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P35832 (PTP99_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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 99A

EC=3.1.3.48
Alternative name(s):
Receptor-linked protein-tyrosine phosphatase 99A
Short name=DPTP99A
Gene names
Name:Ptp99A
ORF Names:CG2005
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1301 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May play a key role in signal transduction and growth control. May have a role in the establishment of the intersegmental and segmental nerves. Ref.1

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Selectively expressed in a subset of axons and pioneer neurons (including aCC and RP2) in the embryo. Ref.1 Ref.2 Ref.3

Developmental stage

Start of expression coincides with the onset of axonogenesis. Ref.1

Sequence similarities

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

Contains 3 fibronectin type-III domains.

Contains 2 tyrosine-protein phosphatase domains.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P35832-1)

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 A (identifier: P35832-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1050-1119: Missing.
Isoform C (identifier: P35832-3)

The sequence of this isoform differs from the canonical sequence as follows:
     238-238: R → REFNYVFIWGLFGVKG
     1050-1119: Missing.
Note: No experimental confirmation available.
Isoform D (identifier: P35832-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1050-1058: GNVPQHVIL → AQQRQMLKT
     1059-1301: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 13011273Tyrosine-protein phosphatase 99A
PRO_0000025429

Regions

Topological domain29 – 394366Extracellular Potential
Transmembrane395 – 41521Helical; Potential
Topological domain416 – 1301886Cytoplasmic Potential
Domain66 – 165100Fibronectin type-III 1
Domain173 – 26997Fibronectin type-III 2
Domain270 – 376107Fibronectin type-III 3
Domain476 – 741266Tyrosine-protein phosphatase 1
Domain764 – 1016253Tyrosine-protein phosphatase 2
Compositional bias34 – 6734Ser-rich
Compositional bias1054 – 109138Gln-rich
Compositional bias1124 – 11285Poly-Ser
Compositional bias1228 – 125225Gln-rich

Sites

Active site6821Phosphocysteine intermediate By similarity

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence2381R → REFNYVFIWGLFGVKG in isoform C.
VSP_015261
Alternative sequence1050 – 111970Missing in isoform A and isoform C.
VSP_005142
Alternative sequence1050 – 10589GNVPQHVIL → AQQRQMLKT in isoform D.
VSP_015262
Alternative sequence1059 – 1301243Missing in isoform D.
VSP_015263

Experimental info

Sequence conflict461V → A in AAF56891. Ref.4
Sequence conflict461V → A in AAN14172. Ref.4
Sequence conflict461V → A in AAS65222. Ref.4
Sequence conflict461V → A in AAX53004. Ref.4
Sequence conflict681F → S in AAF56891. Ref.4
Sequence conflict681F → S in AAN14172. Ref.4
Sequence conflict681F → S in AAS65222. Ref.4
Sequence conflict681F → S in AAX53004. Ref.4
Sequence conflict831S → T in AAF56891. Ref.4
Sequence conflict831S → T in AAN14172. Ref.4
Sequence conflict831S → T in AAS65222. Ref.4
Sequence conflict831S → T in AAX53004. Ref.4
Sequence conflict1081A → E in AAF56891. Ref.4
Sequence conflict1081A → E in AAN14172. Ref.4
Sequence conflict1081A → E in AAS65222. Ref.4
Sequence conflict1081A → E in AAX53004. Ref.4
Sequence conflict1161A → V in AAF56891. Ref.4
Sequence conflict1161A → V in AAN14172. Ref.4
Sequence conflict1161A → V in AAS65222. Ref.4
Sequence conflict1161A → V in AAX53004. Ref.4
Sequence conflict5861R → P in AAA28483. Ref.3
Sequence conflict11331T → P in AAF56891. Ref.4
Sequence conflict11331T → P in AAN14172. Ref.4
Sequence conflict11331T → P in AAS65222. Ref.4
Sequence conflict1167 – 117610ASPVTPATAS → GSPAT in AAF56891. Ref.4
Sequence conflict1167 – 117610ASPVTPATAS → GSPAT in AAN14172. Ref.4
Sequence conflict1167 – 117610ASPVTPATAS → GSPAT in AAS65222. Ref.4
Sequence conflict12051N → H Ref.1
Sequence conflict12051N → H Ref.3

Sequences

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

Last modified August 30, 2005. Version 2.
Checksum: AB1FB7A8F5D7D30F

FASTA1,301145,396
        10         20         30         40         50         60 
MPRPQHHALL RAMLKLLLFA SIAEHCATAL PTNSSNSPSS PSPFTVASLP PTTASSSSSP 

        70         80         90        100        110        120 
AVISTSSFDR NLADLVNPEA ETSGSGWESL ETEFNLATTV DSSTQKTAKE PVLGTAATSI 

       130        140        150        160        170        180 
EQQDQPPDVP ATTLAFANAF PVPVAGEMGN GNGNYNDATP PYAAVDDNYV PSKPQNLTIL 

       190        200        210        220        230        240 
DVSANSITMS WHPPKNQNGA IAGYHVFHIH DNQTGVEIVK NSRNSVETLI HFELQNLRPY 

       250        260        270        280        290        300 
TDYRVIVKAF TTKNEGEPSD QIAQRTDVGG PSAPAIVNLT CHSQESITIR WRRPYEFYNT 

       310        320        330        340        350        360 
IDFYIIKTRL AGQDTHRDIR INASAKELET AMILQNLTTN SYYEVKVAAA TFSVINPKKI 

       370        380        390        400        410        420 
VLGKFSESRI IQLQPNCEKL QPLLRQSHND YNLAVLVGII FSCFGIILII MAFFLWSRKC 

       430        440        450        460        470        480 
FHAAYYYLDD PPHHPNAPQV DWEVPVKIGD EIRAAVPVNE FAKHVASLHA DGDIGFSREY 

       490        500        510        520        530        540 
EAIQNECISD DLPCEHSQHP ENKRKNRYLN ITAYDHSRVH LHPTPGQKKN LDYINANFID 

       550        560        570        580        590        600 
GYQKGHAFIG TQGPLPDTFD CFWRMIWEQR VAIIVMITNL VERGRRKCDM YWPKDGVETY 

       610        620        630        640        650        660 
GVIQVKLIEE EVMSTYTVRT LQIKHLKLKK KKQCNTEKLV YQYHYTNWPD HGTPDHPLPV 

       670        680        690        700        710        720 
LNFVKKSSAA NPAEAGPIVV HCSAGVGRTG TYIVLDAMLK QIQQKNIVNV FGFLRHIRAQ 

       730        740        750        760        770        780 
RNFLVQTEEQ YIFLHDALVE AIASGETNLM AEQVEELKNC TPYLEQQYKN IIQFQPKDIH 

       790        800        810        820        830        840 
IASAMKQVNS IKNRGAIFPI EGSRVHLTPK PGEDGSDYIN ASWLHGFRRL RDFIVTQHPM 

       850        860        870        880        890        900 
AHTIKDFWQM VWDHNAQTVV LLSSLDDINF AQFWPDEATP IESDHYRVKF LNKTNKSDYV 

       910        920        930        940        950        960 
SRDFVIQSIQ DDYELTVKML HCPSWPEMSN PNSIYDFIVD VHERCNDYRN GPIVIVDRYG 

       970        980        990       1000       1010       1020 
GAQACTFCAI SSLAIEMEYC STANVYQYAK LYHNKRPGVW TSSEDIRVIY NILSFLPGNL 

      1030       1040       1050       1060       1070       1080 
NLLKRTALRT EFEDVTTATP DLYSKICSNG NVPQHVILQQ QQLHMLQLQQ QHLETQQQQQ 

      1090       1100       1110       1120       1130       1140 
QQQQQQQQQQ QTALNETVST PSTDTNPSLL PILSLLPPTV APLSSSSSTT PPTPSTPTPQ 

      1150       1160       1170       1180       1190       1200 
PPQTIQLSSH SPSDLSHQIS STVANAASPV TPATASASAG ATPTTPMTPT VPPTIPTIPS 

      1210       1220       1230       1240       1250       1260 
LASQNSLTLT NANFHTVTNN AADLMEHQQQ QMLALMQQQT QLQQQYNTHP QQHHNNVGDL 

      1270       1280       1290       1300 
LMNNADNSPT ASPTITNNNH ITNNNVTSAA ATDAQNLDIV G 

« Hide

Isoform A [UniParc].

Checksum: DD38E6D4A8505FD2
Show »

FASTA1,231137,399
Isoform C [UniParc].

Checksum: 0517A4F8753FF168
Show »

FASTA1,246139,157
Isoform D [UniParc].

Checksum: 211DA48DE1DD067C
Show »

FASTA1,058119,563

References

« Hide 'large scale' references
[1]"Two Drosophila receptor-like tyrosine phosphatase genes are expressed in a subset of developing axons and pioneer neurons in the embryonic CNS."
Yang X., Seow K.T., Bahri S.M., Oon S.H., Chia W.
Cell 67:661-673(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Embryo.
[2]"Three receptor-linked protein-tyrosine phosphatases are selectively expressed on central nervous system axons in the Drosophila embryo."
Tian S.-S., Tsoulfas P., Zinn K.
Cell 67:675-685(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY.
Tissue: Embryo.
[3]"Cloning and characterization of a receptor-class phosphotyrosine phosphatase gene expressed on central nervous system axons in Drosophila melanogaster."
Hariharan I.K., Chuang P.-T., Rubin G.M.
Proc. Natl. Acad. Sci. U.S.A. 88:11266-11270(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), TISSUE SPECIFICITY.
Tissue: Eye imaginal disk.
[4]"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.
[5]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80464 mRNA. Translation: AAA28486.1.
M80539 mRNA. Translation: AAA28485.1.
M81795 mRNA. Translation: AAA28483.1.
AE014297 Genomic DNA. Translation: AAF56891.3.
AE014297 Genomic DNA. Translation: AAN14172.1.
AE014297 Genomic DNA. Translation: AAS65222.1.
AE014297 Genomic DNA. Translation: AAX53004.1.
PIRA41622.
RefSeqNP_476816.1. NM_057468.3.
NP_733288.1. NM_170409.3.
NP_996302.1. NM_206579.3.
UniGeneDm.4029.

3D structure databases

ProteinModelPortalP35832.
SMRP35832. Positions 455-742.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68335. 1 interaction.

Proteomic databases

PaxDbP35832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID43469.
KEGGdme:Dmel_CG11516.

Organism-specific databases

CTD43469.
FlyBaseFBgn0004369. Ptp99A.

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000148805.
InParanoidP35832.
KOK16667.
OrthoDBEOG7288S7.
PhylomeDBP35832.

Gene expression databases

BgeeP35832.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 2 hits.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
PROSITEPS50853. FN3. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPtp99A. drosophila.
GenomeRNAi43469.
NextBio834086.

Entry information

Entry namePTP99_DROME
AccessionPrimary (citable) accession number: P35832
Secondary accession number(s): Q59DT5 expand/collapse secondary AC list , Q7KRW3, Q8IMK9, Q9VAL3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 123 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