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Reviewed, UniProtKB/Swiss-Prot P08630 (BTKL_DROME)

Last modified June 16, 2009. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tyrosine-protein kinase Btk29A
      Short name=Dsrc28C
      Short name=Dsrc29a
    EC=2.7.10.2
Gene names
Name: Btk29A
Synonyms: Src2, Src29A, Tec29
ORF Names: CG8049
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length786 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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.2 Ref.9 Ref.1

Developmental stage

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

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
Gene Ontology (GO)
   Biological processDNA endoreduplication

Inferred from mutant phenotype. Source: FlyBase

JNK cascade

Traceable author statement. Source: FlyBase

actin cytoskeleton organization

Inferred from mutant phenotype. Source: FlyBase

cellularization

Inferred from mutant phenotype. Source: FlyBase

copulation

Non-traceable author statement. Source: FlyBase

courtship behavior

Non-traceable author statement. Source: FlyBase

determination of adult life span Ref.2

Inferred from mutant phenotype. Source: UniProtKB

dorsal closure

Traceable author statement. Source: FlyBase

head involution

Inferred from mutant phenotype. Source: FlyBase

imaginal disc-derived male genitalia development Ref.2

Inferred from mutant phenotype. Source: UniProtKB

karyosome formation

Inferred from mutant phenotype. Source: FlyBase

open tracheal system development

Inferred from mutant phenotype. Source: FlyBase

ovarian fusome organization

Inferred from mutant phenotype. Source: FlyBase

ovarian ring canal formation Ref.7 Ref.9

Inferred from direct assay. Source: UniProtKB

protein amino acid phosphorylation

Non-traceable author statement. Source: FlyBase

regulation of actin filament polymerization

Inferred from mutant phenotype. Source: FlyBase

salivary gland morphogenesis

Inferred from mutant phenotype. Source: FlyBase

   Cellular componentcytoplasm

Inferred from direct assay. Source: FlyBase

germline ring canal Ref.7 Ref.9

Inferred from direct assay. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: FlyBase

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9W1711EBI-274168,EBI-168461

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).

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: 3110602] [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: 10330180] [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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[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: 12537569] [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: 9660966] [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: 3923437] [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: 9655810] [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

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.
NP_001097121.1.
NP_476745.1.
NP_476746.1.
NP_723369.1.
NP_723370.1.
UniGeneDm.7306

3D structure databases

HSSPHSSP built from PDB template 1BYG based on UniProtKB P41240.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:23748N.
IntActP08630. 7 interactions.

Genome annotation databases

EnsemblFBgn0003502. Drosophila melanogaster. [Contig view]
GeneID34132.
KEGGdme:Dmel_CG8049.

Organism-specific databases

FlyBaseFBgn0003502. Btk29A.

Phylogenomic databases

OMAP08630. VIANSEK.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-007985-MON.
DMEL-XXX-02:DMEL-XXX-02-007986-MON.
BRENDA2.7.10.2. 48.

Gene expression databases

ArrayExpressP08630.
GermOnlineCG8049. Drosophila melanogaster.

Family and domain databases

InterProIPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR001562. Znf_Btk_motif.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:3.30.505.10. SH2. 1 hit.
PfamPF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
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 Resources

NextBio787021.

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: June 16, 2009
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents