PTP69_DROME
ID PTP69_DROME Reviewed; 1462 AA.
AC P16620; Q8IGY3; Q9VU03;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Tyrosine-protein phosphatase 69D;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine-phosphate phosphohydrolase;
DE Short=DPTP;
DE Flags: Precursor;
GN Name=Ptp69D; Synonyms=DPTP; ORFNames=CG10975;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), POSSIBLE FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=2554325; DOI=10.1073/pnas.86.22.8698;
RA Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.;
RT "A family of receptor-linked protein tyrosine phosphatases in humans and
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58; ASN-613 AND ASN-701, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: Possible cell adhesion receptor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:2554325};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P16620-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P16620-2; Sequence=VSP_015257;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class subfamily. {ECO:0000305}.
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DR EMBL; M27699; AAA28842.1; -; mRNA.
DR EMBL; AE014296; AAF49892.2; -; Genomic_DNA.
DR EMBL; AE014296; AAO41254.1; -; Genomic_DNA.
DR EMBL; BT001531; AAN71286.1; -; mRNA.
DR PIR; B36182; B36182.
DR RefSeq; NP_524048.2; NM_079324.3. [P16620-1]
DR RefSeq; NP_788502.1; NM_176324.2. [P16620-2]
DR AlphaFoldDB; P16620; -.
DR SMR; P16620; -.
DR BioGRID; 64791; 12.
DR IntAct; P16620; 9.
DR MINT; P16620; -.
DR STRING; 7227.FBpp0075645; -.
DR GlyGen; P16620; 20 sites.
DR iPTMnet; P16620; -.
DR PaxDb; P16620; -.
DR PRIDE; P16620; -.
DR EnsemblMetazoa; FBtr0075913; FBpp0075645; FBgn0014007. [P16620-1]
DR EnsemblMetazoa; FBtr0075914; FBpp0075646; FBgn0014007. [P16620-2]
DR GeneID; 39443; -.
DR KEGG; dme:Dmel_CG10975; -.
DR CTD; 39443; -.
DR FlyBase; FBgn0014007; Ptp69D.
DR VEuPathDB; VectorBase:FBgn0014007; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000174163; -.
DR InParanoid; P16620; -.
DR OMA; NSDMKEN; -.
DR PhylomeDB; P16620; -.
DR SignaLink; P16620; -.
DR BioGRID-ORCS; 39443; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39443; -.
DR PRO; PR:P16620; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0014007; Expressed in wing disc and 33 other tissues.
DR ExpressionAtlas; P16620; baseline and differential.
DR Genevisible; P16620; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IGI:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007415; P:defasciculation of motor neuron axon; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0097155; P:fasciculation of sensory neuron axon; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0016201; P:synaptic target inhibition; IMP:FlyBase.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 5.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW Hydrolase; Immunoglobulin domain; Membrane; Protein phosphatase; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1462
FT /note="Tyrosine-protein phosphatase 69D"
FT /id="PRO_0000025428"
FT TOPO_DOM 29..805
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 806..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..1462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..125
FT /note="Ig-like C2-type 1"
FT DOMAIN 131..230
FT /note="Ig-like C2-type 2"
FT DOMAIN 237..332
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 334..435
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 439..547
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 893..1156
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1187..1450
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 1097
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1391
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 755
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 154..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 845
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_015257"
FT CONFLICT 91
FT /note="I -> M (in Ref. 1; AAA28842)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="A -> T (in Ref. 1; AAA28842)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="K -> N (in Ref. 1; AAA28842)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="R -> K (in Ref. 1; AAA28842)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="D -> A (in Ref. 1; AAA28842)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="D -> G (in Ref. 1; AAA28842)"
FT /evidence="ECO:0000305"
FT CONFLICT 990
FT /note="M -> I (in Ref. 1; AAA28842)"
FT /evidence="ECO:0000305"
FT CONFLICT 1189
FT /note="V -> M (in Ref. 1; AAA28842)"
FT /evidence="ECO:0000305"
FT CONFLICT 1265
FT /note="L -> F (in Ref. 1; AAA28842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1462 AA; 167460 MW; 61214ADC778D319A CRC64;
MALLYRRMSM LLNIILAYIF LCAICVQGSV KQEWAEIGKN VSLECASENE AVAWKLGNQT
INKNHTRYKI RTEPLKSNDD GSENNDSQDF IKYKNVLALL DVNIKDSGNY TCTAQTGQNH
STEFQVRPYL PSKVLQSTPD RIKRKIKQDV MLYCLIEMYP QNETTNRNLK WLKDGSQFEF
LDTFSSISKL NDTHLNFTLE FTEVYKKENG TYKCTVFDDT GLEITSKEIT LFVMEVPQVS
IDFAKAVGAN KIYLNWTVND GNDPIQKFFI TLQEAGTPTF TYHKDFINGS HTSYILDHFK
PNTTYFLRIV GKNSIGNGQP TQYPQGITTL SYDPIFIPKV ETTGSTASTI TIGWNPPPPD
LIDYIQYYEL IVSESGEVPK VIEEAIYQQN SRNLPYMFDK LKTATDYEFR VRACSDLTKT
CGPWSENVNG TTMDGVATKP TNLSIQCHHD NVTRGNSIAI NWDVPKTPNG KVVSYLIHLL
GNPMSTVDRE MWGPKIRRID EPHHKTLYES VSPNTNYTVT VSAITRHKKN GEPATGSCLM
PVSTPDAIGR TMWSKVNLDS KYVLKLYLPK ISERNGPICC YRLYLVRINN DNKELPDPEK
LNIATYQEVH SDNVTRSSAY IAEMISSKYF RPEIFLGDEK RFSENNDIIR DNDEICRKCL
EGTPFLRKPE IIHIPPQGSL SNSDSELPIL SEKDNLIKGA NLTEHALKIL ESKLRDKRNA
VTSDENPILS AVNPNVPLHD SSRDVFDGEI DINSNYTGFL EIIVRDRNNA LMAYSKYFDI
ITPATEAEPI QSLNNMDYYL SIGVKAGAVL LGVILVFIVL WVFHHKKTKN ELQGEDTLTL
RDSLSRALFG RRNHNHSHFI TSGNHKGFDA GPIHRLDLEN AYKNRHKDTD YGFLREYEML
PNRFSDRTTK NSDLKENACK NRYPDIKAYD QTRVKLAVIN GLQTTDYINA NFVIGYKERK
KFICAQGPME STIDDFWRMI WEQHLEIIVM LTNLEEYNKA KCAKYWPEKV FDTKQFGDIL
VKFAQERKTG DYIERTLNVS KNKANVGEEE DRRQITQYHY LTWKDFMAPE HPHGIIKFIR
QINSVYSLQR GPILVHCSAG VGRTGTLVAL DSLIQQLEEE DSVSIYNTVC DLRHQRNFLV
QSLKQYIFLY RALLDTGTFG NTDICIDTMA SAIESLKRKP NEGKCKLEVE FEKLLATADE
ISKSCSVGEN EENNMKNRSQ EIIPYDRNRV ILTPLPMREN STYINASFIE GYDNSETFII
AQDPLENTIG DFWRMISEQS VTTLVMISEI GDGPRKCPRY WADDEVQYDH ILVKYVHSES
CPYYTRREFY VTNCKIDDTL KVTQFQYNGW PTVDGEVPEV CRGIIELVDQ AYNHYKNNKN
SGCRSPLTVH CSLGTDRSSI FVAMCILVQH LRLEKCVDIC ATTRKLRSQR TGLINSYAQY
EFLHRAIINY SDLHHIAEST LD
