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   27-MAR-2024, entry version 176.
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   GlyCosmos; P35832; 6 sites, No reported glycans.
DR   GlyGen; P35832; 6 sites.
DR   PaxDb; 7227-FBpp0292247; -.
DR   GeneID; 43469; -.
DR   KEGG; dme:Dmel_CG11516; -.
DR   AGR; FB:FBgn0004369; -.
DR   CTD; 43469; -.
DR   FlyBase; FBgn0004369; Ptp99A.
DR   VEuPathDB; VectorBase:FBgn0004369; -.
DR   InParanoid; P35832; -.
DR   OrthoDB; 2903434at2759; -.
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   GO; GO:0030424; C:axon; IDA:FlyBase.
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   CDD; cd00063; FN3; 2.
DR   CDD; cd14550; R5-PTP-2; 1.
DR   CDD; cd14549; R5-PTPc-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 1.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
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.
DR   Genevisible; P35832; DM.
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;
FT                   AAF56891/AAN14172/AAS65222/AAX53004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="F -> S (in Ref. 4;
FT                   AAF56891/AAN14172/AAS65222/AAX53004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83
FT                   /note="S -> T (in Ref. 4;
FT                   AAF56891/AAN14172/AAS65222/AAX53004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="A -> E (in Ref. 4;
FT                   AAF56891/AAN14172/AAS65222/AAX53004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116
FT                   /note="A -> V (in Ref. 4;
FT                   AAF56891/AAN14172/AAS65222/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;
FT                   AAF56891/AAN14172/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
//