P18824 (ARM_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Armadillo segment polarity protein

Gene names

Name:	arm
ORF Names:	CG11579

Organism

Drosophila melanogaster (Fruit fly)

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	843 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Isoform neural may associate with CadN and participate in the transmission of developmental information. Can associate with alpha-catenin. Isoform cytoplasmic accumulates through wg signaling; arm function in wg signal transduction is required early in development for determination of neuroblast fate. Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis. Ref.2
Subunit structure	Interacts with Mer and Moe at the adherens junction. Ref.8
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction › adherens junction By similarity. Note: Inner surface of cell membrane and adherens junction. Ref.8
Tissue specificity	Isoform cytoplasmic is predominant before germ band retraction, after retraction and, during larval stages, it is found in high levels in specific cells along the CNS midline. Isoform neural is first seen after germ band retraction in the axon tracts of the CNS, also present in axons during larval stages and accumulates in the motor neurons of the segmental and intersegmental nerves as they exit the CNS. Both isoforms accumulate in the PNS. Ref.2
Developmental stage	Present at all stages, but reached the highest levels during early to mid-embryogenesis.
Post-translational modification	Phosphorylated on Ser, Thr and Tyr residues. Level of phosphorylation varies both during embryonic development and from embryonic tissue to tissue. Sgg is required for phosphorylation and wg signal negatively regulates arm phosphorylation. Hypophosphorylated form of arm increases in steady-state levels. Ref.7 Ref.9
Sequence similarities	Belongs to the beta-catenin family. Contains 13 ARM repeats.

Ontologies

Keywords
Biological process	Cell adhesion Wnt signaling pathway
Cellular component	Cell junction Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Developmental protein Segmentation polarity protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Uncategorized	promoter binding Inferred from Biological aspect of Ancestor. Source: RefGenome specific RNA polymerase II transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Biological process	Wnt receptor signaling pathway Inferred from mutant phenotype Ref.2. Source: UniProtKB branch fusion, open tracheal system Inferred from mutant phenotype. Source: FlyBase cell fate determination Inferred from mutant phenotype. Source: FlyBase cell morphogenesis Inferred from mutant phenotype. Source: FlyBase cell-cell adhesion Inferred from mutant phenotype. Source: FlyBase chitin-based larval cuticle pattern formation Inferred from mutant phenotype. Source: FlyBase compound eye retinal cell programmed cell death Inferred from mutant phenotype. Source: FlyBase cytoskeletal anchoring at plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome delamination Inferred from mutant phenotype. Source: FlyBase dorsal closure Inferred from mutant phenotype. Source: FlyBase epithelial cell type specification, open tracheal system Inferred from mutant phenotype. Source: FlyBase establishment or maintenance of cell polarity Non-traceable author statement. Source: FlyBase heart formation Inferred from mutant phenotype. Source: FlyBase imaginal disc-derived wing expansion Inferred from mutant phenotype. Source: FlyBase negative regulation of heart induction by canonical Wnt receptor signaling pathway Inferred from mutant phenotype. Source: FlyBase negative regulation of transcription from RNA polymerase II promoter Inferred from Biological aspect of Ancestor. Source: RefGenome neuroblast development Inferred from mutant phenotype. Source: FlyBase neuroblast fate commitment Inferred from mutant phenotype Ref.2. Source: UniProtKB oocyte development Inferred from Biological aspect of Ancestor. Source: RefGenome oocyte localization involved in germarium-derived egg chamber formation Traceable author statement. Source: FlyBase ovarian follicle cell development Traceable author statement. Source: FlyBase photoreceptor cell differentiation Inferred from mutant phenotype. Source: FlyBase positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: FlyBase regulation of cell shape Inferred from mutant phenotype. Source: FlyBase segment polarity determination Inferred from electronic annotation. Source: UniProtKB-KW somatic stem cell maintenance Inferred from mutant phenotype. Source: FlyBase ventral furrow formation Inferred from mutant phenotype. Source: FlyBase zonula adherens assembly Inferred from mutant phenotype. Source: FlyBase
Cellular component	Axin-APC-beta-catenin-GSK3B complex Inferred from Biological aspect of Ancestor. Source: RefGenome Z disc Inferred from Biological aspect of Ancestor. Source: RefGenome apical plasma membrane Inferred from direct assay. Source: FlyBase basolateral plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome catenin complex Inferred from Biological aspect of Ancestor. Source: RefGenome cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome desmosome Inferred from Biological aspect of Ancestor. Source: RefGenome fascia adherens Inferred from Biological aspect of Ancestor. Source: RefGenome internal side of plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome spot adherens junction Non-traceable author statement. Source: FlyBase transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome zonula adherens Inferred from direct assay. Source: FlyBase
Molecular function	RPTP-like protein binding Inferred from Biological aspect of Ancestor. Source: RefGenome alpha-catenin binding Inferred from Biological aspect of Ancestor. Source: RefGenome cadherin binding Inferred from Biological aspect of Ancestor. Source: RefGenome protein kinase binding Inferred from Biological aspect of Ancestor. Source: RefGenome structural molecule activity Inferred from Biological aspect of Ancestor. Source: RefGenome transcription coactivator activity Inferred from direct assay. Source: FlyBase transcription factor binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL9	O00512	3	EBI-216128,EBI-533127	From a different organism.
lgs	Q961D9	5	EBI-216128,EBI-85519
pan	P91943	2	EBI-216128,EBI-147301

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Cytoplasmic (identifier: P18824-1)

Also known as: A; B;

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 Neural (identifier: P18824-2)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     718-843: LGPEEAYEGL...NLAAWYDTDC → ILYQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 843	843	Armadillo segment polarity protein		PRO_0000064292
Regions
	Repeat	159 – 200	42	ARM 1
	Repeat	201 – 242	42	ARM 2
	Repeat	243 – 284	42	ARM 3
	Repeat	285 – 326	42	ARM 4
	Repeat	327 – 368	42	ARM 5
	Repeat	369 – 410	42	ARM 6
	Repeat	411 – 449	39	ARM 7
	Repeat	450 – 496	47	ARM 8
	Repeat	497 – 538	42	ARM 9
	Repeat	539 – 584	46	ARM 10
	Repeat	585 – 608	24	ARM 11
	Repeat	609 – 647	39	ARM 12
	Repeat	648 – 689	42	ARM 13; truncated
	Compositional bias	1 – 158	158	Asp/Glu-rich (acidic)
	Compositional bias	690 – 843	154	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	650	1	Phosphothreonine Ref.9
	Modified residue	688	1	Phosphoserine Ref.9
	Modified residue	694	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	718 – 843	126	LGPEE…YDTDC → ILYQ in isoform Neural.		VSP_006738

Sequences

	Sequence		Length	Mass (Da)
	Isoform Cytoplasmic (A) (B) [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 40DAD6FB83163049	FASTA	843	91,153
	10 20 30 40 50 60 MSYMPAQNRT MSHNNQYNPP DLPPMVSAKE QTLMWQQNSY LGDSGIHSGA VTQVPSLSGK 70 80 90 100 110 120 EDEEMEGDPL MFDLDTGFPQ NFTQDQVDDM NQQLSQTRSQ RVRAAMFPET LEEGIEIPST 130 140 150 160 170 180 QFDPQQPTAV QRLSEPSQML KHAVVNLINY QDDAELATRA IPELIKLLND EDQVVVSQAA 190 200 210 220 230 240 MMVHQLSKKE ASRHAIMNSP QMVAALVRAI SNSNDLESTK AAVGTLHNLS HHRQGLLAIF 250 260 270 280 290 300 KSGGIPALVK LLSSPVESVL FYAITTLHNL LLHQDGSKMA VRLAGGLQKM VTLLQRNNVK 310 320 330 340 350 360 FLAIVTDCLQ ILAYGNQESK LIILASGGPN ELVRIMRSYD YEKLLWTTSR VLKVLSVCSS 370 380 390 400 410 420 NKPAIVDAGG MQALAMHLGN MSPRLVQNCL WTLRNLSDAA TKVEGLEALL QSLVQVLGST 430 440 450 460 470 480 DVNVVTCAAG ILSNLTCNNQ RNKATVCQVG GVDALVRTII NAGDREEITE PAVCALRHLT 490 500 510 520 530 540 SRHVDSELAQ NAVRLNYGLS VIVKLLHPPS RWPLIKAVIG LIRNLALCPA NHAPLREHGA 550 560 570 580 590 600 IHHLVRLLMR AFQDTERQRS SIATTGSQQP SAYADGVRME EIVEGTVGAL HILARESHNR 610 620 630 640 650 660 ALIRQQSVIP IFVRLLFNEI ENIQRVAAGV LCELAADKEG AEIIEQEGAT GPLTDLLHSR 670 680 690 700 710 720 NEGVATYAAA VLFRMSEDKP QDYKKRLSIE LTNSLLREDN NIWANADLGM GPDLQDMLGP 730 740 750 760 770 780 EEAYEGLYGQ GPPSVHSSHG GRAFHQQGYD TLPIDSMQGL EISSPVGGGG AGGAPGNGGA 790 800 810 820 830 840 VGGASGGGGN IGAIPPSGAP TSPYSMDMDV GEIDAGALNF DLDAMPTPPN DNNNLAAWYD TDC
	Isoform Neural (C) [UniParc]. Checksum: 0E19594766E0847F	FASTA	721	79,314
	10 20 30 40 50 60 MSYMPAQNRT MSHNNQYNPP DLPPMVSAKE QTLMWQQNSY LGDSGIHSGA VTQVPSLSGK 70 80 90 100 110 120 EDEEMEGDPL MFDLDTGFPQ NFTQDQVDDM NQQLSQTRSQ RVRAAMFPET LEEGIEIPST 130 140 150 160 170 180 QFDPQQPTAV QRLSEPSQML KHAVVNLINY QDDAELATRA IPELIKLLND EDQVVVSQAA 190 200 210 220 230 240 MMVHQLSKKE ASRHAIMNSP QMVAALVRAI SNSNDLESTK AAVGTLHNLS HHRQGLLAIF 250 260 270 280 290 300 KSGGIPALVK LLSSPVESVL FYAITTLHNL LLHQDGSKMA VRLAGGLQKM VTLLQRNNVK 310 320 330 340 350 360 FLAIVTDCLQ ILAYGNQESK LIILASGGPN ELVRIMRSYD YEKLLWTTSR VLKVLSVCSS 370 380 390 400 410 420 NKPAIVDAGG MQALAMHLGN MSPRLVQNCL WTLRNLSDAA TKVEGLEALL QSLVQVLGST 430 440 450 460 470 480 DVNVVTCAAG ILSNLTCNNQ RNKATVCQVG GVDALVRTII NAGDREEITE PAVCALRHLT 490 500 510 520 530 540 SRHVDSELAQ NAVRLNYGLS VIVKLLHPPS RWPLIKAVIG LIRNLALCPA NHAPLREHGA 550 560 570 580 590 600 IHHLVRLLMR AFQDTERQRS SIATTGSQQP SAYADGVRME EIVEGTVGAL HILARESHNR 610 620 630 640 650 660 ALIRQQSVIP IFVRLLFNEI ENIQRVAAGV LCELAADKEG AEIIEQEGAT GPLTDLLHSR 670 680 690 700 710 720 NEGVATYAAA VLFRMSEDKP QDYKKRLSIE LTNSLLREDN NIWANADLGM GPDLQDMILY Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of the armadillo locus: uniformly distributed transcripts and a protein with novel internal repeats are associated with a Drosophila segment polarity gene." Riggleman B., Wieschaus E., Schedl P. Genes Dev. 3:96-113(1989) [PubMed: 2707602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Oregon-R. Tissue: Embryo.
[2]	"Roles of Armadillo, a Drosophila catenin, during central nervous system development." Loureiro J., Peifer M. Curr. Biol. 8:622-632(1998) [PubMed: 9635189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CYTOPLASMIC AND NEURAL), FUNCTION, TISSUE SPECIFICITY. 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. Strain: Berkeley.
[5]	"From sequence to chromosome: the tip of the X chromosome of D. melanogaster." Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M. Science 287:2220-2222(2000) [PubMed: 10731137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oregon-R.
[6]	"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] (ISOFORM CYTOPLASMIC). Strain: Berkeley. Tissue: Embryo.
[7]	"Phosphorylation of the Drosophila adherens junction protein Armadillo: roles for wingless signal and zeste-white 3 kinase." Peifer M., Pai L.-M., Casey M. Dev. Biol. 166:543-556(1994) [PubMed: 7529201] [Abstract] Cited for: PHOSPHORYLATION.
[8]	"Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin." McCartney B.M., Fehon R.G. J. Cell Biol. 133:843-852(1996) [PubMed: 8666669] [Abstract] Cited for: INTERACTION WITH MER AND MOE, SUBCELLULAR LOCATION. Strain: Oregon-R. Tissue: Embryo.
[9]	"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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-650; SER-688 AND SER-694, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X54468 Genomic DNA. Translation: CAA38350.1. AF001213 mRNA. Translation: AAB58731.1. AE014298 Genomic DNA. Translation: AAF45686.2. AE014298 Genomic DNA. Translation: AAF45687.2. AE014298 Genomic DNA. Translation: AAN09064.2. AE014298 Genomic DNA. Translation: AAS65246.1. AL021106, AL021086 Genomic DNA. Translation: CAA15946.1. AL021086, AL021106 Genomic DNA. Translation: CAA15935.1. AY118525 mRNA. Translation: AAM49894.1.
PIR	T12689.
RefSeq	NP_476665.2. NM_057317.3. NP_476666.1. NM_057318.3. NP_599100.1. NM_134273.2. NP_726775.2. NM_166912.2. NP_996328.1. NM_206605.1.
UniGene	Dm.4782.
3D structure databases
ProteinModelPortal	P18824.
SMR	P18824. Positions 30-55, 126-678.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-19968N.
IntAct	P18824. 9 interactions.
MINT	MINT-344131.
STRING	P18824.
Proteomic databases
PRIDE	P18824.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0089988; FBpp0089031; FBgn0000117. FBtr0089989; FBpp0089032; FBgn0000117. FBtr0089991; FBpp0089034; FBgn0000117. FBtr0089992; FBpp0089035; FBgn0000117.
GeneID	31151.
KEGG	dme:Dmel_CG11579.
Organism-specific databases
CTD	31151.
FlyBase	FBgn0000117. arm.
Phylogenomic databases
eggNOG	inNOG06097.
InParanoid	P18824.
OMA	TVCQVGG.
OrthoDB	EOG4WWQ0F.
PhylomeDB	P18824.
Gene expression databases
Bgee	P18824.
GermOnline	CG11579. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000225. Armadillo. IPR013284. Beta-catenin. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 1 hit.
KO	K02105.
Pfam	PF00514. Arm. 4 hits. [Graphical view]
PRINTS	PR01869. BCATNINFAMLY.
SMART	SM00185. ARM. 12 hits. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50176. ARM_REPEAT. 9 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	772169.

Entry information

Entry name

ARM_DROME

Accession

Primary (citable) accession number: P18824
Secondary accession number(s): A4V3V0 , O02371, Q0KHX2, Q8IRW7, Q9W546

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	January 25, 2012
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project