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Protein

Tyrosine-protein kinase receptor torso

Gene

tor

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable receptor with tyrosine-protein kinase activity. Required for determination of anterior and posterior terminal structures in the Drosophila embryo. The ligand of torso seems to be TSL.2 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei502 – 5021ATPPROSITE-ProRule annotation
Active sitei741 – 7411Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi481 – 4899ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein tyrosine kinase activity Source: FlyBase
  • transmembrane receptor protein tyrosine kinase activity Source: FlyBase

GO - Biological processi

  • anterior/posterior axis specification, embryo Source: FlyBase
  • cell fate determination Source: FlyBase
  • chorion-containing eggshell pattern formation Source: FlyBase
  • gastrulation Source: FlyBase
  • Malpighian tubule morphogenesis Source: FlyBase
  • metamorphosis Source: FlyBase
  • negative phototaxis Source: FlyBase
  • negative regulation of multicellular organism growth Source: FlyBase
  • peptidyl-tyrosine phosphorylation Source: GOC
  • pole cell migration Source: FlyBase
  • protein autophosphorylation Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • terminal region determination Source: FlyBase
  • torso signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 1994.
SignaLinkiP18475.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase receptor torso (EC:2.7.10.1)
Gene namesi
Name:tor
ORF Names:CG1389
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003733. tor.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 399379ExtracellularSequence AnalysisAdd
BLAST
Transmembranei400 – 42021HelicalSequence AnalysisAdd
BLAST
Topological domaini421 – 923503CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 923903Tyrosine-protein kinase receptor torsoPRO_0000024477Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence Analysis
Modified residuei608 – 6081Phosphoserine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP18475.

Expressioni

Tissue specificityi

Expressed throughout the embryo but is activated specifically at the poles.2 Publications

Developmental stagei

Expressed both maternally and zygotically.2 Publications

Gene expression databases

BgeeiP18475.
ExpressionAtlasiP18475. differential.
GenevisibleiP18475. DM.

Interactioni

Protein-protein interaction databases

BioGridi61589. 28 interactions.
IntActiP18475. 2 interactions.
MINTiMINT-755149.
STRINGi7227.FBpp0111751.

Structurei

3D structure databases

ProteinModelPortaliP18475.
SMRiP18475. Positions 465-922.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini475 – 874400Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00800000124033.
InParanoidiP18475.
KOiK12378.
OMAiAFKCEIQ.
OrthoDBiEOG7BZVTF.
PhylomeDBiP18475.

Family and domain databases

InterProiIPR003961. FN3_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P18475-1) [UniParc]FASTAAdd to basket

Also known as: C

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLIFYAKYAF IFWFFVGSNQ GEMLLMDKIS HDKTLLNVTA CTQNCLEKGQ
60 70 80 90 100
MDFRSCLKDC RINGTFPGAL RKVQENYQMN MICRTESEIV FQIDWVQHSR
110 120 130 140 150
GTEPAPNATY IIRVDAVKDD NKETALYLSD DNFLILPGLE SNSTHNITAL
160 170 180 190 200
AMHGDGSYSL IAKDQTFATL IRGYQPSKMG AVNLLRFVPQ PDDLHHIAAE
210 220 230 240 250
IEWKPSAESN CYFDMVSYST NSVNMDEPLE VQFRDRKKLY RHTVDNLEFD
260 270 280 290 300
KQYHVGVRTV NIMNRLESDL QWLPIAVPSC LDWYPYNYTL CPPHKPENLT
310 320 330 340 350
VTQKQYLPNI LALNITWARP RYLPDNYTLH IFDLFKGGTE LNYTLDQNRS
360 370 380 390 400
HFYVPKITVL GSHFEVHLVA QSAGGKNVSG LTLDKVHRGV LLSEGNMVKL
410 420 430 440 450
VLFIIVPICC ILMLCSLTFC RRNRSEVQAL QMDAKDAKAS EFHLSLMDSS
460 470 480 490 500
GLLVTLSANE SLEVMDELEV EPHSVLLQDV LGEGAFGLVR RGVYKKRQVA
510 520 530 540 550
VKLLKDEPND EDVYAFKCEI QMLKAVGKHP NIVGIVGYST RFSNQMMLLI
560 570 580 590 600
EYCSLGSLQN FLREEWKFRQ EQNAIGLKKN LEQNVDNRRF NRLPRNSIHD
610 620 630 640 650
RIEDINNSML STVEEESESD QTHSSRCETY TLTRITNAAD NKGYGLEDIE
660 670 680 690 700
NIGGSYIPKT AEAPKDRPKR KLKPQPKKDS KQDFKSDNKK RIFENKEYFD
710 720 730 740 750
CLDSSDTKPR IPLKYADLLD IAQQVAVGME FLAQNKVVHR DLAARNVLIS
760 770 780 790 800
VDRSIKIADF GLSRDVYHEN VYRKSGGSGK LPIKWLALES LTHQVYTSQS
810 820 830 840 850
DVWSFGVLLY EITTLGGMPY PSVSPSDLLQ LLRQGHRMKR PEGCTQEMFS
860 870 880 890 900
LMESCWSSVP SHRPTFSALK HRLGGMILAT NDVPERLKQL QAATESKLKS
910 920
CDGLNSKVEQ VPCEEELYLE PLN
Length:923
Mass (Da):105,201
Last modified:August 30, 2005 - v2
Checksum:i746F46E1A4277ACF
GO
Isoform B (identifier: P18475-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     907-923: KVEQVPCEEELYLEPLN → IGLRISAK

Note: No experimental confirmation available.
Show »
Length:914
Mass (Da):104,026
Checksum:iE56B6FB1098131DB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251A → T in CAA33247 (PubMed:2927509).Curated
Sequence conflicti387 – 3871H → P in CAA33247 (PubMed:2927509).Curated
Sequence conflicti667 – 6671R → Q in CAA33247 (PubMed:2927509).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei907 – 92317KVEQV…LEPLN → IGLRISAK in isoform B. CuratedVSP_034011Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15150 Genomic DNA. Translation: CAA33247.1.
AE013599 Genomic DNA. Translation: AAF59203.1.
AE013599 Genomic DNA. Translation: ABV53713.1.
AE013599 Genomic DNA. Translation: ABV53714.1.
AY071403 mRNA. Translation: AAL49025.1.
PIRiS03900.
RefSeqiNP_001097212.2. NM_001103742.2.
NP_476762.1. NM_057414.4. [P18475-1]
UniGeneiDm.512.

Genome annotation databases

EnsemblMetazoaiFBtr0088938; FBpp0088012; FBgn0003733. [P18475-1]
GeneIDi35717.
KEGGidme:Dmel_CG1389.
UCSCiCG1389-RA. d. melanogaster. [P18475-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15150 Genomic DNA. Translation: CAA33247.1.
AE013599 Genomic DNA. Translation: AAF59203.1.
AE013599 Genomic DNA. Translation: ABV53713.1.
AE013599 Genomic DNA. Translation: ABV53714.1.
AY071403 mRNA. Translation: AAL49025.1.
PIRiS03900.
RefSeqiNP_001097212.2. NM_001103742.2.
NP_476762.1. NM_057414.4. [P18475-1]
UniGeneiDm.512.

3D structure databases

ProteinModelPortaliP18475.
SMRiP18475. Positions 465-922.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61589. 28 interactions.
IntActiP18475. 2 interactions.
MINTiMINT-755149.
STRINGi7227.FBpp0111751.

Proteomic databases

PaxDbiP18475.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088938; FBpp0088012; FBgn0003733. [P18475-1]
GeneIDi35717.
KEGGidme:Dmel_CG1389.
UCSCiCG1389-RA. d. melanogaster. [P18475-1]

Organism-specific databases

CTDi21977.
FlyBaseiFBgn0003733. tor.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00800000124033.
InParanoidiP18475.
KOiK12378.
OMAiAFKCEIQ.
OrthoDBiEOG7BZVTF.
PhylomeDBiP18475.

Enzyme and pathway databases

BRENDAi2.7.10.1. 1994.
SignaLinkiP18475.

Miscellaneous databases

GenomeRNAii35717.
NextBioi794882.
PROiP18475.

Gene expression databases

BgeeiP18475.
ExpressionAtlasiP18475. differential.
GenevisibleiP18475. DM.

Family and domain databases

InterProiIPR003961. FN3_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila gene torso encodes a putative receptor tyrosine kinase."
    Sprenger F., Stevens L.M., Nuesslein-Volhard C.
    Nature 338:478-483(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Biochemical analysis of torso and D-raf during Drosophila embryogenesis: implications for terminal signal transduction."
    Sprenger F., Torsoclair M.M., Morrison D.K.
    Mol. Cell. Biol. 13:1163-1172(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiTORSO_DROME
AccessioniPrimary (citable) accession number: P18475
Secondary accession number(s): A8DY54, A8DY56, Q9V4R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: August 30, 2005
Last modified: July 22, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.