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P16621

- LAR_DROME

UniProt

P16621 - LAR_DROME

Protein

Tyrosine-protein phosphatase Lar

Gene

Lar

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). It controls motor axon guidance.2 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1638 – 16381SubstrateBy similarity
    Active sitei1670 – 16701Phosphocysteine intermediateBy similarity
    Binding sitei1714 – 17141SubstrateBy similarity
    Active sitei1961 – 19611Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein tyrosine phosphatase activity Source: FlyBase
    4. SAM domain binding Source: FlyBase
    5. transmembrane receptor protein tyrosine phosphatase activity Source: FlyBase

    GO - Biological processi

    1. axon extension Source: FlyBase
    2. axon guidance Source: FlyBase
    3. axon target recognition Source: FlyBase
    4. cell adhesion Source: FlyBase
    5. embryonic development via the syncytial blastoderm Source: FlyBase
    6. motor neuron axon guidance Source: FlyBase
    7. nervous system development Source: FlyBase
    8. oogenesis Source: FlyBase
    9. peptidyl-tyrosine dephosphorylation Source: GOC
    10. photoreceptor cell morphogenesis Source: FlyBase
    11. protein dephosphorylation Source: FlyBase
    12. R7 cell development Source: FlyBase
    13. regulation of axon extension involved in axon guidance Source: FlyBase
    14. regulation of cell shape Source: FlyBase
    15. retinal ganglion cell axon guidance Source: FlyBase
    16. synaptic growth at neuromuscular junction Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase, Receptor

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase Lar (EC:3.1.3.48)
    Alternative name(s):
    Protein-tyrosine-phosphate phosphohydrolase
    dLAR
    Gene namesi
    Name:Lar
    ORF Names:CG10443
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0000464. Lar.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: FlyBase
    2. focal adhesion Source: FlyBase
    3. integral component of membrane Source: UniProtKB-KW
    4. microtubule associated complex Source: FlyBase
    5. plasma membrane Source: FlyBase

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Add
    BLAST
    Chaini33 – 20291997Tyrosine-protein phosphatase LarPRO_0000025431Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi57 ↔ 1111 PublicationPROSITE-ProRule annotation
    Disulfide bondi161 ↔ 2091 PublicationPROSITE-ProRule annotation
    Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi256 ↔ 301PROSITE-ProRule annotation
    Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi774 – 7741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi915 – 9151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi962 – 9621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1183 – 11831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1304 – 13041N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1572 – 15721Phosphothreonine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP16621.
    PRIDEiP16621.

    Expressioni

    Tissue specificityi

    Selectively expressed in a subset of axons and pioneer neurons in the embryo.1 Publication

    Gene expression databases

    BgeeiP16621.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AblP005224EBI-668630,EBI-534090
    enaQ8T4F72EBI-668630,EBI-466810
    Liprin-alphaQ9VM936EBI-668630,EBI-113116

    Protein-protein interaction databases

    BioGridi61235. 8 interactions.
    DIPiDIP-38648N.
    IntActiP16621. 3 interactions.
    MINTiMINT-8310371.

    Structurei

    Secondary structure

    1
    2029
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 404
    Beta strandi45 – 484
    Beta strandi53 – 608
    Beta strandi66 – 716
    Beta strandi83 – 886
    Turni89 – 913
    Beta strandi92 – 998
    Turni102 – 1043
    Beta strandi107 – 1148
    Beta strandi116 – 1183
    Beta strandi120 – 13011
    Beta strandi141 – 1444
    Beta strandi149 – 1524
    Beta strandi157 – 1593
    Beta strandi162 – 1643
    Beta strandi170 – 1756
    Beta strandi187 – 1904
    Beta strandi193 – 1964
    Helixi201 – 2033
    Beta strandi205 – 2139
    Beta strandi216 – 2194
    Beta strandi223 – 2286

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YD1X-ray1.80A33-232[»]
    3PXJX-ray2.30A/B/C/D32-237[»]
    ProteinModelPortaliP16621.
    SMRiP16621. Positions 32-1003, 1063-1099, 1448-2024.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16621.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 13771345ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1403 – 2029627CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1378 – 140225HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 12893Ig-like C2-type 1Add
    BLAST
    Domaini140 – 22485Ig-like C2-type 2Add
    BLAST
    Domaini234 – 31683Ig-like C2-type 3Add
    BLAST
    Domaini324 – 41491Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini419 – 51395Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini517 – 60892Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini613 – 70795Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini711 – 810100Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini815 – 91197Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini912 – 100594Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1009 – 110294Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1104 – 1206103Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1474 – 1729256Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1761 – 2020260Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni70 – 8213Heparin-bindingAdd
    BLAST
    Regioni1670 – 16767Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00590000082937.
    InParanoidiP16621.
    KOiK05695.
    OrthoDBiEOG7M98FB.
    PhylomeDBiP16621.

    Family and domain databases

    Gene3Di2.60.40.10. 12 hits.
    3.90.190.10. 2 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00041. fn3. 9 hits.
    PF07679. I-set. 3 hits.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 9 hits.
    SM00408. IGc2. 3 hits.
    SM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 6 hits.
    SSF52799. SSF52799. 2 hits.
    PROSITEiPS50853. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16621-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLQMTAARP IAALSLLVLS LLTWTHPTIV DAAHPPEIIR KPQNQGVRVG     50
    GVASFYCAAR GDPPPSIVWR KNGKKVSGTQ SRYTVLEQPG GISILRIEPV 100
    RAGRDDAPYE CVAENGVGDA VSADATLTIY EGDKTPAGFP VITQGPGTRV 150
    IEVGHTVLMT CKAIGNPTPN IYWIKNQTKV DMSNPRYSLK DGFLQIENSR 200
    EEDQGKYECV AENSMGTEHS KATNLYVKVR RVPPTFSRPP ETISEVMLGS 250
    NLNLSCIAVG SPMPHVKWMK GSEDLTPENE MPIGRNVLQL INIQESANYT 300
    CIAASTLGQI DSVSVVKVQS LPTAPTDVQI SEVTATSVRL EWSYKGPEDL 350
    QYYVIQYKPK NANQAFSEIS GIITMYYVVR ALSPYTEYEF YVIAVNNIGR 400
    GPPSAPATCT TGETKMESAP RNVQVRTLSS STMVITWEPP ETPNGQVTGY 450
    KVYYTTNSNQ PEASWNSQMV DNSELTTVSE LTPHAIYTVR VQAYTSMGAG 500
    PMSTPVQVKA QQGVPSQPSN FRATDIGETA VTLQWTKPTH SSENIVHYEL 550
    YWNDTYANQA HHKRISNSEA YTLDGLYPDT LYYIWLAARS QRGEGATTPP 600
    IPVRTKQYVP GAPPRNITAI ATSSTTISLS WLPPPVERSN GRIIYYKVFF 650
    VEVGREDDEA TTMTLNMTSI VLDELKRWTE YKIWVLAGTS VGDGPRSHPI 700
    ILRTQEDVPG DPQDVKATPL NSTSIHVSWK PPLEKDRNGI IRGYHIHAQE 750
    LRDEGKGFLN EPFKFDVVDT LEFNVTGLQP DTKYSIQVAA LTRKGDGDRS 800
    AAIVVKTPGG VPVRPTVSLK IMEREPIVSI ELEWERPAQT YGELRGYRLR 850
    WGVKDQALKE EMLSGPQMTK KRFDNLERGV EYEFRVAGSN HIGIGQETVK 900
    IFQTPEGTPG GPPSNITIRF QTPDVLCVTW DPPTREHRNG IITRYDVQFH 950
    KKIDHGLGSE RNMTLRKAVF TNLEENTEYI FRVRAYTKQG AGPFSDKLIV 1000
    ETERDMGRAP MSLQAEATSE QTAEIWWEPV TSRGKLLGYK IFYTMTAVED 1050
    LDDWQTKTVG LTESADLVNL EKFAQYAVAI AARFKNGLGR LSEKVTVRIK 1100
    PEDVPLNLRA HDVSTHSMTL SWSPPIRLTP VNYKISFDAM KVFVDSQGFS 1150
    QTQIVPKREI ILKHYVKTHT INELSPFTTY NVNVSAIPSD YSYRPPTKIT 1200
    VTTQMAAPQP MVKPDFYGVV NGEEILVILP QASEEYGPIS HYYLVVVPED 1250
    KSNLHKIPDQ FLTDDLLPGR NKPERPNAPY IAAKFPQRSI PFTFHLGSGD 1300
    DYHNFTNRKL EREKRYRIFV RAVVDTPQKH LYTSSPFSEF LSLDMREAPP 1350
    GERPHRPDPN WPAEPEVSVN RNKDEPEILW VVLPLMVSTF IVSTALIVLC 1400
    VVKRRRQPCK TPDQAAVTRP LMAADLGAGP TPSDPVDMRR LNFQTPGMIS 1450
    HPPIPISEFA NHIERLKSND NQKFSQEYES IEPGQQFTWD NSNLEHNKSK 1500
    NRYANVTAYD HSRVQLPAVE GVVGSDYINA NYCDGYRKHN AYVATQGPLQ 1550
    ETFVDFWRMC WELKTATIVM MTRLEERTRI KCDQYWPTRG TETYGQIFVT 1600
    ITETQELATY SIRTFQLCRQ GFNDRREIKQ LQFTAWPDHG VPDHPAPFLQ 1650
    FLRRCRALTP PESGPVIVHC SAGVGRTGCY IVIDSMLERM KHEKIIDIYG 1700
    HVTCLRAQRN YMVQTEDQYI FIHDAILEAI ICGVTEVPAR NLHTHLQKLL 1750
    ITEPGETISG MEVEFKKLSN VKMDSSKFVT ANLPCNKHKN RLVHILPYES 1800
    SRVYLTPIHG IEGSDYVNAS FIDGYRYRSA YIAAQGPVQD AAEDFWRMLW 1850
    EHNSTIVVML TKLKEMGREK CFQYWPHERS VRYQYYVVDP IAEYNMPQYK 1900
    LREFKVTDAR DGSSRTVRQF QFIDWPEQGV PKSGEGFIDF IGQVHKTKEQ 1950
    FGQDGPITVH CSAGVGRSGV FITLSIVLER MQYEGVLDVF QTVRILRSQR 2000
    PAMVQTEDQY HFCYRAALEY LGSFDNYTN 2029
    Length:2,029
    Mass (Da):229,056
    Last modified:August 30, 2005 - v2
    Checksum:iDF1F676A94050F2B
    GO

    Sequence cautioni

    The sequence AAK93409.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti480 – 4812EL → DV(PubMed:2554325)Curated
    Sequence conflicti480 – 4812EL → DV(PubMed:8598047)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA36182. TDFFLK.
    RefSeqiNP_523604.2. NM_078880.3.
    UniGeneiDm.24416.

    Genome annotation databases

    EnsemblMetazoaiFBtr0081260; FBpp0080801; FBgn0000464.
    GeneIDi35259.
    KEGGidme:Dmel_CG10443.
    UCSCiCG10443-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRi A36182. TDFFLK.
    RefSeqi NP_523604.2. NM_078880.3.
    UniGenei Dm.24416.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P16621.
    SMRi P16621. Positions 32-1003, 1063-1099, 1448-2024.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61235. 8 interactions.
    DIPi DIP-38648N.
    IntActi P16621. 3 interactions.
    MINTi MINT-8310371.

    Proteomic databases

    PaxDbi P16621.
    PRIDEi P16621.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0081260 ; FBpp0080801 ; FBgn0000464 .
    GeneIDi 35259.
    KEGGi dme:Dmel_CG10443.
    UCSCi CG10443-RA. d. melanogaster.

    Organism-specific databases

    CTDi 104121.
    FlyBasei FBgn0000464. Lar.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00590000082937.
    InParanoidi P16621.
    KOi K05695.
    OrthoDBi EOG7M98FB.
    PhylomeDBi P16621.

    Miscellaneous databases

    EvolutionaryTracei P16621.
    GenomeRNAii 35259.
    NextBioi 792660.

    Gene expression databases

    Bgeei P16621.

    Family and domain databases

    Gene3Di 2.60.40.10. 12 hits.
    3.90.190.10. 2 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00041. fn3. 9 hits.
    PF07679. I-set. 3 hits.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 9 hits.
    SM00408. IGc2. 3 hits.
    SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 6 hits.
    SSF52799. SSF52799. 2 hits.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. 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.

    Entry informationi

    Entry nameiLAR_DROME
    AccessioniPrimary (citable) accession number: P16621
    Secondary accession number(s): Q960M3, Q9VIS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3