ID A0A0L0C3G8_LUCCU Unreviewed; 1018 AA.
AC A0A0L0C3G8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=FF38_06364 {ECO:0000313|EMBL:KNC26792.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC26792.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC26792.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC26792.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC26792.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC26792.1}.
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DR EMBL; JRES01000955; KNC26792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0C3G8; -.
DR STRING; 7375.A0A0L0C3G8; -.
DR EnsemblMetazoa; KNC26792; KNC26792; FF38_06364.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
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; cd14544; PTPc-N11_6; 1.
DR CDD; cd09931; SH2_C-SH2_SHP_like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR46257; TYROSINE-PROTEIN PHOSPHATASE CORKSCREW; 1.
DR PANTHER; PTHR46257:SF3; TYROSINE-PROTEIN PHOSPHATASE CORKSCREW; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT DOMAIN 270..364
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 386..786
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 697..777
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 18..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 114498 MW; 436F5E63E1009CA7 CRC64;
MIFNKYLLKI SNAVQHKNNK ENLKSSSSSS NHKNQQNSSQ SLDIPHTNNN NNNNNTAANR
NFEYERAIAA SYKQQQHTTQ HQQSQRNQHH HHHTTTSSSS SHLIPKKKKP KINVHNTNNT
KTHLTTDELA IIIKGGSNNN KTKRHTLKET STHNTQYSAT PPLRETKSSL TLNLSTSPSS
GVYSNAGSSF SSTPNSITLQ APPSSSSRSS SSTESLNSSE NGGTPYSSNV STPTSLPFAG
NPVWPLSGAA TLQISFELTL LHIRMWIYPW FHGNLSGKEG EKLLLERGKN GSFLVRESQS
KPGDFVLSVR TDDKVTNVMI RWQDNKYDVG GGEPFNTLSE LIEHYKRNPM VETCGTVVHL
RQPFNATRIT AAGINARVEQ LVKGGFWEEF EALQQDSRDI FSRNEGYKME NRNKNRYRNI
LPYDHTRVKL NDVDHTLAGA EYINANYIRL PTDGEQNNMN ASQESLNAMV SSCPACTAAQ
MQKNCPNCQI LNKTCVQCAV KTATLPYSNC TTCNKKNDNL SKQQHQQHKR SESLTNSALM
STSSNGCLSQ QQQQQPPPRP AAPSSATAAS RPLNKKNSND LTEREMFKTY IATQGCLANT
ITDFWNMIWQ ENTRVIVMTT KEYERGKNKC AKYWPDEGQC KQFGPAKIQC ISENSTNDYT
LREFLFSWRD QPERRIFHYH FQVWPDHGVP ADPGCVLNFL QDVNTKQGQL TQAGEKPGPI
CVHCSAGIGR TGTFIVIDMI LDQIDRHGLD TEIDIQRTIQ MVRSQRSGLV QTEAQYKFVY
YAVQHYIQTL IQRKRAEEQS LQVGREYTNI KYTGEIGNDT QRSPLPPNLS LASKQLQQQQ
QQQCANPTAT NCSSGSSSSS SSNNINNCND NINQQQQQST KSTSMFNKMP LPSPTTTPSS
RQKLQQHVAY ITNIQQQQLQ KQQQLLYSND LYQNSNSSSS NTTTPKHNEQ QQQQQQQQQQ
TGKQVSSTST TNSSSSSTTN TTTTRPDMMR HQNPHHLQQQ QQQQQHYAPP PPTPPRKT
//
