ID PTP10_DROME Reviewed; 1631 AA.
AC P35992; A4V4B4; B7Z142; Q0KHT5; Q86NN9; Q8IR87; Q9VYW1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 3.
DT 01-MAY-2013, entry version 121.
DE RecName: Full=Tyrosine-protein phosphatase 10D;
DE EC=3.1.3.48;
DE AltName: Full=Receptor-linked protein-tyrosine phosphatase 10D;
DE Short=DPTP10D;
DE Flags: Precursor;
GN Name=Ptp10D; ORFNames=CG1817;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND E), 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
RT in a subset of developing axons and pioneer neurons in the embryonic
RT CNS.";
RL Cell 67:661-673(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), 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 [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.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA 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.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA 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.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572;
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.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May have a role in axon outgrowth and guidance.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B; Synonyms=Long;
CC IsoId=P35992-1; Sequence=Displayed;
CC Name=A; Synonyms=D;
CC IsoId=P35992-3; Sequence=VSP_015266;
CC Note=No experimental confirmation available;
CC Name=E; Synonyms=Short;
CC IsoId=P35992-2; Sequence=VSP_005143, VSP_005144;
CC -!- TISSUE SPECIFICITY: In 9-12 hour embryos, expression is
CC specifically seen in the anterior commissure and its junctions
CC with the longitudinal tracts.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed throughout development to adulthood, lowest expression
CC is during second and third larval instars.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class subfamily.
CC -!- SIMILARITY: Contains 12 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR EMBL; M80465; AAA28484.1; -; mRNA.
DR EMBL; M80538; AAA28952.1; -; mRNA.
DR EMBL; AE014298; AAF48072.3; -; Genomic_DNA.
DR EMBL; AE014298; AAS65319.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65320.1; -; Genomic_DNA.
DR EMBL; AE014298; ACL82919.1; -; Genomic_DNA.
DR EMBL; BT004474; AAO42638.1; -; mRNA.
DR PIR; C41214; C41214.
DR PIR; D41214; D41214.
DR RefSeq; NP_001138187.1; NM_001144715.2.
DR RefSeq; NP_001259454.1; NM_001272525.1.
DR RefSeq; NP_727544.2; NM_167292.3.
DR RefSeq; NP_996413.2; NM_206690.2.
DR RefSeq; NP_996414.2; NM_206691.3.
DR UniGene; Dm.7386; -.
DR PDB; 3S3E; X-ray; 2.40 A; A/B=1250-1533.
DR PDB; 3S3F; X-ray; 2.70 A; A/B=1250-1533.
DR PDB; 3S3H; X-ray; 2.80 A; A/B=1250-1533.
DR PDB; 3S3K; X-ray; 3.20 A; A/B=1250-1533.
DR PDBsum; 3S3E; -.
DR PDBsum; 3S3F; -.
DR PDBsum; 3S3H; -.
DR PDBsum; 3S3K; -.
DR ProteinModelPortal; P35992; -.
DR SMR; P35992; 121-1050, 1249-1531.
DR IntAct; P35992; 2.
DR PaxDb; P35992; -.
DR PRIDE; P35992; -.
DR EnsemblMetazoa; FBtr0073522; FBpp0073369; FBgn0004370.
DR GeneID; 32115; -.
DR KEGG; dme:Dmel_CG1817; -.
DR CTD; 32115; -.
DR FlyBase; FBgn0004370; Ptp10D.
DR eggNOG; COG5599; -.
DR GeneTree; ENSGT00700000104166; -.
DR InParanoid; P35992; -.
DR KO; K01104; -.
DR OMA; LHSTRDD; -.
DR OrthoDB; EOG483BKC; -.
DR ChiTaRS; Ptp10D; drosophila.
DR GenomeRNAi; 32115; -.
DR NextBio; 776913; -.
DR Bgee; P35992; -.
DR GermOnline; CG1817; Drosophila melanogaster.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISS:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IGI:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IGI:FlyBase.
DR Gene3D; 2.60.40.10; -; 9.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF00041; fn3; 10.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 11.
DR SMART; SM00194; PTPc; 1.
DR SUPFAM; SSF49265; FN_III-like; 10.
DR PROSITE; PS50853; FN3; 11.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Developmental protein; Differentiation; Glycoprotein; Hydrolase;
KW Membrane; Neurogenesis; Protein phosphatase; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 42 Potential.
FT CHAIN 43 1631 Tyrosine-protein phosphatase 10D.
FT /FTId=PRO_0000025427.
FT TOPO_DOM 43 1197 Extracellular (Potential).
FT TRANSMEM 1198 1218 Helical; (Potential).
FT TOPO_DOM 1219 1631 Cytoplasmic (Potential).
FT DOMAIN 43 119 Fibronectin type-III 1.
FT DOMAIN 120 214 Fibronectin type-III 2.
FT DOMAIN 215 308 Fibronectin type-III 3.
FT DOMAIN 309 402 Fibronectin type-III 4.
FT DOMAIN 403 493 Fibronectin type-III 5.
FT DOMAIN 494 580 Fibronectin type-III 6.
FT DOMAIN 581 669 Fibronectin type-III 7.
FT DOMAIN 670 766 Fibronectin type-III 8.
FT DOMAIN 767 861 Fibronectin type-III 9.
FT DOMAIN 862 955 Fibronectin type-III 10.
FT DOMAIN 956 1048 Fibronectin type-III 11.
FT DOMAIN 1049 1190 Fibronectin type-III 12.
FT DOMAIN 1272 1527 Tyrosine-protein phosphatase.
FT REGION 1468 1474 Substrate binding (By similarity).
FT ACT_SITE 1468 1468 Phosphocysteine intermediate (By
FT similarity).
FT BINDING 1436 1436 Substrate (By similarity).
FT BINDING 1512 1512 Substrate (By similarity).
FT CARBOHYD 75 75 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 106 106 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 128 128 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 169 169 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 212 212 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 229 229 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 259 259 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 289 289 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 317 317 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 471 471 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 486 486 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 512 512 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 533 533 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 588 588 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 668 668 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 687 687 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 719 719 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 723 723 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 823 823 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 841 841 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 874 874 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 908 908 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 925 925 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1001 1001 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1104 1104 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1136 1136 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1195 1195 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 1549 1558 GQQVQLDENG -> DDEGIAESGM (in isoform E).
FT /FTId=VSP_005143.
FT VAR_SEQ 1559 1631 Missing (in isoform E).
FT /FTId=VSP_005144.
FT VAR_SEQ 1626 1631 VDAPDR -> PSSMICKDSKGGNIDVLESQQQQQQQQQQQP
FT NQGGHNITTISAINGYNTLQHRRKSQLITFSSSSCDIKNSL
FT SHEYINGSNGSAANGPPSSGSGSGSGPGSNRASRANVRLSF
FT AEEDVMILPQNHSQQSNHQDDEVFTRRRSLLEVEIGVEVGE
FT DGELAPHEMEEDLEEEDEDEELYMHDEFETHIDTKSNNAND
FT DSGGGSYEDSHALHSSLGGSNRNSLEKDDDDIEVDVISTDV
FT SCYDQLLGSSCNTRNGDDDDIATLVGDGDYSTTKLSKASRL
FT SGAGVGGLVVSGGGGGTAIGGGIAVNGGGVLGNGVGSEAGG
FT GIIYANPFMDDEGIAESGM (in isoform A).
FT /FTId=VSP_015266.
FT CONFLICT 124 124 D -> I (in Ref. 1; AAA28484).
FT CONFLICT 127 127 S -> L (in Ref. 1; AAA28484).
FT CONFLICT 188 188 P -> L (in Ref. 5; AAO42638).
FT CONFLICT 369 369 F -> S (in Ref. 1; AAA28484 and 2;
FT AAA28952).
FT CONFLICT 558 558 G -> A (in Ref. 1; AAA28484 and 2;
FT AAA28952).
FT CONFLICT 810 810 L -> S (in Ref. 1; AAA28484 and 2;
FT AAA28952).
FT CONFLICT 1403 1403 N -> S (in Ref. 5; AAO42638).
FT HELIX 1254 1256
FT HELIX 1257 1277
FT TURN 1278 1285
FT HELIX 1290 1292
FT TURN 1294 1296
FT HELIX 1297 1299
FT HELIX 1309 1311
FT STRAND 1312 1314
FT TURN 1319 1321
FT TURN 1322 1325
FT STRAND 1326 1332
FT STRAND 1340 1344
FT HELIX 1349 1351
FT HELIX 1352 1361
FT STRAND 1366 1369
FT STRAND 1373 1375
FT STRAND 1387 1390
FT STRAND 1392 1394
FT STRAND 1397 1406
FT STRAND 1408 1419
FT STRAND 1422 1431
FT STRAND 1436 1438
FT HELIX 1444 1457
FT STRAND 1464 1467
FT STRAND 1469 1472
FT HELIX 1473 1487
FT TURN 1488 1490
FT STRAND 1492 1494
FT HELIX 1496 1506
FT HELIX 1514 1528
SQ SEQUENCE 1631 AA; 185081 MW; 22A59AB61665875D CRC64;
MLYQLSKATT RIRLKRQKAV PQHRWLWSLA FLAAFTLKDV RCADLAISIP NNPGLDDGAS
YRLDYSPPFG YPEPNTTIAS REIGDEIQFS RALPGTKYNF WLYYTNFTHH DWLTWTVTIT
TAPDPPSNLS VQVRSGKNAI ILWSPPTQGS YTAFKIKVLG LSEASSSYNR TFQVNDNTFQ
HSVKELTPGA TYQVQAYTIY DGKESVAYTS RNFTTKPNTP GKFIVWFRNE TTLLVLWQPP
YPAGIYTHYK VSIEPPDAND SVLYVEKEGE PPGPAQAAFK GLVPGRAYNI SVQTMSEDEI
SLPTTAQYRT VPLRPLNVTF DRDFITSNSF RVLWEAPKGI SEFDKYQVSV ATTRRQSTVP
RSNEPVAFFD FRDIAEPGKT FNVIVKTVSG KVTSWPATGD VTLRPLPVRN LRSINDDKTN
TMIITWEADP ASTQDEYRIV YHELETFNGD TSTLTTDRTR FTLESLLPGR NYSLSVQAVS
KKMESNETSI FVVTRPSSPI IEDLKSIRMG LNISWKSDVN SKQEQYEVLY SRNGTSDLRT
QKTKESRLVI KNLQPGAGYE LKVFAVSHDL RSEPHAYFQA VYPNPPRNMT IETVRSNSVL
VHWSPPESGE FTEYSIRYRT DSEQQWVRLP SVRSTEADIT DMTKGEKYTI QVNTVSFGVE
SPVPQEVNTT VPPNPVSNII QLVDSRNITL EWPKPEGRVE SYILKWWPSD NPGRVQTKNV
SENKSADDLS TVRVLIGELM PGVQYKFDIQ TTSYGILSGI TSLYPRTMPL IQSDVVVANG
EKEDERDTIT LSYTPTPQSS SKFDIYRFSL GDAEIRDKEK LANDTDRKVT FTGLVPGRLY
NITVWTVSGG VASLPIQRQD RLYPEPITQL HATNITDTEI SLRWDLPKGE YNDFDIAYLT
ADNLLAQNMT TRNEITISDL RPHRNYTFTV VVRSGTESSV LRSSSPLSAS FTTNEAVPGR
VERFHPTDVQ PSEINFEWSL PSSEANGVIR QFSIAYTNIN NLTDAGMQDF ESEEAFGVIK
NLKPGETYVF KIQAKTAIGF GPEREYRQTM PILAPPRPAT QVVPTEVYRS SSTIQIRFRK
NYFSDQNGQV RMYTIIVAED DAKNASGLEM PSWLDVQSYS VWLPYQAIDP YYPFENRSVE
DFTIGTENCD NHKIGYCNGP LKSGTTYRVK VRAFTGADKF TDTAYSFPIQ TDQDNTSLIV
AITVPLTIIL VLLVTLLFYK RRRNNCRKTT KDSRANDNMS LPDSVIEQNR PILIKNFAEH
YRLMSADSDF RFSEEFEELK HVGRDQPCTF ADLPCNRPKN RFTNILPYDH SRFKLQPVDD
DEGSDYINAN YVPGHNSPRE FIVTQGPLHS TRDDFWRMCW ESNSRAIVML TRCFEKGREK
CDQYWPNDTV PVFYGDIKVQ ILNDSHYADW VMTEFMLCRG SEQRILRHFH FTTWPDFGVP
NPPQTLVRFV RAFRDRIGAE QRPIVVHCSA GVGRSGTFIT LDRILQQINT SDYVDIFGIV
YAMRKERVWM VQTEQQYICI HQCLLAVLEG KENIVGPARE MHDNEGYEGQ QVQLDENGDV
VATIEGHLSH HDLQQAEAEA IDDENAAILH DDQQPLTSSF TGHHTHMPPT TSMSSFGGGG
GGHTNVDAPD R
//
