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P08630 (BTKL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Btk29A

EC=2.7.10.2
Alternative name(s):
Dsrc28C
Dsrc29a
Gene names
Name:Btk29A
Synonyms:Src2, Src29A, Tec29
ORF Names:CG8049
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length786 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Required for proper ring canal development. Also required for the development of male genitalia and for adult survival. Ref.2 Ref.9

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Note: Ring canals.

Tissue specificity

Ring canals in the egg chambers and imaginal disks of third-instar larvae. Ref.1 Ref.2 Ref.9

Developmental stage

Expressed both maternally and zygotically. Predominantly in early to middle embryogenesis, in larvae and adult females. Ref.1 Ref.2

Disruption phenotype

Flies exhibit shortened copulatory duration (due to incomplete fusion of the left and right halves of the apodeme that holds the penis during copulation) and reduced adult-stage life span. Ref.2

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.

Contains 1 Btk-type zinc finger.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAA28912.1 differs from that shown. Reason: Frameshift at positions 62, 215, 218, 220 and 401.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA endoreduplication

Inferred from mutant phenotype PubMed 16000381. Source: FlyBase

JNK cascade

Traceable author statement PubMed 12147138. Source: FlyBase

actin cytoskeleton organization

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

cellularization

Inferred from mutant phenotype PubMed 14736750. Source: FlyBase

courtship behavior

Non-traceable author statement PubMed 11715043. Source: FlyBase

determination of adult lifespan

Inferred from mutant phenotype Ref.2. Source: UniProtKB

dorsal closure

Traceable author statement PubMed 12147138. Source: FlyBase

female germline ring canal formation

Inferred from direct assay Ref.9Ref.7. Source: UniProtKB

head involution

Inferred from mutant phenotype PubMed 9660965. Source: FlyBase

imaginal disc-derived male genitalia development

Inferred from mutant phenotype Ref.2. Source: UniProtKB

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 21635778. Source: FlyBase

karyosome formation

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

oogenesis

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

open tracheal system development

Inferred from mutant phenotype PubMed 16469972. Source: FlyBase

ovarian fusome organization

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

ovarian nurse cell to oocyte transport

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 1397284. Source: FlyBase

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

regulation of actin filament polymerization

Inferred from mutant phenotype PubMed 16000381. Source: FlyBase

regulation of imaginal disc-derived wing size

Inferred from mutant phenotype PubMed 23232763. Source: FlyBase

salivary gland morphogenesis

Inferred from mutant phenotype PubMed 16000381. Source: FlyBase

sensitization

Inferred from mutant phenotype PubMed 17464798. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 2108066. Source: FlyBase

germline ring canal

Inferred from direct assay Ref.9Ref.7. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 2108066. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine kinase activity

Inferred from direct assay PubMed 1397284. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P08630-1)

Also known as: D; E; Type 2;

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.
Isoform A (identifier: P08630-2)

Also known as: C; F; Type 1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-183: Missing.
     184-231: EDSNTPKSYR...HWREANNNPS → MIPCVSLAET...SLTSSKTKEG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 786786Tyrosine-protein kinase Btk29A
PRO_0000088068

Regions

Domain41 – 184144PH
Domain342 – 40261SH3
Domain410 – 50394SH2
Domain526 – 779254Protein kinase
Zinc finger187 – 22337Btk-type
Nucleotide binding532 – 5409ATP By similarity
Compositional bias14 – 2714Ser-rich
Compositional bias231 – 26434Ser-rich
Compositional bias263 – 28927Gly-rich

Sites

Active site6471Proton acceptor By similarity
Metal binding1951Zinc By similarity
Metal binding2061Zinc By similarity
Metal binding2071Zinc By similarity
Metal binding2171Zinc By similarity
Binding site5541ATP By similarity

Amino acid modifications

Modified residue6771Phosphotyrosine; by autocatalysis By similarity

Natural variations

Alternative sequence1 – 183183Missing in isoform A.
VSP_004964
Alternative sequence184 – 23148EDSNT…NNNPS → MIPCVSLAETSVIGNMKERV KEMKVFGCRLNFWNHIGHSL TSSKTKEG in isoform A.
VSP_004965

Experimental info

Sequence conflict2431S → A in AAA28912. Ref.1
Sequence conflict3171T → N in AAA28912. Ref.1
Sequence conflict3171T → N in BAA24063. Ref.2
Sequence conflict3171T → N in BAA24064. Ref.2
Sequence conflict352 – 3532PF → LG in AAA28912. Ref.1
Sequence conflict3631L → VG in AAA28912. Ref.1
Sequence conflict398 – 4003KPK → QAE in AAA28912. Ref.1
Sequence conflict4141D → Y in AAA28912. Ref.1
Sequence conflict524 – 5252ME → IQ in AAA28912. Ref.1
Sequence conflict5891S → T in AAA28912. Ref.1
Sequence conflict5891S → T in CAA26170. Ref.7
Sequence conflict6571S → F in CAA26170. Ref.7
Sequence conflict681 – 6844GGTK → AEPS in CAA26170. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform B (D) (E) (Type 2) [UniParc].

Last modified November 25, 2002. Version 2.
Checksum: E2BCE122E6AAA0AA

FASTA78687,392
        10         20         30         40         50         60 
MMGTKHRNSH VNGSIKSSSS LRSSSKSFQA KMDLMSERLY DVVKSGSMVK RAQNKKRFTP 

        70         80         90        100        110        120 
VNYKHRWFEL TKRTFSYFDV ENVERRRERG RIHLKGVRLV EEATVSGEGG DPFAPDGYPF 

       130        140        150        160        170        180 
QVGYCEISAS ANSHQLENGN GGGSGVGIEG QQSGRAVPQY TLYVIANSEK ERSEWIRAIR 

       190        200        210        220        230        240 
QVCEDSNTPK SYRYHPGLWS GKKWSCCKGL SRTTFGCRAA AHWREANNNP SNGSSPAQNS 

       250        260        270        280        290        300 
TRSISPNSST TNSQFSLQHN SSGSLGGGVG GGLGGGGSLG LGGGGGGGGS CTPTSLQPQS 

       310        320        330        340        350        360 
SLTTFKQSPT LLNGNGTLLD ANMPGGIPTP GTPNSKAKDN SHFVKLVVAL YPFKAIEGGD 

       370        380        390        400        410        420 
LSLEKNAEYE VIDDSQEHWW KVKDALGNVG YIPSNYVKPK ALLGLERYEW YVGDMSRQRA 

       430        440        450        460        470        480 
ESLLKQGDKE GCFVVRKSST KGLYTLSLHT KVPQSHVKHY HIKQNARCEY YLSEKHCCET 

       490        500        510        520        530        540 
IPDLINYHRH NSGGLACRLK SSPCDRPVPP TAGLSHDKWE IHPMELMLME ELGSGQFGVV 

       550        560        570        580        590        600 
RRGKWRGSID TAVKMMKEGT MSEDDFIEEA KVMTKLQHPN LVQLYGVCSK HRPIYIVTEY 

       610        620        630        640        650        660 
MKHGSLLNYL RRHEKTLIGN MGLLLDMCIQ VSKGMTYLER HNYIHRDLAA RNCLVGSENV 

       670        680        690        700        710        720 
VKVADFGLAR YVLDDQYTSS GGTKFPIKWA PPEVLNYTRF SSKSDVWAYG VLMWEIFTCG 

       730        740        750        760        770        780 
KMPYGRLKNT EVVERVQRGI ILEKPKSCAK EIYDVMKLCW SHGPEERPAF RVLMDQLALV 


AQTLTD 

« Hide

Isoform A (C) (F) (Type 1) [UniParc].

Checksum: 6FDEE9B1F2C230AD
Show »

FASTA60366,750

References

« Hide 'large scale' references
[1]"Primary sequence and developmental expression of a novel Drosophila melanogaster src gene."
Gregory R.J., Kammermeyer K.L., Vincent W.S. III, Wadsworth S.G.
Mol. Cell. Biol. 7:2119-2127(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]"The Drosophila Bruton's tyrosine kinase (Btk) homolog is required for adult survival and male genital formation."
Baba K., Takeshita A., Majima K., Ueda R., Kondo S., Juni N., Yamamoto D.
Mol. Cell. Biol. 19:4405-4413(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
Strain: Canton-S and Oregon-R.
Tissue: Head.
[3]"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. expand/collapse author list , 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.
[4]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
Strain: Berkeley.
Tissue: Embryo.
[6]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
[7]"SRC64 regulates the localization of a Tec-family kinase required for Drosophila ring canal growth."
Guarnieri D.J., Dodson G.S., Simon M.A.
Mol. Cell 1:831-840(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 199-786 (ISOFORM A).
Tissue: Eye-antennal disk.
[8]"Maternal inheritance of transcripts from three Drosophila src-related genes."
Wadsworth S.C., Madhavan K., Bilodeau-Wentworth D.
Nucleic Acids Res. 13:2153-2170(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 552-684.
[9]"Src64 is required for ovarian ring canal morphogenesis during Drosophila oogenesis."
Dodson G.S., Guarnieri D.J., Simon M.A.
Development 125:2883-2892(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[10]Sjolander K.
Unpublished observations (JUL-1997)
Cited for: SIMILARITY TO BTK SUBFAMILY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16599 mRNA. Translation: AAA28912.1. Frameshift.
AB009840 mRNA. Translation: BAA24063.1.
AB009841 mRNA. Translation: BAA24064.1.
AE014134 Genomic DNA. Translation: AAF52631.3.
AE014134 Genomic DNA. Translation: AAF52632.2.
AE014134 Genomic DNA. Translation: AAN11161.1.
AE014134 Genomic DNA. Translation: AAN11162.1.
AE014134 Genomic DNA. Translation: ABV53648.1.
AE014134 Genomic DNA. Translation: ABV53649.1.
AY069457 mRNA. Translation: AAL39602.1.
AY128441 mRNA. Translation: AAM75034.1.
BT011183 mRNA. Translation: AAR88544.1.
AF044337 mRNA. Translation: AAB99858.1.
X02305 Genomic DNA. Translation: CAA26170.1.
PIRA23051.
TVFFDS. A27807.
RefSeqNP_001097120.1. NM_001103650.2. [P08630-2]
NP_001097121.1. NM_001103651.2. [P08630-1]
NP_476745.1. NM_057397.5. [P08630-1]
NP_476746.1. NM_057398.4. [P08630-2]
NP_723369.1. NM_164804.2. [P08630-1]
NP_723370.1. NM_164805.2. [P08630-2]
UniGeneDm.7306.

3D structure databases

ProteinModelPortalP08630.
SMRP08630. Positions 48-217, 346-777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60259. 13 interactions.
DIPDIP-23748N.
IntActP08630. 1 interaction.
MINTMINT-896102.

Proteomic databases

PaxDbP08630.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079616; FBpp0079236; FBgn0003502. [P08630-1]
FBtr0079617; FBpp0079237; FBgn0003502. [P08630-1]
FBtr0112836; FBpp0111749; FBgn0003502. [P08630-1]
GeneID34132.
KEGGdme:Dmel_CG8049.

Organism-specific databases

CTD34132.
FlyBaseFBgn0003502. Btk29A.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00640000091251.
InParanoidP08630.
KOK07364.
OMARRNEEYC.
OrthoDBEOG7KM5SC.
PhylomeDBP08630.

Enzyme and pathway databases

SignaLinkP08630.

Gene expression databases

BgeeP08630.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001562. Znf_Btk_motif.
[Graphical view]
PfamPF00779. BTK. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
PS51113. ZF_BTK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBtk29A. drosophila.
GenomeRNAi34132.
NextBio787021.
PROP08630.

Entry information

Entry nameBTKL_DROME
AccessionPrimary (citable) accession number: P08630
Secondary accession number(s): A4V0F3 expand/collapse secondary AC list , A4V0F4, O45032, O76132, O76133, P11361, Q6NNV0, Q8T0A0, Q9VLQ2, Q9VLQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 25, 2002
Last modified: July 9, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase