ID D6WSY8_TRICA Unreviewed; 907 AA.
AC D6WSY8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=AUGUSTUS-3.0.2_09605 {ECO:0000313|EMBL:EFA06675.2};
GN ORFNames=TcasGA2_TC009605 {ECO:0000313|EMBL:EFA06675.2};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA06675.2, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:EFA06675.2, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA06675.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2] {ECO:0000313|EMBL:EFA06675.2, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA06675.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001490};
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DR EMBL; KQ971352; EFA06675.2; -; Genomic_DNA.
DR AlphaFoldDB; D6WSY8; -.
DR STRING; 7070.D6WSY8; -.
DR EnsemblMetazoa; TC009605_001; TC009605_001; TC009605.
DR HOGENOM; CLU_305963_0_0_1; -.
DR InParanoid; D6WSY8; -.
DR OMA; HCIVMAT; -.
DR Proteomes; UP000007266; Linkage group 7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0048666; P:neuron development; IEA:UniProt.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00047; PTPc; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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:SF550; PROTEIN-TYROSINE-PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
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; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..125
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 369..605
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 522..596
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 663..896
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 814..887
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 907 AA; 104030 MW; A8D16962E59F545D CRC64;
MFSETRCDEM NGPLWYQMAY NCTKKSQPPY DLQMKWTPKN DLELEWKHPN ATNGEIKYFS
IRLFSMSDAG FLHNLTINNY NLTYHFKLNS DEIQPTTSYR LQIAACNERG EGEFLTGDNT
SPPDVPKVDL HTESSNETIT VKFDTNELRG KTDSLRLLLF ISEKSGNAKL ENNIVTGLQN
LKLVSNCTSN SISFKSLTIG NNQQSTHCTQ MDNPPLKPGT PYNITVVLIN YFNQTNRTNL
FTISTTTKST SIYAGPNLNL LALLVLLLAI PLIVLYFKRH AILSWIQRIQ REDTNEIPDV
KDDQIPLTGL TPQITQTRNP RNEAKPKIPS KCIKIMEFEM YVKESIQSGE LDRQHALFPR
GQTKPWNYGS LKENKSKNRY NNLIAYDHSR VILQKIKGDS YSDYINASYI DGHKISKAYI
ATQGPKAVTL NDFWRMVWEQ NVMHIANLAN VYEGGKKKVE KYWPDINETL QFGTISVQHL
STQVFADYEH RFFSVCQNNE IRKIDQLHFM SWPDHGVPLY SQSLVPFLQK LLKFPLSTYS
PIVVHCSAGV GRTGTILLCD ICLRMAAREG TIDVLRNLEH LRQQRANMVD NIEQYKLAHL
VILECLVGMH TSIGCTEIKD SVNRILANGT ATLQMRYLKN TQWQDQAMKT VAQIVEEVPI
IEEKNRFKGI IPEIQGRVFL SRFPSEDETS SYINAVKVDG FRSPGRFIVT QQPMPNTLGD
FWRLVEENDI RVILSLNDVN LKNKTSCRFW PTRSNPEMTP VPHITLKYLK NDLSESYNIT
TVQLIANSRK EQFSVQIISV KHWTSGNNCP DNIGNFLTFW QESDAISRRS NPILVTCYDG
VTASGLYVAL SFVIEKMNLE QVCDVCQAVR SVRHNREQFV QNVEQFEFLY KAALLYIDRF
ESYANFN
//
