ROR1_DROME
ID ROR1_DROME Reviewed; 685 AA.
AC Q24488;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Tyrosine-protein kinase transmembrane receptor Ror;
DE Short=dRor;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=Ror; ORFNames=CG4926;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Larval brain;
RX PubMed=8394009; DOI=10.1073/pnas.90.15.7109;
RA Wilson C., Goberdhan D.C.I., Steller H.;
RT "Dror, a potential neurotrophic receptor gene, encodes a Drosophila homolog
RT of the vertebrate Ror family of Trk-related receptor tyrosine kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7109-7113(1993).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE OF 545-597.
RX PubMed=9731193; DOI=10.1006/bbrc.1998.9003;
RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.;
RT "Sampling the genomic pool of protein tyrosine kinase genes using the
RT polymerase chain reaction with genomic DNA.";
RL Biochem. Biophys. Res. Commun. 249:660-667(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-112 AND SER-131, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Tyrosine-protein kinase receptor that functions during early
CC stages of neuronal development. {ECO:0000303|PubMed:8394009}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons of the developing nervous
CC system. {ECO:0000269|PubMed:8394009}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ROR subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; L20297; AAA28860.1; -; mRNA.
DR EMBL; AE014134; AAF52885.1; -; Genomic_DNA.
DR EMBL; AJ002908; CAA05743.1; -; Genomic_DNA.
DR PIR; A48289; A48289.
DR RefSeq; NP_476962.1; NM_057614.3.
DR AlphaFoldDB; Q24488; -.
DR SMR; Q24488; -.
DR BioGRID; 60456; 5.
DR STRING; 7227.FBpp0079568; -.
DR GlyGen; Q24488; 5 sites.
DR iPTMnet; Q24488; -.
DR PaxDb; Q24488; -.
DR DNASU; 34367; -.
DR EnsemblMetazoa; FBtr0079978; FBpp0079568; FBgn0010407.
DR GeneID; 34367; -.
DR KEGG; dme:Dmel_CG4926; -.
DR UCSC; CG4926-RA; d. melanogaster.
DR CTD; 34367; -.
DR FlyBase; FBgn0010407; Ror.
DR VEuPathDB; VectorBase:FBgn0010407; -.
DR eggNOG; KOG1026; Eukaryota.
DR GeneTree; ENSGT00940000166767; -.
DR HOGENOM; CLU_000288_30_3_1; -.
DR InParanoid; Q24488; -.
DR OMA; KTWHEGH; -.
DR OrthoDB; 471114at2759; -.
DR PhylomeDB; Q24488; -.
DR BRENDA; 2.7.10.1; 1994.
DR Reactome; R-DME-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR BioGRID-ORCS; 34367; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34367; -.
DR PRO; PR:Q24488; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0010407; Expressed in eye disc (Drosophila) and 9 other tissues.
DR ExpressionAtlas; Q24488; baseline and differential.
DR Genevisible; Q24488; DM.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; NAS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IEP:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; NAS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd07459; CRD_TK_ROR_like; 1.
DR CDD; cd00108; KR; 1.
DR Gene3D; 1.10.2000.10; -; 2.
DR Gene3D; 2.40.20.10; -; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR041775; Ror-like_CRD.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00130; KR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Disulfide bond; Glycoprotein; Kinase;
KW Kringle; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..685
FT /note="Tyrosine-protein kinase transmembrane receptor Ror"
FT /id="PRO_0000024462"
FT TOPO_DOM 25..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..225
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000305"
FT DOMAIN 236..310
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 410..677
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 539
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 416..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 565
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 569
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 570
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..106
FT /evidence="ECO:0000250"
FT DISULFID 49..99
FT /evidence="ECO:0000250"
FT DISULFID 90..192
FT /evidence="ECO:0000250"
FT DISULFID 180..222
FT /evidence="ECO:0000250"
FT DISULFID 184..213
FT /evidence="ECO:0000250"
FT DISULFID 237..310
FT /evidence="ECO:0000250"
FT DISULFID 258..292
FT /evidence="ECO:0000250"
FT DISULFID 280..305
FT /evidence="ECO:0000250"
SQ SEQUENCE 685 AA; 78143 MW; 526162D27D5FD7C7 CRC64;
MNKYSAFIVC ISLVLLFTKK DVGSHNVDSR IYGFQQSSGI CHIYNGTICR DVLSNAHVFV
SPNLTMNDLE ERLKAAYGVI KESKDMNANC RMYALPSLCF SSMPICRTPE RTNLLYFANV
ATNAKQLKNV SIRRKRTKSK DIKNISIFKK KSTIYEDVFS TDISSKYPPT RESENLKRIC
REECELLENE LCQKEYAIAK RHPVIGMVGV EDCQKLPQHK DCLSLGITIE VDKTENCYWE
DGSTYRGVAN VSASGKPCLR WSWLMKEISD FPELIGQNYC RNPGSVENSP WCFVDSSRER
IIELCDIPKC ADKIWIAIVG TTAAIILIFI IIFAIILFKR RTIMHYGMRN IHNINTPSAD
KNIYGNSQLN NAQDAGRGNL GNLSDHVALN SKLIERNTLL RINHFTLQDV EFLEELGEGA
FGKVYKGQLL QPNKTTITVA IKALKENASV KTQQDFKREI ELISDLKHQN IVCILGVVLN
KEPYCMLFEY MANGDLHEFL ISNSPTEGKS LSQLEFLQIA LQISEGMQYL SAHHYVHRDL
AARNCLVNEG LVVKISDFGL SRDIYSSDYY RVQSKSLLPV RWMPSESILY GKFTTESDVW
SFGVVLWEIY SYGMQPYYGF SNQEVINLIR SRQLLSAPEN CPTAVYSLMI ECWHEQSVKR
PTFTDISNRL KTWHEGHFKA SNPEM
