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Q9VZZ4

- PXDN_DROME

UniProt

Q9VZZ4 - PXDN_DROME

Protein

Peroxidasin

Gene

Pxn

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 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Plays a role in extracellular matrix consolidation, phagocytosis and defense.1 Publication

    Catalytic activityi

    2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

    Cofactori

    Binds 1 calcium ion per subunit.By similarity
    Binds 1 heme B (iron-protoporphyrin IX) group covalently per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei862 – 8621Heme (covalent; via 2 links)By similarity
    Active sitei863 – 8631Proton acceptorPROSITE-ProRule annotation
    Metal bindingi864 – 8641CalciumPROSITE-ProRule annotation
    Metal bindingi941 – 9411CalciumPROSITE-ProRule annotation
    Metal bindingi943 – 9431Calcium; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi945 – 9451CalciumPROSITE-ProRule annotation
    Metal bindingi947 – 9471CalciumPROSITE-ProRule annotation
    Sitei1012 – 10121Transition state stabilizerPROSITE-ProRule annotation
    Binding sitei1015 – 10151Heme (covalent; via 2 links)By similarity
    Metal bindingi1109 – 11091Iron (heme axial ligand)PROSITE-ProRule annotation

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. metal ion binding Source: UniProtKB-KW
    3. peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. extracellular matrix organization Source: UniProtKB
    2. hydrogen peroxide catabolic process Source: UniProtKB-KW
    3. phagocytosis Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Protein family/group databases

    PeroxiBasei3369. DmPxd-A.
    3370. DmPxd.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxidasin (EC:1.11.1.7)
    Gene namesi
    Name:Pxn
    ORF Names:CG12002
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0011828. Pxn.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: FlyBase

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 15271504PeroxidasinPRO_0000319624Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi257 ↔ 307By similarity
    Disulfide bondi388 ↔ 437By similarity
    Glycosylationi419 – 4191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi479 ↔ 529By similarity
    Disulfide bondi574 ↔ 627By similarity
    Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi673 – 6731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi682 – 6821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi731 – 7311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi767 – 7671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi768 ↔ 784By similarity
    Disulfide bondi882 ↔ 892By similarity
    Disulfide bondi886 ↔ 909By similarity
    Glycosylationi962 – 9621N-linked (GlcNAc...)1 Publication
    Disulfide bondi994 ↔ 1005By similarity
    Glycosylationi1120 – 11201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1212 ↔ 1269By similarity
    Glycosylationi1213 – 12131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1310 ↔ 1336By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9VZZ4.
    PRIDEiQ9VZZ4.

    Expressioni

    Tissue specificityi

    Expressed in hemocytes. Also expressed in the fat body and gastric caeca.1 Publication

    Developmental stagei

    Expressed throughout embryonic and larval development. Expressed in hemocytes as they migrate in the early embryo and later in embryogenesis, become localized to basement membranes.1 Publication

    Gene expression databases

    BgeeiQ9VZZ4.

    Interactioni

    Subunit structurei

    Homotrimer; disulfide-linked.1 Publication

    Protein-protein interaction databases

    BioGridi63831. 4 interactions.
    IntActiQ9VZZ4. 2 interactions.
    MINTiMINT-1680107.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VZZ4.
    SMRiQ9VZZ4. Positions 24-709, 774-1349.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 5229LRRNTAdd
    BLAST
    Repeati53 – 7422LRR 1Add
    BLAST
    Repeati77 – 9822LRR 2Add
    BLAST
    Repeati101 – 12222LRR 3Add
    BLAST
    Repeati125 – 14622LRR 4Add
    BLAST
    Repeati149 – 17022LRR 5Add
    BLAST
    Domaini182 – 23554LRRCTAdd
    BLAST
    Domaini236 – 32287Ig-like C2-type 1Add
    BLAST
    Domaini365 – 45389Ig-like C2-type 2Add
    BLAST
    Domaini458 – 54588Ig-like C2-type 3Add
    BLAST
    Domaini553 – 64391Ig-like C2-type 4Add
    BLAST
    Domaini1463 – 152462VWFCPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1403 – 144139Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation
    Contains 5 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated
    Contains 1 VWFC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4886.
    GeneTreeiENSGT00550000074325.
    InParanoidiQ9VZZ4.
    OMAiRVRNGRC.
    OrthoDBiEOG7D2FD6.
    PhylomeDBiQ9VZZ4.

    Family and domain databases

    Gene3Di1.10.640.10. 2 hits.
    2.60.40.10. 4 hits.
    InterProiIPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF03098. An_peroxidase. 1 hit.
    PF07679. I-set. 4 hits.
    PF13855. LRR_8. 2 hits.
    PF00093. VWC. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SMARTiSM00409. IG. 1 hit.
    SM00408. IGc2. 3 hits.
    SM00369. LRR_TYP. 3 hits.
    SM00013. LRRNT. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view]
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS50835. IG_LIKE. 4 hits.
    PS50292. PEROXIDASE_3. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q9VZZ4-1) [UniParc]FASTAAdd to Basket

    Also known as: C, D, E

    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.

    « Hide

    MRFMLLMLQL LGLLLLLAGG VQSVYCPAGC TCLERTVRCI RAKLSAVPKL     50
    PQDTQTLDLR FNHIEELPAN AFSGLAQLTT LFLNDNELAY LQDGALNGLT 100
    ALRFVYLNNN RLSRLPATIF QRMPRLEAIF LENNDIWQLP AGLFDNLPRL 150
    NRLIMYNNKL TQLPVDGFNR LNNLKRLRLD GNAIDCNCGV YSLWRRWHLD 200
    VQRQLVSISL TCAAPQMLQN QGFSSLGEHH FKCAKPQFLV APQDAQVAAG 250
    EQVELSCEVT GLPRPQITWM HNTQELGLEE QAQAEILPSG SLLIRSADTS 300
    DMGIYQCIAR NEMGALRSQP VRLVVNGGNH PLDSPIDARS NQVWADAGTP 350
    MHGATPLPSP LPSPPHFTHQ PHDQIVALHG SGHVLLDCAA SGWPQPDIQW 400
    FVNGRQLLQS TPSLQLQANG SLILLQPNQL SAGTYRCEAR NSLGSVQATA 450
    RIELKELPEI LTAPQSQTIK LGKAFVLECD ADGNPLPTID WQLNGVPLPG 500
    NTPDLQLENE NTELVVGAAR QEHAGVYRCT AHNENGETSV EATIKVERSQ 550
    SPPQLAIEPS NLVAITGTTI ELPCQADQPE DGLQISWRHD GRLIDPNVQL 600
    AEKYQISGAG SLFVKNVTIP DGGRYECQLK NQFGRASASA LVTIRNNVDL 650
    APGDRYVRIA FAEAAKEIDL AINNTLDMLF SNRSDKAPPN YGELLRVFRF 700
    PTGEARQLAR AAEIYERTLV NIRKHVQEGD NLTMKSEEYE FRDLLSREHL 750
    HLVAELSGCM EHREMPNCTD MCFHSRYRSI DGTCNNLQHP TWGASLTAFR 800
    RLAPPIYENG FSMPVGWTKG MLYSGHAKPS ARLVSTSLVA TKEITPDARI 850
    THMVMQWGQF LDHDLDHAIP SVSSESWDGI DCKKSCEMAP PCYPIEVPPN 900
    DPRVRNRRCI DVVRSSAICG SGMTSLFFDS VQHREQINQL TSYIDASQVY 950
    GYSTAFAQEL RNLTSQEGLL RVGVHFPRQK DMLPFAAPQD GMDCRRNLDE 1000
    NTMSCFVSGD IRVNEQVGLL AMHTIWMREH NRIASKLKQI NSHWDGDTLY 1050
    QEARKIVGAQ MQHITFKQWL PLIIGESGME MMGEYQGYNP QLNPSIANEF 1100
    ATAALRFGHT IINPILHRLN ETFQPIPQGH LLLHKAFFAP WRLAYEGGVD 1150
    PLMRGFLAVP AKLKTPDQNL NTELTEKLFQ TAHAVALDLA AINIQRGRDH 1200
    GMPGYNVYRK LCNLTVAQDF EDLAGEISSA EIRQKMKELY GHPDNVDVWL 1250
    GGILEDQVEG GKVGPLFQCL LVEQFRRLRD GDRLYYENPG VFSPEQLTQI 1300
    KQANFGRVLC DVGDNFDQVT ENVFILAKHQ GGYKKCEDII GINLYLWQEC 1350
    GRCNSPPAIF DSYIPQTYTK RSNRQKRDLG KENDEVATAE SYDSPLESLY 1400
    DVNEERVSGL EELIGSFQKE LKKLHKKLRK LEDSCNSADS EPVAQVVQLA 1450
    AAPPQLVSKP KRSHCVDDKG TTRLNNEVWS PDVCTKCNCF HGQVNCLRER 1500
    CGEVSCPPGV DPLTPPEACC PHCPMVK 1527
    Length:1,527
    Mass (Da):170,514
    Last modified:May 1, 2000 - v1
    Checksum:i71174FEBEA7C9152
    GO
    Isoform B (identifier: Q9VZZ4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         456-457: EL → GE
         458-1527: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:457
    Mass (Da):50,558
    Checksum:i243FB8041A16D483
    GO

    Sequence cautioni

    The sequence AAA61568.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281A → G in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti183 – 1831A → AID in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti263 – 2631P → H in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti282 – 2821A → T in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti294 – 2941I → H in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti351 – 3511M → T in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti361 – 3622LP → SPSH in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti380 – 3801G → S in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti692 – 6921G → D in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti959 – 9602EL → LA in AAA61568. (PubMed:8062820)Curated
    Sequence conflicti1083 – 10831G → S in AAA61568. (PubMed:8062820)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei456 – 4572EL → GE in isoform B. 1 PublicationVSP_032693
    Alternative sequencei458 – 15271070Missing in isoform B. 1 PublicationVSP_032694Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11052 mRNA. Translation: AAA61568.1. Frameshift.
    AE014296 Genomic DNA. Translation: AAF47668.1.
    AE014296 Genomic DNA. Translation: AAN11518.1.
    AE014296 Genomic DNA. Translation: AAS64946.1.
    AE014296 Genomic DNA. Translation: AAS64947.1.
    AE014296 Genomic DNA. Translation: AAS64948.1.
    AY051536 mRNA. Translation: AAK92960.1.
    AY052120 mRNA. Translation: AAK93544.1.
    RefSeqiNP_523891.2. NM_079167.4. [Q9VZZ4-1]
    NP_728759.1. NM_167957.2. [Q9VZZ4-2]
    NP_995975.1. NM_206253.2. [Q9VZZ4-1]
    NP_995976.1. NM_206254.2. [Q9VZZ4-1]
    NP_995977.1. NM_206255.2. [Q9VZZ4-1]
    UniGeneiDm.8030.

    Genome annotation databases

    EnsemblMetazoaiFBtr0072951; FBpp0072828; FBgn0011828. [Q9VZZ4-1]
    FBtr0072952; FBpp0089205; FBgn0011828. [Q9VZZ4-1]
    FBtr0072953; FBpp0089215; FBgn0011828. [Q9VZZ4-1]
    FBtr0072954; FBpp0089216; FBgn0011828. [Q9VZZ4-1]
    GeneIDi38326.
    KEGGidme:Dmel_CG12002.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11052 mRNA. Translation: AAA61568.1 . Frameshift.
    AE014296 Genomic DNA. Translation: AAF47668.1 .
    AE014296 Genomic DNA. Translation: AAN11518.1 .
    AE014296 Genomic DNA. Translation: AAS64946.1 .
    AE014296 Genomic DNA. Translation: AAS64947.1 .
    AE014296 Genomic DNA. Translation: AAS64948.1 .
    AY051536 mRNA. Translation: AAK92960.1 .
    AY052120 mRNA. Translation: AAK93544.1 .
    RefSeqi NP_523891.2. NM_079167.4. [Q9VZZ4-1 ]
    NP_728759.1. NM_167957.2. [Q9VZZ4-2 ]
    NP_995975.1. NM_206253.2. [Q9VZZ4-1 ]
    NP_995976.1. NM_206254.2. [Q9VZZ4-1 ]
    NP_995977.1. NM_206255.2. [Q9VZZ4-1 ]
    UniGenei Dm.8030.

    3D structure databases

    ProteinModelPortali Q9VZZ4.
    SMRi Q9VZZ4. Positions 24-709, 774-1349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 63831. 4 interactions.
    IntActi Q9VZZ4. 2 interactions.
    MINTi MINT-1680107.

    Protein family/group databases

    PeroxiBasei 3369. DmPxd-A.
    3370. DmPxd.

    Proteomic databases

    PaxDbi Q9VZZ4.
    PRIDEi Q9VZZ4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0072951 ; FBpp0072828 ; FBgn0011828 . [Q9VZZ4-1 ]
    FBtr0072952 ; FBpp0089205 ; FBgn0011828 . [Q9VZZ4-1 ]
    FBtr0072953 ; FBpp0089215 ; FBgn0011828 . [Q9VZZ4-1 ]
    FBtr0072954 ; FBpp0089216 ; FBgn0011828 . [Q9VZZ4-1 ]
    GeneIDi 38326.
    KEGGi dme:Dmel_CG12002.

    Organism-specific databases

    CTDi 5829.
    FlyBasei FBgn0011828. Pxn.

    Phylogenomic databases

    eggNOGi COG4886.
    GeneTreei ENSGT00550000074325.
    InParanoidi Q9VZZ4.
    OMAi RVRNGRC.
    OrthoDBi EOG7D2FD6.
    PhylomeDBi Q9VZZ4.

    Miscellaneous databases

    ChiTaRSi PXN. drosophila.
    GenomeRNAii 38326.
    NextBioi 808033.
    PROi Q9VZZ4.

    Gene expression databases

    Bgeei Q9VZZ4.

    Family and domain databases

    Gene3Di 1.10.640.10. 2 hits.
    2.60.40.10. 4 hits.
    InterProi IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF03098. An_peroxidase. 1 hit.
    PF07679. I-set. 4 hits.
    PF13855. LRR_8. 2 hits.
    PF00093. VWC. 1 hit.
    [Graphical view ]
    PRINTSi PR00457. ANPEROXIDASE.
    SMARTi SM00409. IG. 1 hit.
    SM00408. IGc2. 3 hits.
    SM00369. LRR_TYP. 3 hits.
    SM00013. LRRNT. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48113. SSF48113. 1 hit.
    PROSITEi PS50835. IG_LIKE. 4 hits.
    PS50292. PEROXIDASE_3. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Peroxidasin: a novel enzyme-matrix protein of Drosophila development."
      Nelson R.E., Fessler L.I., Takagi Y., Blumberg B., Keene D.R., Olson P.F., Parker C.G., Fessler J.H.
      EMBO J. 13:3438-3447(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Salivary gland.
    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.
      , 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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1527 (ISOFORM A).
      Strain: Berkeley.
      Tissue: Head.
    5. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
      Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
      Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-962, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Oregon-R.
      Tissue: Head.

    Entry informationi

    Entry nameiPXDN_DROME
    AccessioniPrimary (citable) accession number: Q9VZZ4
    Secondary accession number(s): Q23991, Q960D1, Q961K8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3