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P16620 (PTP69_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase 69D

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine-phosphate phosphohydrolase
Short name=DPTP
Gene names
Name:Ptp69D
Synonyms:DPTP
ORF Names:CG10975
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1462 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. Ref.1

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.1

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class subfamily.

Contains 3 fibronectin type-III domains.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 2 tyrosine-protein phosphatase domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from mutant phenotype PubMed 18516287. Source: FlyBase

axonal defasciculation

Traceable author statement PubMed 9529614. Source: FlyBase

axonogenesis

Inferred from mutant phenotype PubMed 17164414. Source: FlyBase

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

defasciculation of motor neuron axon

Inferred from mutant phenotype PubMed 8598046. Source: FlyBase

dendrite morphogenesis

Inferred from mutant phenotype PubMed 17164414. Source: FlyBase

lateral inhibition

Inferred from mutant phenotype PubMed 19363474. Source: FlyBase

motor neuron axon guidance

Inferred from mutant phenotype PubMed 8598046. Source: FlyBase

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.1. Source: GOC

protein dephosphorylation

Inferred from direct assay Ref.1. Source: FlyBase

   Cellular_componentaxon

Inferred from direct assay PubMed 18237413. Source: FlyBase

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 20462449. Source: FlyBase

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from direct assay Ref.1. Source: FlyBase

transmembrane receptor protein tyrosine phosphatase activity

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

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P16620-1)

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 (identifier: P16620-2)

The sequence of this isoform differs from the canonical sequence as follows:
     845-845: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 14621434Tyrosine-protein phosphatase 69D
PRO_0000025428

Regions

Topological domain29 – 805777Extracellular Potential
Transmembrane806 – 82318Helical; Potential
Topological domain824 – 1462639Cytoplasmic Potential
Domain29 – 12597Ig-like C2-type 1
Domain131 – 230100Ig-like C2-type 2
Domain237 – 33296Fibronectin type-III 1
Domain334 – 435102Fibronectin type-III 2
Domain439 – 547109Fibronectin type-III 3
Domain893 – 1156264Tyrosine-protein phosphatase 1
Domain1187 – 1450264Tyrosine-protein phosphatase 2

Sites

Active site10971Phosphocysteine intermediate By similarity
Active site13911Phosphocysteine intermediate By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation581N-linked (GlcNAc...) Ref.5
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation4421N-linked (GlcNAc...) Potential
Glycosylation4511N-linked (GlcNAc...) Potential
Glycosylation5161N-linked (GlcNAc...) Potential
Glycosylation6131N-linked (GlcNAc...) Ref.5
Glycosylation7011N-linked (GlcNAc...) Ref.5
Glycosylation7551N-linked (GlcNAc...) Potential
Disulfide bond45 ↔ 112 Potential
Disulfide bond154 ↔ 214 Potential

Natural variations

Alternative sequence8451Missing in isoform B.
VSP_015257

Experimental info

Sequence conflict911I → M in AAA28842. Ref.1
Sequence conflict981A → T in AAA28842. Ref.1
Sequence conflict1051K → N in AAA28842. Ref.1
Sequence conflict1271R → K in AAA28842. Ref.1
Sequence conflict6381D → A in AAA28842. Ref.1
Sequence conflict6511D → G in AAA28842. Ref.1
Sequence conflict9901M → I in AAA28842. Ref.1
Sequence conflict11891V → M in AAA28842. Ref.1
Sequence conflict12651L → F in AAA28842. Ref.1

Sequences

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

Last modified August 30, 2005. Version 2.
Checksum: 61214ADC778D319A

FASTA1,462167,460
        10         20         30         40         50         60 
MALLYRRMSM LLNIILAYIF LCAICVQGSV KQEWAEIGKN VSLECASENE AVAWKLGNQT 

        70         80         90        100        110        120 
INKNHTRYKI RTEPLKSNDD GSENNDSQDF IKYKNVLALL DVNIKDSGNY TCTAQTGQNH 

       130        140        150        160        170        180 
STEFQVRPYL PSKVLQSTPD RIKRKIKQDV MLYCLIEMYP QNETTNRNLK WLKDGSQFEF 

       190        200        210        220        230        240 
LDTFSSISKL NDTHLNFTLE FTEVYKKENG TYKCTVFDDT GLEITSKEIT LFVMEVPQVS 

       250        260        270        280        290        300 
IDFAKAVGAN KIYLNWTVND GNDPIQKFFI TLQEAGTPTF TYHKDFINGS HTSYILDHFK 

       310        320        330        340        350        360 
PNTTYFLRIV GKNSIGNGQP TQYPQGITTL SYDPIFIPKV ETTGSTASTI TIGWNPPPPD 

       370        380        390        400        410        420 
LIDYIQYYEL IVSESGEVPK VIEEAIYQQN SRNLPYMFDK LKTATDYEFR VRACSDLTKT 

       430        440        450        460        470        480 
CGPWSENVNG TTMDGVATKP TNLSIQCHHD NVTRGNSIAI NWDVPKTPNG KVVSYLIHLL 

       490        500        510        520        530        540 
GNPMSTVDRE MWGPKIRRID EPHHKTLYES VSPNTNYTVT VSAITRHKKN GEPATGSCLM 

       550        560        570        580        590        600 
PVSTPDAIGR TMWSKVNLDS KYVLKLYLPK ISERNGPICC YRLYLVRINN DNKELPDPEK 

       610        620        630        640        650        660 
LNIATYQEVH SDNVTRSSAY IAEMISSKYF RPEIFLGDEK RFSENNDIIR DNDEICRKCL 

       670        680        690        700        710        720 
EGTPFLRKPE IIHIPPQGSL SNSDSELPIL SEKDNLIKGA NLTEHALKIL ESKLRDKRNA 

       730        740        750        760        770        780 
VTSDENPILS AVNPNVPLHD SSRDVFDGEI DINSNYTGFL EIIVRDRNNA LMAYSKYFDI 

       790        800        810        820        830        840 
ITPATEAEPI QSLNNMDYYL SIGVKAGAVL LGVILVFIVL WVFHHKKTKN ELQGEDTLTL 

       850        860        870        880        890        900 
RDSLSRALFG RRNHNHSHFI TSGNHKGFDA GPIHRLDLEN AYKNRHKDTD YGFLREYEML 

       910        920        930        940        950        960 
PNRFSDRTTK NSDLKENACK NRYPDIKAYD QTRVKLAVIN GLQTTDYINA NFVIGYKERK 

       970        980        990       1000       1010       1020 
KFICAQGPME STIDDFWRMI WEQHLEIIVM LTNLEEYNKA KCAKYWPEKV FDTKQFGDIL 

      1030       1040       1050       1060       1070       1080 
VKFAQERKTG DYIERTLNVS KNKANVGEEE DRRQITQYHY LTWKDFMAPE HPHGIIKFIR 

      1090       1100       1110       1120       1130       1140 
QINSVYSLQR GPILVHCSAG VGRTGTLVAL DSLIQQLEEE DSVSIYNTVC DLRHQRNFLV 

      1150       1160       1170       1180       1190       1200 
QSLKQYIFLY RALLDTGTFG NTDICIDTMA SAIESLKRKP NEGKCKLEVE FEKLLATADE 

      1210       1220       1230       1240       1250       1260 
ISKSCSVGEN EENNMKNRSQ EIIPYDRNRV ILTPLPMREN STYINASFIE GYDNSETFII 

      1270       1280       1290       1300       1310       1320 
AQDPLENTIG DFWRMISEQS VTTLVMISEI GDGPRKCPRY WADDEVQYDH ILVKYVHSES 

      1330       1340       1350       1360       1370       1380 
CPYYTRREFY VTNCKIDDTL KVTQFQYNGW PTVDGEVPEV CRGIIELVDQ AYNHYKNNKN 

      1390       1400       1410       1420       1430       1440 
SGCRSPLTVH CSLGTDRSSI FVAMCILVQH LRLEKCVDIC ATTRKLRSQR TGLINSYAQY 

      1450       1460 
EFLHRAIINY SDLHHIAEST LD 

« Hide

Isoform B [UniParc].

Checksum: 6E5B21C7402C65DD
Show »

FASTA1,461167,373

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] (ISOFORM A), POSSIBLE FUNCTION, CATALYTIC ACTIVITY.
[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. 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.
[3]"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.
[4]"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] (ISOFORM B).
Strain: Berkeley.
Tissue: Embryo.
[5]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58; ASN-613 AND ASN-701, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27699 mRNA. Translation: AAA28842.1.
AE014296 Genomic DNA. Translation: AAF49892.2.
AE014296 Genomic DNA. Translation: AAO41254.1.
BT001531 mRNA. Translation: AAN71286.1.
PIRB36182.
RefSeqNP_524048.2. NM_079324.3.
NP_788502.1. NM_176324.2.
UniGeneDm.945.

3D structure databases

ProteinModelPortalP16620.
SMRP16620. Positions 872-1447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid64791. 6 interactions.
IntActP16620. 3 interactions.
MINTMINT-5227360.

Proteomic databases

PaxDbP16620.
PRIDEP16620.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075913; FBpp0075645; FBgn0014007. [P16620-1]
GeneID39443.
KEGGdme:Dmel_CG10975.

Organism-specific databases

CTD39443.
FlyBaseFBgn0014007. Ptp69D.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00680000099951.
InParanoidP16620.
KOK01104.
OMAYNGWPTV.
OrthoDBEOG7034G2.
PhylomeDBP16620.

Gene expression databases

BgeeP16620.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi39443.
NextBio813657.

Entry information

Entry namePTP69_DROME
AccessionPrimary (citable) accession number: P16620
Secondary accession number(s): Q8IGY3, Q9VU03
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 141 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

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase