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P16621 (LAR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. 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 namesRecommended 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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length2029 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCell adhesion
   Cellular componentMembrane
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandHeparin-binding
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processR7 cell development

Inferred from mutant phenotype PubMed 16864797PubMed 18400161PubMed 19889974. Source: FlyBase

axon extension

Inferred from mutant phenotype PubMed 19766621. Source: FlyBase

axon guidance

Inferred from mutant phenotype PubMed 18516287PubMed 19766621PubMed 19889974Ref.2. 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

nervous system development

Inferred from mutant phenotype PubMed 12972609. Source: FlyBase

oogenesis

Inferred from mutant phenotype PubMed 12972609. Source: FlyBase

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.1. Source: GOC

photoreceptor cell morphogenesis

Inferred from mutant phenotype PubMed 16864797. Source: FlyBase

protein dephosphorylation

Inferred from direct assay Ref.1. 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_componentaxon

Inferred from direct assay PubMed 18237413. Source: FlyBase

focal adhesion

Inferred from direct assay PubMed 21430143. Source: FlyBase

integral component of 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_functionSAM domain binding

Inferred from physical interaction PubMed 21084592PubMed 21430143. Source: FlyBase

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine phosphatase activity

Inferred from direct assay Ref.1. Source: FlyBase

transmembrane receptor protein tyrosine phosphatase activity

Inferred from sequence or structural similarity PubMed 1657402Ref.1. Source: FlyBase

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232
Chain33 – 20291997Tyrosine-protein phosphatase Lar
PRO_0000025431

Regions

Topological domain33 – 13771345Extracellular Potential
Transmembrane1378 – 140225Helical; Potential
Topological domain1403 – 2029627Cytoplasmic Potential
Domain36 – 12893Ig-like C2-type 1
Domain140 – 22485Ig-like C2-type 2
Domain234 – 31683Ig-like C2-type 3
Domain324 – 41491Fibronectin type-III 1
Domain419 – 51395Fibronectin type-III 2
Domain517 – 60892Fibronectin type-III 3
Domain613 – 70795Fibronectin type-III 4
Domain711 – 810100Fibronectin type-III 5
Domain815 – 91197Fibronectin type-III 6
Domain912 – 100594Fibronectin type-III 7
Domain1009 – 110294Fibronectin type-III 8
Domain1104 – 1206103Fibronectin type-III 9
Domain1474 – 1729256Tyrosine-protein phosphatase 1
Domain1761 – 2020260Tyrosine-protein phosphatase 2
Region70 – 8213Heparin-binding
Region1670 – 16767Substrate binding By similarity

Sites

Active site16701Phosphocysteine intermediate By similarity
Active site19611Phosphocysteine intermediate By similarity
Binding site16381Substrate By similarity
Binding site17141Substrate By similarity

Amino acid modifications

Modified residue15721Phosphothreonine Ref.6
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation5531N-linked (GlcNAc...) Potential
Glycosylation6161N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Glycosylation7211N-linked (GlcNAc...) Potential
Glycosylation7741N-linked (GlcNAc...) Potential
Glycosylation9151N-linked (GlcNAc...) Potential
Glycosylation9621N-linked (GlcNAc...) Potential
Glycosylation11831N-linked (GlcNAc...) Potential
Glycosylation13041N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 111 Ref.7
Disulfide bond161 ↔ 209 Ref.7
Disulfide bond256 ↔ 301 Potential

Experimental info

Sequence conflict480 – 4812EL → DV Ref.1
Sequence conflict480 – 4812EL → DV Ref.2

Secondary structure

........................................... 2029
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16621 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: DF1F676A94050F2B

FASTA2,029229,056
        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 

« Hide

References

« Hide '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. 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.
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, IDENTIFICATION BY 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 expand/collapse EMBL AC list , 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.
PIRTDFFLK. A36182.
RefSeqNP_523604.2. NM_078880.3.
UniGeneDm.24416.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YD1X-ray1.80A33-232[»]
3PXJX-ray2.30A/B/C/D32-237[»]
ProteinModelPortalP16621.
SMRP16621. Positions 31-1010, 1364-2024.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61235. 8 interactions.
DIPDIP-38648N.
IntActP16621. 3 interactions.
MINTMINT-8310371.

Proteomic databases

PaxDbP16621.
PRIDEP16621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0081260; FBpp0080801; FBgn0000464.
GeneID35259.
KEGGdme:Dmel_CG10443.
UCSCCG10443-RA. d. melanogaster.

Organism-specific databases

CTD104121.
FlyBaseFBgn0000464. Lar.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00590000082937.
InParanoidP16621.
KOK05695.
OrthoDBEOG7M98FB.
PhylomeDBP16621.

Gene expression databases

BgeeP16621.

Family and domain databases

Gene3D2.60.40.10. 12 hits.
InterProIPR003961. 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]
PfamPF00041. fn3. 9 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 9 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 6 hits.
PROSITEPS50853. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP16621.
GenomeRNAi35259.
NextBio792660.

Entry information

Entry nameLAR_DROME
AccessionPrimary (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: April 16, 2014
This is version 156 of the entry and version 2 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