Reviewed, UniProtKB/Swiss-Prot Q9V6K3 (ROR2_DROME)

Names and origin

Protein names

Recommended name:
    Tyrosine-protein kinase transmembrane receptor Ror2
      Short name=dRor2
    EC=2.7.10.1
Alternative name(s):
    Neurospecific receptor tyrosine kinase

Gene names

Name:	Nrk
Synonyms:	ROR2
ORF Names:	CG4007

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	724 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Tyrosine-protein kinase receptor that functions during early stages of neuronal development By similarity.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subcellular location	Membrane; Single-pass type I membrane protein Potential.
Tissue specificity	Expressed in neural cell lineage from embryonic stage 11 onwards, resulting in expression in the brain and ventral nerve cord at the end of embryogenesis.
Developmental stage	Expressed at high levels in embryos and larvae, low levels in adults and pupae show maximal expression.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. ROR subfamily. Contains 1 FZ (frizzled) domain. Contains 1 kringle domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Kringle Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Ref.5 Inferred from direct assay. Source: FlyBase transmembrane receptor protein tyrosine kinase signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 41	41	Potential
	Chain	42 – 724	683	Tyrosine-protein kinase transmembrane receptor Ror2		PRO_0000024463
Regions
	Topological domain	42 – 322	281	Extracellular Potential
	Transmembrane	323 – 343	21	Potential
	Topological domain	344 – 724	381	Cytoplasmic Potential
	Domain	441 – 711	271	Protein kinase
	Nucleotide binding	447 – 455	9	ATP By similarity
Sites
	Active site	580	1	Proton acceptor By similarity
	Binding site	475	1	ATP By similarity
Amino acid modifications
	Modified residue	606	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	610	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	611	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	186	1	N-linked (GlcNAc...) Potential
	Glycosylation	194	1	N-linked (GlcNAc...) Potential
	Glycosylation	201	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	N-linked (GlcNAc...) Potential
	Disulfide bond	70 ↔ 134		By similarity
	Disulfide bond	78 ↔ 127		By similarity
	Disulfide bond	118 ↔ 159		By similarity
	Disulfide bond	147 ↔ 202		By similarity
	Disulfide bond	151 ↔ 187		By similarity
	Disulfide bond	219 ↔ 297		By similarity
	Disulfide bond	240 ↔ 280		By similarity
	Disulfide bond	268 ↔ 292		By similarity
Experimental info
	Sequence conflict	51	1	V → A in AAD02091. Ref.1
	Sequence conflict	192	1	H → Y in BAA20134. Ref.5
	Sequence conflict	306	1	V → G in AAD02091. Ref.1
	Sequence conflict	387	1	G → V in BAA20134. Ref.5
	Sequence conflict	391	1	T → M in BAA20134. Ref.5
	Sequence conflict	547	1	Q → R in AAD02091. Ref.1
	Sequence conflict	547	1	Q → R in BAA20134. Ref.5
	Sequence conflict	706 – 724	19	EINHC…CKAML → RSTTASSTASPRASARQCFR GLPEK in BAA20134. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9V6K3-1 [UniParc]. Last modified October 1, 2000. Version 2. Checksum: 0FFB9E1F7E4F6A26	FASTA	724	81,837
	10 20 30 40 50 60 MAAGQWVGVV ERVLRGMVLK WGANLAVLGL CVFLFASATH ANSLNAIEEP VTRRHHQRHH 70 80 90 100 110 120 EREREENGYC APYSGKVCKE YLTGQVWYSL EDPTGGWKNE QVTTALWDEL ISDLTGLCRE 130 140 150 160 170 180 AAEKMLCAYA FPNCHMEGGR AVKAPLCFED CQATHLQFCY NDWVLIEEKK ERNMFIKSRG 190 200 210 220 230 240 HFRLPNCSSL PHYNASMRRP NCSYIGLTEL KESEVSYDCR NGNGRFYMGT MNVSKSGIPC 250 260 270 280 290 300 QRWDTQYPHK HFQPPLVFHQ LLEGENYCRN AGGEEPHPWC YTVDESVRWQ HCDIPMCPDY 310 320 330 340 350 360 VDPNAVDLNT PIKMEKFFTP SMIFLLAGIG FVAIVTLHLM ILLVYKLSKH KDYSQPAGAA 370 380 390 400 410 420 TAECSVSMRG GGDCGGNLNT SRETLGGNGN TNTLAKWGTI RSTATIHSNC VALTTVTNVS 430 440 450 460 470 480 DAKGTKPNAR LEKLEYPRGD IVYVRSLGQG AFGRVFQARA PGLVPDQEDL LVAVKMLKDD 490 500 510 520 530 540 ASDQMQMDFE REACLLAEFD HPNIVRLLGV CALGRPMCLL FEYMAPGDLS EFLRACSPYA 550 560 570 580 590 600 THQAPTQDRL QLNELHLLQM AANIAAGMLY LSERKFVHRD LATRNCLINE HMAVKIADFG 610 620 630 640 650 660 LSHKIYLQDY YKGDENDFIP IRWMPLESIL YNKFSLESDV WAYGICLWEV FSFALQPYFG 670 680 690 700 710 720 LTHEEVIKYI KEGNVLGCPD NTPLSVYALM RRCWNRKPSE RPGFAEINHC IQHSIAESEC KAML

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Drosophila dRor2 gene." Frith K.J., Scott M.J. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"A novel Drosophila receptor tyrosine kinase expressed specifically in the nervous system. Unique structural features and implication in developmental signaling." Oishi I., Sugiyama S., Liu Z.J., Yamamura H., Nishida Y., Minami Y. J. Biol. Chem. 272:11916-11923(1997) [PubMed: 9115253] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-724, CHARACTERIZATION. Tissue: Imaginal disk.
[6]	"Sampling the genomic pool of protein tyrosine kinase genes using the polymerase chain reaction with genomic DNA." Oates A.C., Wollberg P., Achen M.G., Wilks A.F. Biochem. Biophys. Res. Commun. 249:660-667(1998) [PubMed: 9731193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 586-638.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF037164 Genomic DNA. Translation: AAD02091.1. AE013599 Genomic DNA. Translation: AAF58420.2. BT033065 mRNA. Translation: ACE82588.1. AB001420 mRNA. Translation: BAA20134.1. AJ002920 Genomic DNA. Translation: CAA05755.1.
RefSeq	NP_477255.1.
UniGene	Dm.4822
3D structure databases
HSSP	HSSP built from PDB template 1LUF based on UniProtKB Q62838.
ModBase	Search...
Genome annotation databases
Ensembl	FBgn0020391. Drosophila melanogaster. [Contig view]
GeneID	36445.
KEGG	dme:Dmel_CG4007.
NMPDR	fig|7227.3.peg.4990.
Organism-specific databases
FlyBase	FBgn0020391. Nrk.
Phylogenomic databases
HOGENOM	Q9V6K3.
OMA	Q9V6K3. MPLESIL.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-004374-MON.
Gene expression databases
ArrayExpress	Q9V6K3.
GermOnline	CG4007. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000001. Kringle. IPR018056. Kringle_CS. IPR018059. Kringle_sub. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR001245. Tyr_pkinase. IPR008266. Tyr_pkinase_AS. IPR016247. TyrPK_TMrec_ROR. [Graphical view]
Gene3D	G3DSA:2.40.20.10. Kringle. 1 hit.
Pfam	PF00051. Kringle. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PIRSF	PIRSF000624. TyrPK_TMrec_ROR. 1 hit.
PRINTS	PR00018. KRINGLE. PR00109. TYRKINASE.
ProDom	PD000395. Kringle. 1 hit. PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00130. KR. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
PROSITE	PS50038. FZ. 1 hit. PS00021. KRINGLE_1. 1 hit. PS50070. KRINGLE_2. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	798604.

Entry information

Entry name

ROR2_DROME

Accession

Primary (citable) accession number: Q9V6K3
Secondary accession number(s): B3LF77 , O02001, O96391, Q9TYH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project