ROR2_DROME
ID ROR2_DROME Reviewed; 724 AA.
AC Q9V6K3; B3LF77; O02001; O96391; Q9TYH9;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Tyrosine-protein kinase transmembrane receptor Ror2;
DE Short=dRor2;
DE EC=2.7.10.1;
DE AltName: Full=Neurospecific receptor tyrosine kinase;
DE Flags: Precursor;
GN Name=Nrk; Synonyms=ROR2; ORFNames=CG4007;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Frith K.J., Scott M.J.;
RT "The Drosophila dRor2 gene.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-724, AND CHARACTERIZATION.
RC TISSUE=Imaginal disk;
RX PubMed=9115253; DOI=10.1074/jbc.272.18.11916;
RA Oishi I., Sugiyama S., Liu Z.J., Yamamura H., Nishida Y., Minami Y.;
RT "A novel Drosophila receptor tyrosine kinase expressed specifically in the
RT nervous system. Unique structural features and implication in developmental
RT signaling.";
RL J. Biol. Chem. 272:11916-11923(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 586-638.
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).
CC -!- FUNCTION: Tyrosine-protein kinase receptor that functions during early
CC stages of neuronal development. {ECO:0000250}.
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: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in neural cell lineage from embryonic
CC stage 11 onwards, resulting in expression in the brain and ventral
CC nerve cord at the end of embryogenesis.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in embryos and larvae,
CC low levels in adults and pupae show maximal expression.
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; AF037164; AAD02091.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58420.2; -; Genomic_DNA.
DR EMBL; BT033065; ACE82588.1; -; mRNA.
DR EMBL; AB001420; BAA20134.1; -; mRNA.
DR EMBL; AJ002920; CAA05755.1; -; Genomic_DNA.
DR RefSeq; NP_477255.1; NM_057907.4.
DR PDB; 7ME4; X-ray; 1.75 A; A=42-321.
DR PDBsum; 7ME4; -.
DR AlphaFoldDB; Q9V6K3; -.
DR SMR; Q9V6K3; -.
DR BioGRID; 62212; 2.
DR STRING; 7227.FBpp0086841; -.
DR GlyGen; Q9V6K3; 4 sites.
DR PaxDb; Q9V6K3; -.
DR PRIDE; Q9V6K3; -.
DR EnsemblMetazoa; FBtr0087728; FBpp0086841; FBgn0020391.
DR GeneID; 36445; -.
DR KEGG; dme:Dmel_CG4007; -.
DR CTD; 203447; -.
DR FlyBase; FBgn0020391; Nrk.
DR VEuPathDB; VectorBase:FBgn0020391; -.
DR eggNOG; KOG1026; Eukaryota.
DR GeneTree; ENSGT00940000158226; -.
DR HOGENOM; CLU_000288_30_4_1; -.
DR InParanoid; Q9V6K3; -.
DR OMA; CAPYNGK; -.
DR OrthoDB; 471114at2759; -.
DR PhylomeDB; Q9V6K3; -.
DR BioGRID-ORCS; 36445; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36445; -.
DR PRO; PR:Q9V6K3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0020391; Expressed in central nervous system and 7 other tissues.
DR ExpressionAtlas; Q9V6K3; baseline and differential.
DR Genevisible; Q9V6K3; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IBA:GO_Central.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IDA:FlyBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00108; KR; 1.
DR Gene3D; 1.10.2000.10; -; 1.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016247; Tyr_kinase_rcpt_ROR.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000624; TyrPK_TMrec_ROR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00130; KR; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Developmental protein;
KW Disulfide bond; Glycoprotein; Kinase; Kringle; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..724
FT /note="Tyrosine-protein kinase transmembrane receptor Ror2"
FT /id="PRO_0000024463"
FT TOPO_DOM 42..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 441..711
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 580
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 447..455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 606
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 610
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 611
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..134
FT /evidence="ECO:0000250"
FT DISULFID 78..127
FT /evidence="ECO:0000250"
FT DISULFID 118..159
FT /evidence="ECO:0000250"
FT DISULFID 147..202
FT /evidence="ECO:0000250"
FT DISULFID 151..187
FT /evidence="ECO:0000250"
FT DISULFID 219..297
FT /evidence="ECO:0000250"
FT DISULFID 240..280
FT /evidence="ECO:0000250"
FT DISULFID 268..292
FT /evidence="ECO:0000250"
FT CONFLICT 51
FT /note="V -> A (in Ref. 1; AAD02091)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="H -> Y (in Ref. 5; BAA20134)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="V -> G (in Ref. 1; AAD02091)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="G -> V (in Ref. 5; BAA20134)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="T -> M (in Ref. 5; BAA20134)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="Q -> R (in Ref. 1; AAD02091 and 5; BAA20134)"
FT /evidence="ECO:0000305"
FT CONFLICT 706..724
FT /note="EINHCIQHSIAESECKAML -> RSTTASSTASPRASARQCFRGLPEK (in
FT Ref. 5; BAA20134)"
FT /evidence="ECO:0000305"
FT TURN 77..81
FT /evidence="ECO:0007829|PDB:7ME4"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:7ME4"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:7ME4"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:7ME4"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:7ME4"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:7ME4"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:7ME4"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:7ME4"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:7ME4"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:7ME4"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:7ME4"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:7ME4"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:7ME4"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:7ME4"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:7ME4"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:7ME4"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:7ME4"
SQ SEQUENCE 724 AA; 81837 MW; 0FFB9E1F7E4F6A26 CRC64;
MAAGQWVGVV ERVLRGMVLK WGANLAVLGL CVFLFASATH ANSLNAIEEP VTRRHHQRHH
EREREENGYC APYSGKVCKE YLTGQVWYSL EDPTGGWKNE QVTTALWDEL ISDLTGLCRE
AAEKMLCAYA FPNCHMEGGR AVKAPLCFED CQATHLQFCY NDWVLIEEKK ERNMFIKSRG
HFRLPNCSSL PHYNASMRRP NCSYIGLTEL KESEVSYDCR NGNGRFYMGT MNVSKSGIPC
QRWDTQYPHK HFQPPLVFHQ LLEGENYCRN AGGEEPHPWC YTVDESVRWQ HCDIPMCPDY
VDPNAVDLNT PIKMEKFFTP SMIFLLAGIG FVAIVTLHLM ILLVYKLSKH KDYSQPAGAA
TAECSVSMRG GGDCGGNLNT SRETLGGNGN TNTLAKWGTI RSTATIHSNC VALTTVTNVS
DAKGTKPNAR LEKLEYPRGD IVYVRSLGQG AFGRVFQARA PGLVPDQEDL LVAVKMLKDD
ASDQMQMDFE REACLLAEFD HPNIVRLLGV CALGRPMCLL FEYMAPGDLS EFLRACSPYA
THQAPTQDRL QLNELHLLQM AANIAAGMLY LSERKFVHRD LATRNCLINE HMAVKIADFG
LSHKIYLQDY YKGDENDFIP IRWMPLESIL YNKFSLESDV WAYGICLWEV FSFALQPYFG
LTHEEVIKYI KEGNVLGCPD NTPLSVYALM RRCWNRKPSE RPGFAEINHC IQHSIAESEC
KAML
