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P08953 (TOLL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length1097 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo. Promotes heterophilic cellular adhesion. Spz C-106 in the hemolymph controls expression of the antifungal peptide Drosomycin (Drs) by acting as a ligand of Tl and inducing an intracellular signaling pathway. Ref.1 Ref.7 Ref.8 Ref.9

Subunit structure

Homodimer; disulfide-linked.

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Developmental stage

Expressed both maternally and zygotically. Ref.1

Sequence similarities

Belongs to the Toll-like receptor family.

Contains 18 LRR (leucine-rich) repeats.

Contains 2 LRRCT domains.

Contains 1 LRRNT domain.

Contains 1 TIR domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processToll signaling pathway

Non-traceable author statement PubMed 10449356. Source: FlyBase

antifungal humoral response

Inferred from mutant phenotype Ref.8. Source: FlyBase

antimicrobial humoral response

Inferred from genetic interaction Ref.8. Source: FlyBase

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

defense response

Traceable author statement PubMed 10793472. Source: FlyBase

defense response to Gram-positive bacterium

Traceable author statement PubMed 12888789PubMed 14557290PubMed 15199954. Source: FlyBase

defense response to fungus

Traceable author statement PubMed 12888789PubMed 14557290PubMed 15032585PubMed 15199954. Source: FlyBase

dorsal/ventral axis specification

Inferred from mutant phenotype PubMed 16782008. Source: FlyBase

embryonic pattern specification

Traceable author statement PubMed 11283698. Source: FlyBase

heart development

Inferred from mutant phenotype PubMed 15870289. Source: FlyBase

hemocyte proliferation

Inferred from mutant phenotype PubMed 15882582. Source: FlyBase

hemopoiesis

Traceable author statement PubMed 10793472. Source: FlyBase

immune response

Traceable author statement PubMed 10878576PubMed 11135568PubMed 11252751. Source: FlyBase

innate immune response

Inferred from direct assay PubMed 18583479. Source: FlyBase

mitotic cytokinesis

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

positive regulation of antibacterial peptide biosynthetic process

Inferred from mutant phenotype PubMed 9405661. Source: FlyBase

positive regulation of antifungal peptide biosynthetic process

Inferred from mutant phenotype PubMed 10369678PubMed 9405661. Source: FlyBase

regulation of hemocyte differentiation

Inferred from mutant phenotype PubMed 15381778. Source: FlyBase

response to bacterium

Non-traceable author statement PubMed 12530956. Source: FlyBase

response to fungus

Traceable author statement PubMed 11104525PubMed 11283698. Source: FlyBase

synapse assembly

Inferred from mutant phenotype PubMed 10699982. Source: FlyBase

synaptic target inhibition

Inferred from mutant phenotype PubMed 20504957. Source: FlyBase

zygotic specification of dorsal/ventral axis

Non-traceable author statement PubMed 15199954. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 20921412. Source: FlyBase

early endosome

Inferred from direct assay PubMed 20921412. Source: FlyBase

external side of plasma membrane

Inferred from direct assay PubMed 22464169. Source: FlyBase

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 20404143. Source: FlyBase

protein complex

Inferred from physical interaction PubMed 18347020. Source: FlyBase

   Molecular_functionTIR domain binding

Inferred from physical interaction PubMed 11743586. Source: FlyBase

cytokine binding

Traceable author statement PubMed 12888789. Source: FlyBase

identical protein binding

Inferred from physical interaction PubMed 15197269PubMed 23827685. Source: IntAct

protein binding

Inferred from physical interaction PubMed 16782008. Source: UniProtKB

transmembrane signaling receptor activity

Non-traceable author statement PubMed 10449356. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-143610,EBI-143610
Myd88Q7K1053EBI-143610,EBI-129988

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 10971070Protein toll
PRO_0000034740

Regions

Topological domain28 – 807780Extracellular Potential
Transmembrane808 – 82821Helical; Potential
Topological domain829 – 1097269Cytoplasmic Potential
Repeat175 – 19521LRR 1
Repeat198 – 21922LRR 2
Repeat222 – 24322LRR 3
Repeat246 – 26722LRR 4
Repeat270 – 29122LRR 5
Repeat294 – 31421LRR 6
Repeat320 – 34021LRR 7
Repeat343 – 36422LRR 8
Repeat367 – 38822LRR 9
Repeat391 – 41222LRR 10
Repeat415 – 43622LRR 11
Repeat439 – 46022LRR 12
Repeat474 – 49522LRR 13
Repeat498 – 52124LRR 14
Repeat523 – 54422LRR 15
Domain561 – 62060LRRCT 1
Domain622 – 66342LRRNT
Repeat669 – 69022LRR 16
Repeat693 – 71321LRR 17
Repeat715 – 73824LRR 18
Domain751 – 80151LRRCT 2
Domain857 – 996140TIR

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation1751N-linked (GlcNAc...) Potential
Glycosylation2351N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation3461N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential
Glycosylation5081N-linked (GlcNAc...) Potential
Glycosylation5281N-linked (GlcNAc...) Potential
Glycosylation6541N-linked (GlcNAc...) Potential
Glycosylation6771N-linked (GlcNAc...) Potential
Glycosylation7031N-linked (GlcNAc...) Potential
Glycosylation7151N-linked (GlcNAc...) Potential
Glycosylation7301N-linked (GlcNAc...) Potential
Glycosylation7381N-linked (GlcNAc...) Potential

Natural variations

Natural variant981E → G in strain: MelZim6.
Natural variant2181G → S in strain: MelZim7.
Natural variant2451T → S in strain: MelZim3.
Natural variant3901T → I in strain: MelZim3 and MelZim7.
Natural variant4141G → A in strain: MelZim3.
Natural variant4351V → L in strain: MelZim8.
Natural variant4601M → T in strain: MelZim6.
Natural variant4711Y → D in strain: MelZim1, MelZim4, MelZim5 and MelZim6.
Natural variant4861I → R in strain: MelZim6.
Natural variant5131G → R in strain: MelZim1, MelZim5 and MelZim6.
Natural variant5381A → E in strain: MelZim1, MelZim5 and MelZim6.
Natural variant5441H → Y in strain: MelZim1, MelZim5 and MelZim6.
Natural variant5681T → M in strain: MelZim1, MelZim5 and MelZim6.
Natural variant5921T → A in strain: MelZim6.
Natural variant6031L → M in strain: MelZim1, MelZim5 and MelZim6.
Natural variant6811L → V in strain: MelZim1, MelZim3, MelZim4, MelZim5, MelZim6 and MelZim7.
Natural variant7141T → I in strain: MelZim5 and MelZim8.
Natural variant7321T → S in strain: MelZim8.
Natural variant7411M → I in strain: MelZim1.

Experimental info

Sequence conflict3551K → S in AAQ64932. Ref.5
Sequence conflict3551K → S in AAQ64933. Ref.5
Sequence conflict3551K → S in AAQ64934. Ref.5
Sequence conflict3551K → S in AAQ64935. Ref.5
Sequence conflict3551K → S in AAQ64936. Ref.5
Sequence conflict3551K → S in AAQ64937. Ref.5
Sequence conflict3551K → S in AAQ64938. Ref.5
Sequence conflict6021V → A in AAQ64933. Ref.5
Sequence conflict6021V → A in AAQ64934. Ref.5
Sequence conflict6021V → A in AAQ64937. Ref.5
Sequence conflict6021V → A in AAQ64938. Ref.5
Sequence conflict7861M → I in ABX00775. Ref.4
Sequence conflict8251A → T in ABX00775. Ref.4

Secondary structure

............................................................................................................................................... 1097
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08953 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: D1BFC42245E3EABE

FASTA1,097124,656
        10         20         30         40         50         60 
MSRLKAASEL ALLVIILQLL QWPGSEASFG RDACSEMSID GLCQCAPIMS EYEIICPANA 

        70         80         90        100        110        120 
ENPTFRLTIQ PKDYVQIMCN LTDTTDYQQL PKKLRIGEVD RVQMRRCMLP GHTPIASILD 

       130        140        150        160        170        180 
YLGIVSPTTL IFESDNLGMN ITRQHLDRLH GLKRFRFTTR RLTHIPANLL TDMRNLSHLE 

       190        200        210        220        230        240 
LRANIEEMPS HLFDDLENLE SIEFGSNKLR QMPRGIFGKM PKLKQLNLWS NQLHNLTKHD 

       250        260        270        280        290        300 
FEGATSVLGI DIHDNGIEQL PHDVFAHLTN VTDINLSANL FRSLPQGLFD HNKHLNEVRL 

       310        320        330        340        350        360 
MNNRVPLATL PSRLFANQPE LQILRLRAEL QSLPGDLFEH STQITNISLG DNLLKTLPAT 

       370        380        390        400        410        420 
LLEHQVNLLS LDLSNNRLTH LPDSLFAHTT NLTDLRLEDN LLTGISGDIF SNLGNLVTLV 

       430        440        450        460        470        480 
MSRNRLRTID SRAFVSTNGL RHLHLDHNDI DLQQPLLDIM LQTQINSPFG YMHGLLTLNL 

       490        500        510        520        530        540 
RNNSIIFVYN DWKNTMLQLR ELDLSYNNIS SLGYEDLAFL SQNRLHVNMT HNKIRRIALP 

       550        560        570        580        590        600 
EDVHLGEGYN NNLVHVDLND NPLVCDCTIL WFIQLVRGVH KPQYSRQFKL RTDRLVCSQP 

       610        620        630        640        650        660 
NVLEGTPVRQ IEPQTLICPL DFSDDPRERK CPRGCNCHVR TYDKALVINC HSGNLTHVPR 

       670        680        690        700        710        720 
LPNLHKNMQL MELHLENNTL LRLPSANTPG YESVTSLHLA GNNLTSIDVD QLPTNLTHLD 

       730        740        750        760        770        780 
ISWNHLQMLN ATVLGFLNRT MKWRSVKLSG NPWMCDCTAK PLLLFTQDNF ERIGDRNEMM 

       790        800        810        820        830        840 
CVNAEMPTRM VELSTNDICP AEKGVFIALA VVIALTGLLA GFTAALYYKF QTEIKIWLYA 

       850        860        870        880        890        900 
HNLLLWFVTE EDLDKDKKFD AFISYSHKDQ SFIEDYLVPQ LEHGPQKFQL CVHERDWLVG 

       910        920        930        940        950        960 
GHIPENIMRS VADSRRTIIV LSQNFIKSEW ARLEFRAAHR SALNEGRSRI IVIIYSDIGD 

       970        980        990       1000       1010       1020 
VEKLDEELKA YLKMNTYLKW GDPWFWDKLR FALPHRRPVG NIGNGALIKT ALKGSTDDKL 

      1030       1040       1050       1060       1070       1080 
ELIKPSPVTP PLTTPPAEAT KNPLVAQLNG VTPHQAIMIA NGKNGLTNLY TPNGKSHGNG 

      1090 
HINGAFIINT NAKQSDV 

« Hide

References

« Hide 'large scale' references
[1]"The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein."
Hashimoto C., Hudson K.L., Anderson K.V.
Cell 52:269-279(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
[2]"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.
[3]"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.
Strain: Berkeley.
[4]Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Natural selection drives Drosophila immune system evolution."
Schlenke T.A., Begun D.J.
Genetics 164:1471-1480(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-1097, VARIANTS.
Strain: MelZim1, MelZim3, MelZim4, MelZim5, MelZim6, MelZim7 and MelZim8.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-1097.
Strain: Berkeley.
Tissue: Head.
[7]"The Drosophila membrane receptor Toll can function to promote cellular adhesion."
Keith F.J., Gay N.J.
EMBO J. 9:4299-4306(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults."
Lemaitre B., Nicolas E., Michaut L., Reichhart J.-M., Hoffmann J.A.
Cell 86:973-983(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Binding of the Drosophila cytokine Spatzle to Toll is direct and establishes signaling."
Weber A.N., Tauszig-Delamasure S., Hoffmann J.A., Lelievre E., Gascan H., Ray K.P., Morse M.A., Imler J.L., Gay N.J.
Nat. Immunol. 4:794-800(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19969 mRNA. Translation: AAA28941.1.
AE014297 Genomic DNA. Translation: AAF56624.1.
AE014297 Genomic DNA. Translation: AAN14086.1.
BT031153 mRNA. Translation: ABX00775.1.
AY349649 Genomic DNA. Translation: AAQ64932.1.
AY349650 Genomic DNA. Translation: AAQ64933.1.
AY349651 Genomic DNA. Translation: AAQ64934.1.
AY349652 Genomic DNA. Translation: AAQ64935.1.
AY349653 Genomic DNA. Translation: AAQ64936.1.
AY349654 Genomic DNA. Translation: AAQ64937.1.
AY349655 Genomic DNA. Translation: AAQ64938.1.
AY121616 mRNA. Translation: AAM51943.1.
PIRA29943.
RefSeqNP_524518.1. NM_079794.2.
NP_733166.1. NM_170287.2.
UniGeneDm.2347.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4ARNX-ray2.41A/B/C/D28-228[»]
4ARRX-ray3.00A/B28-228[»]
4BV4X-ray2.35R28-397[»]
4LXRX-ray2.20A28-802[»]
4LXSX-ray3.30A28-802[»]
ProteinModelPortalP08953.
SMRP08953. Positions 28-993.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68116. 10 interactions.
DIPDIP-34358N.
IntActP08953. 3 interactions.
STRING7227.FBpp0084431.

Proteomic databases

PaxDbP08953.
PRIDEP08953.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085059; FBpp0084431; FBgn0262473.
FBtr0330155; FBpp0303188; FBgn0262473.
GeneID43222.
KEGGdme:Dmel_CG5490.

Organism-specific databases

CTD109651.
FlyBaseFBgn0262473. Tl.

Phylogenomic databases

eggNOGCOG4886.
GeneTreeENSGT00710000106753.
InParanoidP08953.
OrthoDBEOG761BT1.
PhylomeDBP08953.

Gene expression databases

BgeeP08953.

Family and domain databases

Gene3D3.40.50.10140. 1 hit.
InterProIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR000157. TIR_dom.
[Graphical view]
PfamPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 2 hits.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMSSF52200. SSF52200. 1 hit.
PROSITEPS51450. LRR. 13 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTl. drosophila.
GenomeRNAi43222.
NextBio832799.
PROP08953.

Entry information

Entry nameTOLL_DROME
AccessionPrimary (citable) accession number: P08953
Secondary accession number(s): A4V3G7 expand/collapse secondary AC list , A8WHK7, Q8MRF3, Q9VBB8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: July 9, 2014
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

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