Reviewed, UniProtKB/Swiss-Prot P08630 (BTKL_DROME)

Names and origin

Protein names

Recommended 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

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	786 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 diversity	Alternative splicing
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA 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 component	cytoplasm 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 function	ATP 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
	Q9W171	1	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 786	786	Tyrosine-protein kinase Btk29A		PRO_0000088068
Regions
	Domain	41 – 184	144	PH
	Domain	342 – 402	61	SH3
	Domain	410 – 503	94	SH2
	Domain	526 – 779	254	Protein kinase
	Zinc finger	187 – 223	37	Btk-type
	Nucleotide binding	532 – 540	9	ATP By similarity
	Compositional bias	14 – 27	14	Ser-rich
	Compositional bias	231 – 264	34	Ser-rich
	Compositional bias	263 – 289	27	Gly-rich
Sites
	Active site	647	1	Proton acceptor By similarity
	Metal binding	195	1	Zinc By similarity
	Metal binding	206	1	Zinc By similarity
	Metal binding	207	1	Zinc By similarity
	Metal binding	217	1	Zinc By similarity
	Binding site	554	1	ATP By similarity
Amino acid modifications
	Modified residue	677	1	Phosphotyrosine; by autocatalysis By similarity
Natural variations
	Alternative sequence	1 – 183	183	Missing in isoform A.		VSP_004964
	Alternative sequence	184 – 231	48	EDSNT…NNNPS → MIPCVSLAETSVIGNMKERV KEMKVFGCRLNFWNHIGHSL TSSKTKEG in isoform A.		VSP_004965
Experimental info
	Sequence conflict	243	1	S → A in AAA28912. Ref.1
	Sequence conflict	317	1	T → N in AAA28912. Ref.1
	Sequence conflict	317	1	T → N in BAA24063. Ref.2
	Sequence conflict	317	1	T → N in BAA24064. Ref.2
	Sequence conflict	352 – 353	2	PF → LG in AAA28912. Ref.1
	Sequence conflict	363	1	L → VG in AAA28912. Ref.1
	Sequence conflict	398 – 400	3	KPK → QAE in AAA28912. Ref.1
	Sequence conflict	414	1	D → Y in AAA28912. Ref.1
	Sequence conflict	524 – 525	2	ME → IQ in AAA28912. Ref.1
	Sequence conflict	589	1	S → T in AAA28912. Ref.1
	Sequence conflict	589	1	S → T in CAA26170. Ref.7
	Sequence conflict	657	1	S → F in CAA26170. Ref.7
	Sequence conflict	681 – 684	4	GGTK → AEPS in CAA26170. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform B (D) (E) (Type 2) [UniParc]. Last modified November 25, 2002. Version 2. Checksum: E2BCE122E6AAA0AA	FASTA	786	87,392
	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
	Isoform A (C) (F) (Type 1). Checksum: 6FDEE9B1F2C230AD	FASTA	603	66,750
	10 20 30 40 50 60 MIPCVSLAET SVIGNMKERV KEMKVFGCRL NFWNHIGHSL TSSKTKEGNG SSPAQNSTRS 70 80 90 100 110 120 ISPNSSTTNS QFSLQHNSSG SLGGGVGGGL GGGGSLGLGG GGGGGGSCTP TSLQPQSSLT 130 140 150 160 170 180 TFKQSPTLLN GNGTLLDANM PGGIPTPGTP NSKAKDNSHF VKLVVALYPF KAIEGGDLSL 190 200 210 220 230 240 EKNAEYEVID DSQEHWWKVK DALGNVGYIP SNYVKPKALL GLERYEWYVG DMSRQRAESL 250 260 270 280 290 300 LKQGDKEGCF VVRKSSTKGL YTLSLHTKVP QSHVKHYHIK QNARCEYYLS EKHCCETIPD 310 320 330 340 350 360 LINYHRHNSG GLACRLKSSP CDRPVPPTAG LSHDKWEIHP MELMLMEELG SGQFGVVRRG 370 380 390 400 410 420 KWRGSIDTAV KMMKEGTMSE DDFIEEAKVM TKLQHPNLVQ LYGVCSKHRP IYIVTEYMKH 430 440 450 460 470 480 GSLLNYLRRH EKTLIGNMGL LLDMCIQVSK GMTYLERHNY IHRDLAARNC LVGSENVVKV 490 500 510 520 530 540 ADFGLARYVL DDQYTSSGGT KFPIKWAPPE VLNYTRFSSK SDVWAYGVLM WEIFTCGKMP 550 560 570 580 590 600 YGRLKNTEVV ERVQRGIILE KPKSCAKEIY DVMKLCWSHG PEERPAFRVL MDQLALVAQT LTD

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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
EMBLGenBankDDBJ	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.
PIR	A23051. TVFFDS. A27807.
RefSeq	NP_001097120.1. NP_001097121.1. NP_476745.1. NP_476746.1. NP_723369.1. NP_723370.1.
UniGene	Dm.7306
3D structure databases
HSSP	HSSP built from PDB template 1BYG based on UniProtKB P41240.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:23748N.
IntAct	P08630. 7 interactions.
Genome annotation databases
Ensembl	FBgn0003502. Drosophila melanogaster. [Contig view]
GeneID	34132.
KEGG	dme:Dmel_CG8049.
Organism-specific databases
FlyBase	FBgn0003502. Btk29A.
Phylogenomic databases
OMA	P08630. VIANSEK.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-007985-MON. DMEL-XXX-02:DMEL-XXX-02-007986-MON.
BRENDA	2.7.10.2. 48.
Gene expression databases
ArrayExpress	P08630.
GermOnline	CG8049. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011993. 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]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit. G3DSA:3.30.505.10. SH2. 1 hit.
Pfam	PF00169. PH. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. PD000093. SH2. 1 hit. PD000066. SH3. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00107. BTK. 1 hit. SM00233. PH. 1 hit. SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
PROSITE	PS50003. 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]
ProtoNet	Search...
Other Resources
NextBio	787021.

Entry information

Entry name

BTKL_DROME

Accession

Primary (citable) accession number: P08630
Secondary accession number(s): A4V0F3 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project