorage-independent growth.";
J. Biol. Chem. 273:28065-28072(1998).
[7]
FUNCTION IN VAV3 ACTIVATION, AND INTERACTION WITH VAV3.
PubMed=11094073; DOI=10.1128/MCB.20.24.9212-9224.2000;
Zeng L., Sachdev P., Yan L., Chan J.L., Trenkle T., McClelland M.,
Welsh J., Wang L.H.;
"Vav3 mediates receptor protein tyrosine kinase signaling, regulates
GTPase activity, modulates cell morphology, and induces cell
transformation.";
Mol. Cell. Biol. 20:9212-9224(2000).
[8]
FUNCTION IN PI3 KINASE AND STAT3 ACTIVATION.
PubMed=11799110; DOI=10.1074/jbc.M108166200;
Nguyen K.T., Zong C.S., Uttamsingh S., Sachdev P., Bhanot M., Le M.T.,
Chan J.L., Wang L.H.;
"The role of phosphatidylinositol 3-kinase, rho family GTPases, and
STAT3 in Ros-induced cell transformation.";
J. Biol. Chem. 277:11107-11115(2002).
-!- FUNCTION: Orphan receptor tyrosine kinase (RTK) that may activate
several downstream signaling pathways related to cell
differentiation, proliferation, growth and survival including the
PI3 kinase-mTOR signaling pathway. Mediates the phosphorylation of
PTPN11, an activator of this pathway. May also phosphorylate and
activate the transcription factor STAT3 to control anchorage-
independent cell growth. Mediates the phosphorylation and the
activation of VAV3, a guanine nucleotide exchange factor
regulating cell morphology. May activate other downstream
signaling proteins including AKT1, MAPK1, MAPK3, IRS1, and PLCG2.
{ECO:0000269|PubMed:11094073, ECO:0000269|PubMed:11799110,
ECO:0000269|PubMed:8657124, ECO:0000269|PubMed:9774423}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Interacts with VAV3; constitutive interaction mediating
VAV3 phosphorylation. {ECO:0000269|PubMed:11094073}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8657124};
Single-pass type I membrane protein {ECO:0000305|PubMed:8657124}.
-!- TISSUE SPECIFICITY: Highest expression in kidney. Also expressed
in gonad, thymus, bursa, brain and kidney.
{ECO:0000269|PubMed:1900358}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M13013; AAA49058.1; -; Genomic_DNA.
EMBL; X06770; CAA29938.1; -; mRNA.
PIR; A60197; TVCHSR.
UniGene; Gga.702; -.
ProteinModelPortal; P08941; -.
SMR; P08941; -.
STRING; 9031.ENSGALP00000036566; -.
iPTMnet; P08941; -.
PaxDb; P08941; -.
eggNOG; ENOG410IQAA; Eukaryota.
eggNOG; ENOG410XSTC; LUCA.
HOGENOM; HOG000137937; -.
HOVERGEN; HBG058631; -.
InParanoid; P08941; -.
PhylomeDB; P08941; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
GO; GO:0002066; P:columnar/cuboidal epithelial cell development; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0032006; P:regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
CDD; cd00063; FN3; 7.
Gene3D; 2.120.10.30; -; 3.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
Pfam; PF00041; fn3; 3.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 9.
SMART; SM00135; LY; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49265; SSF49265; 5.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50853; FN3; 9.
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; Cell membrane; Complete proteome; Glycoprotein; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 2311 Proto-oncogene tyrosine-protein kinase
ROS.
/FTId=PRO_0000016723.
TOPO_DOM 25 1873 Extracellular. {ECO:0000255}.
TRANSMEM 1874 1898 Helical. {ECO:0000255}.
TOPO_DOM 1899 2311 Cytoplasmic. {ECO:0000255}.
DOMAIN 110 202 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 203 294 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 571 671 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 952 1047 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1051 1158 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1459 1569 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1570 1669 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1671 1766 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1767 1868 Fibronectin type-III 9.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1961 2240 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1967 1975 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 2095 2095 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 1996 1996 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2131 2131 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 132 132 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 377 377 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 405 405 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 480 480 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 607 607 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 706 706 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 714 714 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 911 911 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 940 940 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 962 962 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 971 971 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1110 1110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1154 1154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1180 1180 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1233 1233 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1255 1255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1282 1282 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1316 1316 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1470 1470 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1509 1509 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1588 1588 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1628 1628 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1682 1682 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1696 1696 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1730 1730 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1792 1792 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1795 1795 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1822 1822 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 1827 1827 N -> S (in Ref. 2). {ECO:0000305}.
CONFLICT 2140 2141 IN -> LP (in Ref. 3 and 4).
{ECO:0000305}.
CONFLICT 2255 2292 FINQAFEDIDVPPADSDSILSTTLMEARDQEGLNYLVV ->
SSTKLLRVSLGSAVPTAFAQTCNSVNVESQNGLGWKGP
(in Ref. 3; AAA49058). {ECO:0000305}.
SEQUENCE 2311 AA; 260961 MW; CF9680E5B0491417 CRC64;
MRNACLLLNR LGAFYFIWIS AAYCSFSKNC QDLCTSNLEG ELGIANLCNV SDINVACTQG
CQFWNATEQV NCPLKCNKTY TRECETVSCK FGCSRAEDAY GVEAQNCLNK PGAPFASSIG
SHNITLGWKP ANISEVKYII QWKFHQLPGD WRYTEVVSET SYTVKDLQAF TEYEFRVVWI
ITSQLQLHSP PSPSYRTHAS GVPTTAPIIK DIQSSSPNTV EVSWFPPLFP NGLIVGYNLV
LTSENHELLR ASRGHSFQFY STFPNSTYRF SIVAVNEAGA GPPAEANITT PESKVKEKAK
WLFLSRNQSL RKRYMEHFLE AAHCLQNGII HHNITGISVN VYQQVVYFSE GNSIWVKGVV
DMSDVSDLTL FYTGWGNITS ISVDWLYQRM YFVMNEKIHV CQLENCTAAE DITPPYETSP
RKIVADPYNG YIFCLLEDGI YRANLPLFPD TASAASLVVK SHTLRDFMIN FQSKRLIFFN
KTEQAFVSGF LDGSEFHTLR AHVPLDDMES FVYEDNIFTV TDGRAVFHEE ISQVGSSSFN
EYVVDCSLEY PEYFGFGNLL FYAASTQPYP LPTLPRLVTV LFGSDQAVIS WSPPEYTIGT
SRSAWQNWTY DVKVSSQSTF EEEWVVSNIT DTRFAVKNLV SFTEYEMSVR AVSPAGEGPW
SEPFRGMTFE EAEEEPYILA VGAEGLWKQR LDSYGPGEFL YPHIRNISDL DWYNDTLYWS
NSMGKVQTWS MNKKEGTTEN SYVPDIKNAR MLAFDWLGQC LYWAGKANTI YRKSLLGDHM
DVVAHVVYVV KDLAVDSVNG YLYWATTYTV ESARLNGEEY LILQEHLQFS GKQVVGLALD
LTSGFLYWLV QDGLCLNLYR ISICKESCGN IMVTEISAWS VSEVSQNALQ YYSGRLFWIN
RLKFITTQEL NQSISIPFSE PAEFAAFTLV HTSLKPLPGN FSFTPKVIPS SVPESSFKIK
GNSSSFHIIW NASTDVQWGT VFYCVGSNAL QMRTLESERC LHPHDLTVPS YKVDWLEPFT
LFDFSVTPYT YWGKAPTTSV YLRAPEGVPS APANPRIYVL HSNTHEGEEK VLVELRWDKP
ERDNGVLTQF RVYYQLLYES GAADTLMEWN VSDVKPTALL FSIRDEHPRL TVRFQVQAFT
SVGPGPMSDV AQRNSSDIFP VPTLITFSSN KLFLTDIDSN HTIWEVLTNR NIKDICYTAD
DDKVYYILED SLFLLNVQST SESQLFEDVF LRNVTAITVD WIARHLFVAM KTSWNETQVF
FIDLELKTKS LKALNIQLGK RNSTISSLLS YPFLSRLYWI EELDYGSRMF YYDILNNTMY
HILGYESVEE KMRNYCNCNV AEAELGRPIS IDVTDIKKPQ LLFIRGRDEI WASDVDACHC
WRITKIPSFQ GTKIGSLTVD KQFIYWTIEK KEYTEICLAD KESTRHSLQR KANHELKILA
YSSAMQSYPD KKCLTPLLDT EKPTILDTTN TSFTLSLPSV TTQQLCPSIS QPTPTYLVFF
REITSNHENS TYHFSTLLQK TLEIQEPIAV INNLKPFSTY AIQVAVKNYY SNQNQLAVGR
EAISTTLYGV PEGVDSIKTV VLSDTTINIS WSEPLEPNGP LESIRYQISV NLLSLFPEAP
LRKSEFPNGT LSWSVSDLQS GTNNLFKVLA FHPNENWFSE SVPVIAKTFE TPLSPSNIIP
RNTSFQLEWR APLHINGTSF WFELSKWQTR SDWFSPASTT CTVGPVYTCN LTGTLPSANY
LVRATVVYVT GMKSTSSPTS FKTTAGVPSK PGTPKRAEDS KNSVQWEKAE DNGSNLTYYI
LESRKQSGNT NKVKSLWVVV YNGSCDNICT WKAENLEGTF QFRAAAANML GLGEYSDTSK
DIVLAKDTVT SPDITAIVAV IGAVVLGLTI IILFGFVWHQ RWKSRKPAST GQIVLVKEDK
ELAQLRGMAE TVGLANACYA VSTLPSQAEI ESLPAFPRDK LNLHKLLGSG AFGEVYEGTA
LDILADGSGE SRVAVKTLKR GATDQEKSEF LKEAHLMSKF DHPHILKLLG VCLLNEPQYL
ILELMEGGDL LSYLRGARKQ KFQSPLLTLT DLLDICLDIC KGCVYLEKMR FIHRDLAARN
CLVSEKQYGS CSRVVKIGDF GLARDIYKND YYRKRGEGLI NVRWMAPESL IDGVFTNHSD
VWAFGVLVWE TLTLGQQPYP GLSNIEVLHH VRSGGRLESP NNCPDDIRDL MTRCWAQDPH
NRPTFFYIQH KLQEIRHSPL CFSYFLGDKE SVAGFINQAF EDIDVPPADS DSILSTTLME
ARDQEGLNYL VVVKESNQDQ GSISSAELTS V


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