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Q9U1K1 (SPIR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein spire
Gene names
Name:spir
Synonyms:p150-Spir
ORF Names:CG10076
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1020 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton. Ref.1 Ref.2 Ref.7 Ref.10 Ref.11

Subunit structure

Interacts with bsk, Rho1, Rac1, Cdc42 and wash. Interacts with capu. Ref.1 Ref.2 Ref.9 Ref.10

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note: Punctate spots in perinuclear region and cytoplasm. Ref.2 Ref.10

Developmental stage

Expressed both maternally and zygotically. Ref.1

Domain

Binds to actin monomers via the WH2 domain. Ref.1

The Spir-box targets binding to intracellular membrane structures By similarity. UniProtKB Q08AE8

Post-translational modification

Phosphorylated by Jnk kinase (bsk). Ref.2

Disruption phenotype

Flies display premature microtubule-dependent cytoplasmic streaming; failure in the orientation of microtubule plus ends towards the posterior pole. Ref.1

Sequence similarities

Belongs to the spire family.

Contains 1 KIND domain.

Contains 2 WH2 domains.

RNA editing

Edited at position 734.
Partially edited. Target of Adar. Ref.5 Ref.8

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
RNA editing
   DomainRepeat
   LigandActin-binding
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Traceable author statement PubMed 12877999. Source: FlyBase

actin filament network formation

Inferred from mutant phenotype PubMed 24089467. Source: FlyBase

actin filament organization

Inferred from mutant phenotype PubMed 17925229. Source: FlyBase

actin filament-based process

Inferred from direct assay PubMed 16518391. Source: FlyBase

actin nucleation

Inferred from direct assay PubMed 16518391. Source: FlyBase

chorion-containing eggshell formation

Inferred from mutant phenotype PubMed 1783295. Source: FlyBase

karyosome formation

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

oogenesis

Inferred from mutant phenotype PubMed 24089467. Source: FlyBase

pole plasm RNA localization

Inferred from mutant phenotype PubMed 2151612. Source: FlyBase

pole plasm assembly

Inferred from mutant phenotype PubMed 1783295PubMed 2151612. Source: FlyBase

pole plasm oskar mRNA localization

Traceable author statement PubMed 11700288. Source: FlyBase

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of cytoskeleton organization

Inferred from direct assay Ref.9. Source: FlyBase

vesicle-mediated transport

Traceable author statement PubMed 12877999. Source: FlyBase

   Cellular_componentcell cortex

Inferred from direct assay PubMed 16518391PubMed 24089467. Source: FlyBase

cytoplasm

Inferred from direct assay PubMed 16518391. Source: FlyBase

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionactin binding

Traceable author statement PubMed 11700288. Source: FlyBase

microtubule binding

Inferred from mutant phenotype PubMed 16518391. Source: FlyBase

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A Ref.2 (identifier: Q9U1K1-1)

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 B Ref.1 (identifier: Q9U1K1-2)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     585-614: MEPAKQVPPPEEPSFTKDEYHKFYDTALES → T
Isoform C Ref.3 (identifier: Q9U1K1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-96: TEHQAEEQAD...EQCVTLHDIL → EARPAKRSTA...KPRQAIRSSK
     97-491: Missing.
Note: No experimental confirmation available.
Isoform D Ref.1 (identifier: Q9U1K1-4)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     338-338: Missing.
     585-586: ME → SI
     587-1020: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10201020Protein spire
PRO_0000309573

Regions

Domain90 – 327238KIND
Domain399 – 41719WH2 1
Domain463 – 48018WH2 2
Region705 – 72521Spir-box
Compositional bias205 – 22016His-rich
Compositional bias792 – 87786Ser-rich

Natural variations

Alternative sequence2 – 9695TEHQA…LHDIL → EARPAKRSTAASVFRSHHMP RESDLVDIGSDASLYCGSDG ESSQAQSTSTSTPNPQTSSD QDLDQPQPTPRAAPRASASN NPPTPKPRQAIRSSK in isoform C. Ref.3
VSP_052599
Alternative sequence97 – 491395Missing in isoform C. Ref.3
VSP_052600
Alternative sequence3381Missing in isoform D. Ref.1
VSP_052601
Alternative sequence585 – 61430MEPAK…TALES → T in isoform B. Ref.1
VSP_052602
Alternative sequence585 – 5862ME → SI in isoform D. Ref.1
VSP_052603
Alternative sequence587 – 1020434Missing in isoform D. Ref.1
VSP_052604
Natural variant7341K → R in RNA edited version. Ref.8

Experimental info

Mutagenesis2321Y → K: Abolishes interaction with capu. Ref.10
Sequence conflict531L → M in AAF23615. Ref.1
Sequence conflict531L → M in AAF23616. Ref.1
Sequence conflict8851V → A in AAF23615. Ref.1

Secondary structure

....... 1020
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 010CD024F9ABC078

FASTA1,020114,867
        10         20         30         40         50         60 
MTEHQAEEQA DTPPTKVKAT PTPTPSGKFK DAKEDAFLST SPDSANGDAQ HKLPADQLAM 

        70         80         90        100        110        120 
SSSAHPQQAG QARPLILQAF HRCSSPEQCV TLHDILDSFK APLSEDQAWA LIHQFAGLYH 

       130        140        150        160        170        180 
QVAVQAHTCA ADYEAALPTG FELHFHRDGS VHFSGPDQLT PKEQLQQEQI PLPPQHDVIV 

       190        200        210        220        230        240 
DQPDHSASSS GDSSVINRAF DNSNHHHHHQ HHHPPLVVSH RKIISELAEI VYTALDYNLP 

       250        260        270        280        290        300 
EDEECQVSQE LENLFNFMTA DETDDDCIDE GIDEGDKRWD DESEEERNDT KELEHIIETC 

       310        320        330        340        350        360 
RNHIKTTLPE NHYRAVCRAL VTETIELRVF LQQVLNNEAG AEKLIKASES SATTQQELAK 

       370        380        390        400        410        420 
LGFNDWARFW VQVIDELRRG VRLKKSNHER TPIEYELTPY EILMGDIRAK KYQLRKVMVN 

       430        440        450        460        470        480 
GDIPPRVKKD AHAMILEFIR SRPPLKKASD RQLGPPRMCE PSPREQLMES IRKGKELKQI 

       490        500        510        520        530        540 
TPPEAPTLRE RVLPSANSTL SRSRQRLIKV DFSKFQDDDL FYDENSISSS HSTAATHQHH 

       550        560        570        580        590        600 
PHFAEMHRCS QPKMPPYPFG GYMVPSQARQ DCRETASLMR PRRTMEPAKQ VPPPEEPSFT 

       610        620        630        640        650        660 
KDEYHKFYDT ALESYDLATQ CESRRASLRR HTIVGCQSNL DETHSMPPTR PESRQSDDVS 

       670        680        690        700        710        720 
KETPKRSPAE QTHPSDEGSS TSSLGPWNKS FMDKQTWMER GDDRLSVTLA EIVHIRSVMT 

       730        740        750        760        770        780 
KAELEGLPMD VRVKEDVEKR RVCFLCLRTR FSFFGPWGIQ CKLCQRTVCA KCYTKMRIPS 

       790        800        810        820        830        840 
EHFRNVPLVL ISPSLLSSPA SSSTPSPSHH AQQAHSSSTG NIMDDQFPKS LIERLLRSES 

       850        860        870        880        890        900 
DRKTRSTVGS APSSPKHQRS NMSTPGISVG PGASSSSAAA TGQAVEALHD QATMSSSYSA 

       910        920        930        940        950        960 
AMRPSGVHQQ QKQHYNNAMS RSMEGPRSLP VHSPAYRPLS NNSTLERKSR FSRGFNLFSS 

       970        980        990       1000       1010       1020 
GSHLAQTQEQ KENLRGEQVT VCNDCQGLVN EITSSVKQKR SSARNRTIQN LTLDLTPVWK 

« Hide

Isoform B (Long) [UniParc].

Checksum: 5A39B9F07136E212
Show »

FASTA991111,475
Isoform C [UniParc].

Checksum: 6B020E5746568D77
Show »

FASTA62569,401
Isoform D (Short) [UniParc].

Checksum: 8F2F09E9AB96CF7F
Show »

FASTA58566,418

References

« Hide 'large scale' references
[1]"Spire contains actin binding domains and is related to ascidian posterior end mark-5."
Wellington A., Emmons S., James B., Calley J., Grover M., Tolias P., Manseau L.
Development 126:5267-5274(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND D), FUNCTION, INTERACTION WITH RHO1; RAC1 AND CDC42, DEVELOPMENTAL STAGE, ACTIN-BINDING, DISRUPTION PHENOTYPE.
Tissue: Ovary.
[2]"The p150-Spir protein provides a link between c-Jun N-terminal kinase function and actin reorganization."
Otto I.M., Raabe T., Rennefahrt U.E.E., Bork P., Rapp U.R., Kerkhoff E.
Curr. Biol. 10:345-348(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH BSK, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Tissue: Embryo.
[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] [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. 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, ALTERNATIVE SPLICING.
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] (ISOFORMS C AND D), RNA EDITING OF POSITION 734.
Strain: Berkeley.
Tissue: Embryo and Head.
[6]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-1020 (ISOFORM B).
Strain: Berkeley.
Tissue: Embryo.
[7]"Drosophila Spire is an actin nucleation factor."
Quinlan M.E., Heuser J.E., Kerkhoff E., Mullins R.D.
Nature 433:382-388(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"RNA editing in Drosophila melanogaster: new targets and functional consequences."
Stapleton M., Carlson J.W., Celniker S.E.
RNA 12:1922-1932(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA EDITING OF POSITION 734.
[9]"Wash functions downstream of Rho and links linear and branched actin nucleation factors."
Liu R., Abreu-Blanco M.T., Barry K.C., Linardopoulou E.V., Osborn G.E., Parkhurst S.M.
Development 136:2849-2860(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WASH.
[10]"Structure and function of the interacting domains of Spire and Fmn-family formins."
Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W., Quinlan M.E., Eck M.J.
Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CAPU, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-232.
[11]"Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation."
Ducka A.M., Joel P., Popowicz G.M., Trybus K.M., Schleicher M., Noegel A.A., Huber R., Holak T.A., Sitar T.
Proc. Natl. Acad. Sci. U.S.A. 107:11757-11762(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 448-485 IN COMPLEX WITH ACTIN, FUNCTION.
[12]"Multiple forms of Spire-actin complexes and their functional consequences."
Chen C.K., Sawaya M.R., Phillips M.L., Reisler E., Quinlan M.E.
J. Biol. Chem. 287:10684-10692(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 428-485 IN COMPLEX WITH ACTIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF184975 mRNA. Translation: AAF23615.1.
AF184976 mRNA. Translation: AAF23616.1.
AJ238876 mRNA. Translation: CAB62901.1.
AE014134 Genomic DNA. Translation: AAF53884.2.
AE014134 Genomic DNA. Translation: AAN11070.1.
AE014134 Genomic DNA. Translation: AAN11071.1.
AE014134 Genomic DNA. Translation: AAN11072.2.
AY075586 mRNA. Translation: AAL68390.1.
AY089503 mRNA. Translation: AAL90241.1.
BT016094 mRNA. Translation: AAV36979.1.
RefSeqNP_001246102.1. NM_001259173.1.
NP_524854.2. NM_080115.3.
NP_724254.1. NM_165323.2.
NP_724255.1. NM_165324.2.
NP_724256.2. NM_165325.2.
UniGeneDm.3356.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MMVX-ray2.80X429-447[»]
3MN5X-ray1.50S448-485[»]
3MN6X-ray2.00X/Y/Z397-415[»]
3MN7X-ray2.00S441-479[»]
3UE5X-ray2.76B428-485[»]
4EFHX-ray2.48B428-485[»]
ProteinModelPortalQ9U1K1.
SMRQ9U1K1. Positions 85-332, 706-777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid69994. 13 interactions.
DIPDIP-17301N.
IntActQ9U1K1. 3 interactions.
MINTMINT-295231.

Proteomic databases

PaxDbQ9U1K1.
PRIDEQ9U1K1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0081352; FBpp0080884; FBgn0003475. [Q9U1K1-1]
GeneID45931.
KEGGdme:Dmel_CG10076.
UCSCCG10076-RA. d. melanogaster. [Q9U1K1-1]

Organism-specific databases

CTD45931.
FlyBaseFBgn0003475. spir.

Phylogenomic databases

eggNOGNOG69783.
GeneTreeENSGT00390000003058.
InParanoidQ9U1K1.
KOK02098.
OMAWALIYQF.
OrthoDBEOG7F511H.
PhylomeDBQ9U1K1.

Gene expression databases

BgeeQ9U1K1.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR011019. KIND.
IPR003124. WH2_dom.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTSM00750. KIND. 1 hit.
SM00246. WH2. 2 hits.
[Graphical view]
SUPFAMSSF57903. SSF57903. 2 hits.
PROSITEPS51377. KIND. 1 hit.
PS51082. WH2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSspir. drosophila.
EvolutionaryTraceQ9U1K1.
GenomeRNAi45931.
NextBio838510.
PROQ9U1K1.

Entry information

Entry nameSPIR_DROME
AccessionPrimary (citable) accession number: Q9U1K1
Secondary accession number(s): Q5U0Z8 expand/collapse secondary AC list , Q8INV3, Q8INV4, Q8INV5, Q8SXP3, Q8T8P8, Q9U4F0, Q9U4F1, Q9VIN3, Q9VIN4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 107 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