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Q9VZZ4

- PXDN_DROME

UniProt

Q9VZZ4 - PXDN_DROME

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Protein

Peroxidasin

Gene

Pxn

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 1 Ca(2+) ion per subunit.By similarity
  • heme bBy similarityNote: Binds 1 heme b (iron(II)-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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiQ9VZZ4. differential.

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 23-709, 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

        10         20         30         40         50
MRFMLLMLQL LGLLLLLAGG VQSVYCPAGC TCLERTVRCI RAKLSAVPKL
60 70 80 90 100
PQDTQTLDLR FNHIEELPAN AFSGLAQLTT LFLNDNELAY LQDGALNGLT
110 120 130 140 150
ALRFVYLNNN RLSRLPATIF QRMPRLEAIF LENNDIWQLP AGLFDNLPRL
160 170 180 190 200
NRLIMYNNKL TQLPVDGFNR LNNLKRLRLD GNAIDCNCGV YSLWRRWHLD
210 220 230 240 250
VQRQLVSISL TCAAPQMLQN QGFSSLGEHH FKCAKPQFLV APQDAQVAAG
260 270 280 290 300
EQVELSCEVT GLPRPQITWM HNTQELGLEE QAQAEILPSG SLLIRSADTS
310 320 330 340 350
DMGIYQCIAR NEMGALRSQP VRLVVNGGNH PLDSPIDARS NQVWADAGTP
360 370 380 390 400
MHGATPLPSP LPSPPHFTHQ PHDQIVALHG SGHVLLDCAA SGWPQPDIQW
410 420 430 440 450
FVNGRQLLQS TPSLQLQANG SLILLQPNQL SAGTYRCEAR NSLGSVQATA
460 470 480 490 500
RIELKELPEI LTAPQSQTIK LGKAFVLECD ADGNPLPTID WQLNGVPLPG
510 520 530 540 550
NTPDLQLENE NTELVVGAAR QEHAGVYRCT AHNENGETSV EATIKVERSQ
560 570 580 590 600
SPPQLAIEPS NLVAITGTTI ELPCQADQPE DGLQISWRHD GRLIDPNVQL
610 620 630 640 650
AEKYQISGAG SLFVKNVTIP DGGRYECQLK NQFGRASASA LVTIRNNVDL
660 670 680 690 700
APGDRYVRIA FAEAAKEIDL AINNTLDMLF SNRSDKAPPN YGELLRVFRF
710 720 730 740 750
PTGEARQLAR AAEIYERTLV NIRKHVQEGD NLTMKSEEYE FRDLLSREHL
760 770 780 790 800
HLVAELSGCM EHREMPNCTD MCFHSRYRSI DGTCNNLQHP TWGASLTAFR
810 820 830 840 850
RLAPPIYENG FSMPVGWTKG MLYSGHAKPS ARLVSTSLVA TKEITPDARI
860 870 880 890 900
THMVMQWGQF LDHDLDHAIP SVSSESWDGI DCKKSCEMAP PCYPIEVPPN
910 920 930 940 950
DPRVRNRRCI DVVRSSAICG SGMTSLFFDS VQHREQINQL TSYIDASQVY
960 970 980 990 1000
GYSTAFAQEL RNLTSQEGLL RVGVHFPRQK DMLPFAAPQD GMDCRRNLDE
1010 1020 1030 1040 1050
NTMSCFVSGD IRVNEQVGLL AMHTIWMREH NRIASKLKQI NSHWDGDTLY
1060 1070 1080 1090 1100
QEARKIVGAQ MQHITFKQWL PLIIGESGME MMGEYQGYNP QLNPSIANEF
1110 1120 1130 1140 1150
ATAALRFGHT IINPILHRLN ETFQPIPQGH LLLHKAFFAP WRLAYEGGVD
1160 1170 1180 1190 1200
PLMRGFLAVP AKLKTPDQNL NTELTEKLFQ TAHAVALDLA AINIQRGRDH
1210 1220 1230 1240 1250
GMPGYNVYRK LCNLTVAQDF EDLAGEISSA EIRQKMKELY GHPDNVDVWL
1260 1270 1280 1290 1300
GGILEDQVEG GKVGPLFQCL LVEQFRRLRD GDRLYYENPG VFSPEQLTQI
1310 1320 1330 1340 1350
KQANFGRVLC DVGDNFDQVT ENVFILAKHQ GGYKKCEDII GINLYLWQEC
1360 1370 1380 1390 1400
GRCNSPPAIF DSYIPQTYTK RSNRQKRDLG KENDEVATAE SYDSPLESLY
1410 1420 1430 1440 1450
DVNEERVSGL EELIGSFQKE LKKLHKKLRK LEDSCNSADS EPVAQVVQLA
1460 1470 1480 1490 1500
AAPPQLVSKP KRSHCVDDKG TTRLNNEVWS PDVCTKCNCF HGQVNCLRER
1510 1520
CGEVSCPPGV DPLTPPEACC PHCPMVK
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. Curated

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:
EMBLi
GenBanki
DDBJi
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_079167.5. [Q9VZZ4-1]
NP_728759.1. NM_167957.3. [Q9VZZ4-2]
NP_995975.1. NM_206253.3. [Q9VZZ4-1]
NP_995976.1. NM_206254.3. [Q9VZZ4-1]
NP_995977.1. NM_206255.3. [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:
EMBLi
GenBanki
DDBJi
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_079167.5. [Q9VZZ4-1 ]
NP_728759.1. NM_167957.3. [Q9VZZ4-2 ]
NP_995975.1. NM_206253.3. [Q9VZZ4-1 ]
NP_995976.1. NM_206254.3. [Q9VZZ4-1 ]
NP_995977.1. NM_206255.3. [Q9VZZ4-1 ]
UniGenei Dm.8030.

3D structure databases

ProteinModelPortali Q9VZZ4.
SMRi Q9VZZ4. Positions 23-709, 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. fly.
GenomeRNAii 38326.
NextBioi 808033.
PROi Q9VZZ4.

Gene expression databases

Bgeei Q9VZZ4.
ExpressionAtlasi Q9VZZ4. differential.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 120 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