P16621 (LAR_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein phosphatase Lar
EC=3.1.3.48

Alternative name(s):
Protein-tyrosine-phosphate phosphohydrolase
dLAR

Gene names

Name:	Lar
ORF Names:	CG10443

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	2029 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). It controls motor axon guidance. Ref.1 Ref.2
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.1
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Selectively expressed in a subset of axons and pioneer neurons in the embryo. Ref.2
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily. Contains 9 fibronectin type-III domains. Contains 3 Ig-like C2-type (immunoglobulin-like) domains. Contains 2 tyrosine-protein phosphatase domains.
Sequence caution	The sequence AAK93409.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Heparin-binding
Molecular function	Hydrolase Protein phosphatase Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	R7 cell development Inferred from mutant phenotype PubMed 16864797PubMed 18400161PubMed 19889974. Source: FlyBase axon extension Inferred from mutant phenotype PubMed 19766621. Source: FlyBase axon target recognition Inferred from mutant phenotype PubMed 21084592. Source: FlyBase cell adhesion Inferred from mutant phenotype PubMed 14527345. Source: FlyBase embryonic development via the syncytial blastoderm Non-traceable author statement PubMed 11493634. Source: FlyBase motor neuron axon guidance Inferred from mutant phenotype PubMed 16213816Ref.2. Source: FlyBase oogenesis Inferred from mutant phenotype PubMed 12972609. Source: FlyBase photoreceptor cell morphogenesis Inferred from mutant phenotype PubMed 16864797. Source: FlyBase regulation of axon extension involved in axon guidance Inferred from mutant phenotype PubMed 19766621. Source: FlyBase regulation of cell shape Inferred from mutant phenotype PubMed 14527345. Source: FlyBase retinal ganglion cell axon guidance Inferred from mutant phenotype PubMed 16864799. Source: FlyBase synaptic growth at neuromuscular junction Inferred from mutant phenotype PubMed 19889974. Source: FlyBase
Cellular_component	axon Inferred from direct assay PubMed 18237413. Source: FlyBase focal adhesion Inferred from direct assay PubMed 21430143. Source: FlyBase integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Inferred from direct assay PubMed 18433294. Source: FlyBase plasma membrane Inferred from direct assay PubMed 20462449. Source: FlyBase
Molecular_function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor protein tyrosine phosphatase activity Inferred from sequence or structural similarity PubMed 1657402Ref.1. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Abl	P00522	4	EBI-668630,EBI-534090
ena	Q8T4F7	2	EBI-668630,EBI-466810

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Chain

33 – 2029

1997

Tyrosine-protein phosphatase Lar

PRO_0000025431

Regions

Topological domain

33 – 1377

1345

Extracellular Potential

Transmembrane

1378 – 1402

25

Helical; Potential

Topological domain

1403 – 2029

627

Cytoplasmic Potential

Domain

36 – 128

93

Ig-like C2-type 1

Domain

140 – 224

85

Ig-like C2-type 2

Domain

234 – 316

83

Ig-like C2-type 3

Domain

322 – 410

89

Fibronectin type-III 1

Domain

416 – 508

93

Fibronectin type-III 2

Domain

515 – 603

89

Fibronectin type-III 3

Domain

610 – 704

95

Fibronectin type-III 4

Domain

709 – 807

99

Fibronectin type-III 5

Domain

812 – 904

93

Fibronectin type-III 6

Domain

909 – 1002

94

Fibronectin type-III 7

Domain

1006 – 1099

94

Fibronectin type-III 8

Domain

1101 – 1203

103

Fibronectin type-III 9

Domain

1474 – 1729

256

Tyrosine-protein phosphatase 1

Domain

1761 – 2020

260

Tyrosine-protein phosphatase 2

Region

70 – 82

13

Heparin-binding

Region

1670 – 1676

7

Substrate binding By similarity

Sites

Active site

1670

1

Phosphocysteine intermediate By similarity

Active site

1961

1

Phosphocysteine intermediate By similarity

Binding site

1638

1

Substrate By similarity

Binding site

1714

1

Substrate By similarity

Amino acid modifications

Modified residue

1572

1

Phosphothreonine Ref.6

Glycosylation

176

1

N-linked (GlcNAc...) Potential

Glycosylation

253

1

N-linked (GlcNAc...) Potential

Glycosylation

298

1

N-linked (GlcNAc...) Potential

Glycosylation

553

1

N-linked (GlcNAc...) Potential

Glycosylation

616

1

N-linked (GlcNAc...) Potential

Glycosylation

666

1

N-linked (GlcNAc...) Potential

Glycosylation

721

1

N-linked (GlcNAc...) Potential

Glycosylation

774

1

N-linked (GlcNAc...) Potential

Glycosylation

915

1

N-linked (GlcNAc...) Potential

Glycosylation

962

1

N-linked (GlcNAc...) Potential

Glycosylation

1183

1

N-linked (GlcNAc...) Potential

Glycosylation

1304

1

N-linked (GlcNAc...) Potential

Disulfide bond

57 ↔ 111

Ref.7

Disulfide bond

161 ↔ 209

Ref.7

Disulfide bond

256 ↔ 301

Potential

Experimental info

Sequence conflict

480 – 481

2

EL → DV Ref.1

Sequence conflict

480 – 481

2

EL → DV Ref.2

Secondary structure

1

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2029

Helix Strand Turn

Details...

Beta strand

37 – 40

4

Beta strand

45 – 48

4

Beta strand

53 – 60

8

Beta strand

66 – 71

6

Beta strand

83 – 88

6

Turn

89 – 91

3

Beta strand

92 – 99

8

Turn

102 – 104

3

Beta strand

107 – 114

8

Beta strand

116 – 118

3

Beta strand

120 – 130

11

Beta strand

141 – 144

4

Beta strand

149 – 152

4

Beta strand

157 – 159

3

Beta strand

162 – 164

3

Beta strand

170 – 175

6

Beta strand

187 – 190

4

Beta strand

193 – 196

4

Helix

201 – 203

3

Beta strand

205 – 213

9

Beta strand

216 – 219

4

Beta strand

223 – 228

6

Sequences

	Sequence		Length	Mass (Da)
	P16621 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: DF1F676A94050F2B	FASTA	2,029	229,056
	10 20 30 40 50 60 MGLQMTAARP IAALSLLVLS LLTWTHPTIV DAAHPPEIIR KPQNQGVRVG GVASFYCAAR 70 80 90 100 110 120 GDPPPSIVWR KNGKKVSGTQ SRYTVLEQPG GISILRIEPV RAGRDDAPYE CVAENGVGDA 130 140 150 160 170 180 VSADATLTIY EGDKTPAGFP VITQGPGTRV IEVGHTVLMT CKAIGNPTPN IYWIKNQTKV 190 200 210 220 230 240 DMSNPRYSLK DGFLQIENSR EEDQGKYECV AENSMGTEHS KATNLYVKVR RVPPTFSRPP 250 260 270 280 290 300 ETISEVMLGS NLNLSCIAVG SPMPHVKWMK GSEDLTPENE MPIGRNVLQL INIQESANYT 310 320 330 340 350 360 CIAASTLGQI DSVSVVKVQS LPTAPTDVQI SEVTATSVRL EWSYKGPEDL QYYVIQYKPK 370 380 390 400 410 420 NANQAFSEIS GIITMYYVVR ALSPYTEYEF YVIAVNNIGR GPPSAPATCT TGETKMESAP 430 440 450 460 470 480 RNVQVRTLSS STMVITWEPP ETPNGQVTGY KVYYTTNSNQ PEASWNSQMV DNSELTTVSE 490 500 510 520 530 540 LTPHAIYTVR VQAYTSMGAG PMSTPVQVKA QQGVPSQPSN FRATDIGETA VTLQWTKPTH 550 560 570 580 590 600 SSENIVHYEL YWNDTYANQA HHKRISNSEA YTLDGLYPDT LYYIWLAARS QRGEGATTPP 610 620 630 640 650 660 IPVRTKQYVP GAPPRNITAI ATSSTTISLS WLPPPVERSN GRIIYYKVFF VEVGREDDEA 670 680 690 700 710 720 TTMTLNMTSI VLDELKRWTE YKIWVLAGTS VGDGPRSHPI ILRTQEDVPG DPQDVKATPL 730 740 750 760 770 780 NSTSIHVSWK PPLEKDRNGI IRGYHIHAQE LRDEGKGFLN EPFKFDVVDT LEFNVTGLQP 790 800 810 820 830 840 DTKYSIQVAA LTRKGDGDRS AAIVVKTPGG VPVRPTVSLK IMEREPIVSI ELEWERPAQT 850 860 870 880 890 900 YGELRGYRLR WGVKDQALKE EMLSGPQMTK KRFDNLERGV EYEFRVAGSN HIGIGQETVK 910 920 930 940 950 960 IFQTPEGTPG GPPSNITIRF QTPDVLCVTW DPPTREHRNG IITRYDVQFH KKIDHGLGSE 970 980 990 1000 1010 1020 RNMTLRKAVF TNLEENTEYI FRVRAYTKQG AGPFSDKLIV ETERDMGRAP MSLQAEATSE 1030 1040 1050 1060 1070 1080 QTAEIWWEPV TSRGKLLGYK IFYTMTAVED LDDWQTKTVG LTESADLVNL EKFAQYAVAI 1090 1100 1110 1120 1130 1140 AARFKNGLGR LSEKVTVRIK PEDVPLNLRA HDVSTHSMTL SWSPPIRLTP VNYKISFDAM 1150 1160 1170 1180 1190 1200 KVFVDSQGFS QTQIVPKREI ILKHYVKTHT INELSPFTTY NVNVSAIPSD YSYRPPTKIT 1210 1220 1230 1240 1250 1260 VTTQMAAPQP MVKPDFYGVV NGEEILVILP QASEEYGPIS HYYLVVVPED KSNLHKIPDQ 1270 1280 1290 1300 1310 1320 FLTDDLLPGR NKPERPNAPY IAAKFPQRSI PFTFHLGSGD DYHNFTNRKL EREKRYRIFV 1330 1340 1350 1360 1370 1380 RAVVDTPQKH LYTSSPFSEF LSLDMREAPP GERPHRPDPN WPAEPEVSVN RNKDEPEILW 1390 1400 1410 1420 1430 1440 VVLPLMVSTF IVSTALIVLC VVKRRRQPCK TPDQAAVTRP LMAADLGAGP TPSDPVDMRR 1450 1460 1470 1480 1490 1500 LNFQTPGMIS HPPIPISEFA NHIERLKSND NQKFSQEYES IEPGQQFTWD NSNLEHNKSK 1510 1520 1530 1540 1550 1560 NRYANVTAYD HSRVQLPAVE GVVGSDYINA NYCDGYRKHN AYVATQGPLQ ETFVDFWRMC 1570 1580 1590 1600 1610 1620 WELKTATIVM MTRLEERTRI KCDQYWPTRG TETYGQIFVT ITETQELATY SIRTFQLCRQ 1630 1640 1650 1660 1670 1680 GFNDRREIKQ LQFTAWPDHG VPDHPAPFLQ FLRRCRALTP PESGPVIVHC SAGVGRTGCY 1690 1700 1710 1720 1730 1740 IVIDSMLERM KHEKIIDIYG HVTCLRAQRN YMVQTEDQYI FIHDAILEAI ICGVTEVPAR 1750 1760 1770 1780 1790 1800 NLHTHLQKLL ITEPGETISG MEVEFKKLSN VKMDSSKFVT ANLPCNKHKN RLVHILPYES 1810 1820 1830 1840 1850 1860 SRVYLTPIHG IEGSDYVNAS FIDGYRYRSA YIAAQGPVQD AAEDFWRMLW EHNSTIVVML 1870 1880 1890 1900 1910 1920 TKLKEMGREK CFQYWPHERS VRYQYYVVDP IAEYNMPQYK LREFKVTDAR DGSSRTVRQF 1930 1940 1950 1960 1970 1980 QFIDWPEQGV PKSGEGFIDF IGQVHKTKEQ FGQDGPITVH CSAGVGRSGV FITLSIVLER 1990 2000 2010 2020 MQYEGVLDVF QTVRILRSQR PAMVQTEDQY HFCYRAALEY LGSFDNYTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila." Streuli M., Krueger N.X., Tsai A.Y.M., Saito H. Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
[2]	"The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila." Krueger N.X., van Vactor D., Wan H.I., Gelbart W.M., Goodman C.S., Saito H. Cell 84:611-622(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY. Strain: Canton-S.
[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] [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. , 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. 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] OF 428-2029. Strain: Berkeley. Tissue: Embryo.
[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 THR-1572, MASS SPECTROMETRY. Tissue: Embryo.
[7]	"The immunoglobulin-like domains 1 and 2 of the protein tyrosine phosphatase LAR adopt an unusual horseshoe-like conformation." Biersmith B.H., Hammel M., Geisbrecht E.R., Bouyain S. J. Mol. Biol. 408:616-627(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 32-237, HEPARIN-BINDING REGION, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M27700 mRNA. Translation: AAA28668.1.
U36857 , U36849, U36850, U36851, U36852, U36853, U36854, U36855, U36856 Genomic DNA. Translation: AAC47002.1.
AE014134 Genomic DNA. Translation: AAF53837.3.
AY051985 mRNA. Translation: AAK93409.1. Different initiation.

PIR

TDFFLK. A36182.

RefSeq

NP_523604.2. NM_078880.3.

UniGene

Dm.24416.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YD1	X-ray	1.80	A	33-232	[»]
3PXJ	X-ray	2.30	A/B/C/D	32-237	[»]

ProteinModelPortal

P16621.

SMR

P16621. Positions 32-1010, 1448-2024.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38648N.

IntAct

P16621. 2 interactions.

Proteomic databases

PaxDb

P16621.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0081260; FBpp0080801; FBgn0000464.

GeneID

35259.

KEGG

dme:Dmel_CG10443.

UCSC

CG10443-RA. d. melanogaster.

Organism-specific databases

CTD

104121.

FlyBase

FBgn0000464. Lar.

Phylogenomic databases

eggNOG

COG5599.

GeneTree

ENSGT00590000082937.

InParanoid

P16621.

KO

K05695.

OrthoDB

EOG444J14.

PhylomeDB

P16621.

Gene expression databases

Bgee

P16621.

GermOnline

CG10443. Drosophila melanogaster.

Family and domain databases

Gene3D

2.60.40.10. 12 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF00041. fn3. 9 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]

PRINTS

PR00700. PRTYPHPHTASE.

SMART

SM00060. FN3. 9 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 9 hits.

PROSITE

PS50853. FN3. 9 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P16621.

GenomeRNAi

35259.

NextBio

792660.

Entry information

Entry name

LAR_DROME

Accession

Primary (citable) accession number: P16621
Secondary accession number(s): Q960M3, Q9VIS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 30, 2005
Last modified:	May 1, 2013
This is version 147 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project