PTP99_DROME
ID PTP99_DROME Reviewed; 1301 AA.
AC P35832; Q59DT5; Q7KRW3; Q8IMK9; Q9VAL3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Tyrosine-protein phosphatase 99A;
DE EC=3.1.3.48;
DE AltName: Full=Receptor-linked protein-tyrosine phosphatase 99A;
DE Short=DPTP99A;
DE Flags: Precursor;
GN Name=Ptp99A; ORFNames=CG2005;
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] (ISOFORMS A AND B), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1657401; DOI=10.1016/0092-8674(91)90062-4;
RA Yang X., Seow K.T., Bahri S.M., Oon S.H., Chia W.;
RT "Two Drosophila receptor-like tyrosine phosphatase genes are expressed in a
RT subset of developing axons and pioneer neurons in the embryonic CNS.";
RL Cell 67:661-673(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=1657402; DOI=10.1016/0092-8674(91)90063-5;
RA Tian S.-S., Tsoulfas P., Zinn K.;
RT "Three receptor-linked protein-tyrosine phosphatases are selectively
RT expressed on central nervous system axons in the Drosophila embryo.";
RL Cell 67:675-685(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND TISSUE SPECIFICITY.
RC TISSUE=Eye imaginal disk;
RX PubMed=1662390; DOI=10.1073/pnas.88.24.11266;
RA Hariharan I.K., Chuang P.-T., Rubin G.M.;
RT "Cloning and characterization of a receptor-class phosphotyrosine
RT phosphatase gene expressed on central nervous system axons in Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11266-11270(1991).
RN [4]
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 [5]
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).
CC -!- FUNCTION: May play a key role in signal transduction and growth
CC control. May have a role in the establishment of the intersegmental and
CC segmental nerves. {ECO:0000269|PubMed:1657401}.
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};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=B;
CC IsoId=P35832-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P35832-2; Sequence=VSP_005142;
CC Name=C;
CC IsoId=P35832-3; Sequence=VSP_015261, VSP_005142;
CC Name=D;
CC IsoId=P35832-4; Sequence=VSP_015262, VSP_015263;
CC -!- TISSUE SPECIFICITY: Selectively expressed in a subset of axons and
CC pioneer neurons (including aCC and RP2) in the embryo.
CC {ECO:0000269|PubMed:1657401, ECO:0000269|PubMed:1657402,
CC ECO:0000269|PubMed:1662390}.
CC -!- DEVELOPMENTAL STAGE: Start of expression coincides with the onset of
CC axonogenesis. {ECO:0000269|PubMed:1657401}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class subfamily. {ECO:0000305}.
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DR EMBL; M80464; AAA28486.1; -; mRNA.
DR EMBL; M80539; AAA28485.1; -; mRNA.
DR EMBL; M81795; AAA28483.1; -; mRNA.
DR EMBL; AE014297; AAF56891.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN14172.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65222.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX53004.1; -; Genomic_DNA.
DR PIR; A41622; A41622.
DR RefSeq; NP_476816.1; NM_057468.3.
DR RefSeq; NP_733288.1; NM_170409.3.
DR RefSeq; NP_996302.1; NM_206579.3.
DR AlphaFoldDB; P35832; -.
DR SMR; P35832; -.
DR BioGRID; 68335; 10.
DR STRING; 7227.FBpp0292247; -.
DR GlyGen; P35832; 6 sites.
DR PRIDE; P35832; -.
DR GeneID; 43469; -.
DR KEGG; dme:Dmel_CG11516; -.
DR CTD; 43469; -.
DR FlyBase; FBgn0004369; Ptp99A.
DR VEuPathDB; VectorBase:FBgn0004369; -.
DR InParanoid; P35832; -.
DR PhylomeDB; P35832; -.
DR BioGRID-ORCS; 43469; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Ptp99A; fly.
DR GenomeRNAi; 43469; -.
DR PRO; PR:P35832; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR ExpressionAtlas; P35832; baseline and differential.
DR Genevisible; P35832; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:FlyBase.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISS:FlyBase.
DR GO; GO:0007414; P:axonal defasciculation; TAS:FlyBase.
DR GO; GO:0007415; P:defasciculation of motor neuron axon; IGI:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:FlyBase.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Hydrolase; Membrane;
KW Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1301
FT /note="Tyrosine-protein phosphatase 99A"
FT /id="PRO_0000025429"
FT TOPO_DOM 29..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..1301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 66..165
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 173..269
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 270..376
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 476..741
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 764..1016
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 31..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 682
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 238
FT /note="R -> REFNYVFIWGLFGVKG (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_015261"
FT VAR_SEQ 1050..1119
FT /note="Missing (in isoform A and isoform C)"
FT /evidence="ECO:0000303|PubMed:1657401,
FT ECO:0000303|PubMed:1657402"
FT /id="VSP_005142"
FT VAR_SEQ 1050..1058
FT /note="GNVPQHVIL -> AQQRQMLKT (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_015262"
FT VAR_SEQ 1059..1301
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_015263"
FT CONFLICT 46
FT /note="V -> A (in Ref. 4; AAF56891/AAN14172/AAS65222/
FT AAX53004)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="F -> S (in Ref. 4; AAF56891/AAN14172/AAS65222/
FT AAX53004)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> T (in Ref. 4; AAF56891/AAN14172/AAS65222/
FT AAX53004)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="A -> E (in Ref. 4; AAF56891/AAN14172/AAS65222/
FT AAX53004)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> V (in Ref. 4; AAF56891/AAN14172/AAS65222/
FT AAX53004)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="R -> P (in Ref. 3; AAA28483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1133
FT /note="T -> P (in Ref. 4; AAF56891/AAN14172/AAS65222)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167..1176
FT /note="ASPVTPATAS -> GSPAT (in Ref. 4; AAF56891/AAN14172/
FT AAS65222)"
FT /evidence="ECO:0000305"
FT CONFLICT 1205
FT /note="N -> H (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1301 AA; 145396 MW; AB1FB7A8F5D7D30F CRC64;
MPRPQHHALL RAMLKLLLFA SIAEHCATAL PTNSSNSPSS PSPFTVASLP PTTASSSSSP
AVISTSSFDR NLADLVNPEA ETSGSGWESL ETEFNLATTV DSSTQKTAKE PVLGTAATSI
EQQDQPPDVP ATTLAFANAF PVPVAGEMGN GNGNYNDATP PYAAVDDNYV PSKPQNLTIL
DVSANSITMS WHPPKNQNGA IAGYHVFHIH DNQTGVEIVK NSRNSVETLI HFELQNLRPY
TDYRVIVKAF TTKNEGEPSD QIAQRTDVGG PSAPAIVNLT CHSQESITIR WRRPYEFYNT
IDFYIIKTRL AGQDTHRDIR INASAKELET AMILQNLTTN SYYEVKVAAA TFSVINPKKI
VLGKFSESRI IQLQPNCEKL QPLLRQSHND YNLAVLVGII FSCFGIILII MAFFLWSRKC
FHAAYYYLDD PPHHPNAPQV DWEVPVKIGD EIRAAVPVNE FAKHVASLHA DGDIGFSREY
EAIQNECISD DLPCEHSQHP ENKRKNRYLN ITAYDHSRVH LHPTPGQKKN LDYINANFID
GYQKGHAFIG TQGPLPDTFD CFWRMIWEQR VAIIVMITNL VERGRRKCDM YWPKDGVETY
GVIQVKLIEE EVMSTYTVRT LQIKHLKLKK KKQCNTEKLV YQYHYTNWPD HGTPDHPLPV
LNFVKKSSAA NPAEAGPIVV HCSAGVGRTG TYIVLDAMLK QIQQKNIVNV FGFLRHIRAQ
RNFLVQTEEQ YIFLHDALVE AIASGETNLM AEQVEELKNC TPYLEQQYKN IIQFQPKDIH
IASAMKQVNS IKNRGAIFPI EGSRVHLTPK PGEDGSDYIN ASWLHGFRRL RDFIVTQHPM
AHTIKDFWQM VWDHNAQTVV LLSSLDDINF AQFWPDEATP IESDHYRVKF LNKTNKSDYV
SRDFVIQSIQ DDYELTVKML HCPSWPEMSN PNSIYDFIVD VHERCNDYRN GPIVIVDRYG
GAQACTFCAI SSLAIEMEYC STANVYQYAK LYHNKRPGVW TSSEDIRVIY NILSFLPGNL
NLLKRTALRT EFEDVTTATP DLYSKICSNG NVPQHVILQQ QQLHMLQLQQ QHLETQQQQQ
QQQQQQQQQQ QTALNETVST PSTDTNPSLL PILSLLPPTV APLSSSSSTT PPTPSTPTPQ
PPQTIQLSSH SPSDLSHQIS STVANAASPV TPATASASAG ATPTTPMTPT VPPTIPTIPS
LASQNSLTLT NANFHTVTNN AADLMEHQQQ QMLALMQQQT QLQQQYNTHP QQHHNNVGDL
LMNNADNSPT ASPTITNNNH ITNNNVTSAA ATDAQNLDIV G
