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Database: UniProt
Entry: T1JB95_STRMM
LinkDB: T1JB95_STRMM
Original site: T1JB95_STRMM 
ID   T1JB95_STRMM            Unreviewed;      1541 AA.
AC   T1JB95;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Protein-tyrosine-phosphatase {ECO:0008006|Google:ProtNLM};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR011033-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR011033-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
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; JH432010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 126957.T1JB95; -.
DR   EnsemblMetazoa; SMAR011033-RA; SMAR011033-PA; SMAR011033.
DR   eggNOG; KOG0791; Eukaryota.
DR   HOGENOM; CLU_001541_0_0_1; -.
DR   OMA; QLITDTH; -.
DR   OrthoDB; 5399547at2759; -.
DR   PhylomeDB; T1JB95; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0048666; P:neuron development; IEA:UniProt.
DR   CDD; cd00063; FN3; 8.
DR   CDD; cd14548; R3-PTPc; 1.
DR   CDD; cd12087; TM_EGFR-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
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; IPR041201; PTPRJ_TM.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 7.
DR   Pfam; PF18861; PTP_tm; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 11.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 6.
DR   PROSITE; PS50853; FN3; 7.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
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:UP000014500};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1541
FT                   /note="Protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004580126"
FT   TRANSMEM        1176..1198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..202
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          203..298
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          390..481
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          568..659
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          660..753
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          847..936
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          937..1034
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1255..1510
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1427..1501
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1517..1541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1541 AA;  174966 MW;  EC47467FDBBE221B CRC64;
     MTHLSSFPWL LAWVLLWLVL GFQCADVVIQ FLPDVANLGP DVLLRLNYNP PVGVPPANFT
     FHPGDIKHQG ISITEALPGT EYIFQLYFSN KTVSDLLTWS DRLHTVPDEP TDFSLMSRTT
     KTLQLKWDPP MRGGLSDYRL RVTPLTEPSK TSVRIIQIER DKVPFLLKDL TPGATYELKL
     SAMFHNKESL GFISRNMTTK PNAPGRFIVW FRNETTLLVL WQPPYPAGVF NQYKASIEPR
     DAVRSEVFVE KEIDPPGPAQ ADFNELIPGR NYNITVQTVS KGQLSAGTSA QYRTVPSPPR
     NISFDKKLIK TDGFSVTWLP PKMPCEFERY HVSLGIRFKT SLIVDRDSER IATFNEGLEP
     GRTYEIVVKT VSGNVASWPT TANVTTKPLP VTNLTATSLG KGVIHLSWSA NNSSIHDSFK
     VYYQDVEAFN DDGGLAGVTK DTAFVLSSLL DGHNYSISVE AISNNVASDE VVIFQATIPV
     SPIIKYLEPV RNGLNISWKS DVTSRQDSFE IVLIRNDTGE AFHRLTKEDR ILIDNLHAGA
     SYEVKVYALS YGLKSEPHAF YQTVYPNPPQ NLTILSFGNA TVRLHWNPPK SSLYDYYIIK
     YRGYGSLNSS WIEKGIVTNT TYDMMGLLPG NKYTIAIYTI SYRLESADAE KVELSLPPQA
     VSGVNVALDS FNVTFSWSLP IGFVEQYVVM YSSTTNPTDL TTKIIPYNFT NTDKINVVIS
     DLFPGELYHF QIYTVSHGAR SEPFLTQTRT KPRILSDVTT VVGNFETHSL SLRYTLTPNE
     ASIFDRYHFE LNDTTVLSQE KLKNDTHRYL TFTGLTPGQL YDIIVWTVSG KIQSNPIKRQ
     ERLYPEPISD MNATRITDSE ITLVWHPPQG EHSGYQVQYL QQDRLIQNET TIEKITFTNL
     RPHKNYTFTV IVVSGSGTAH IRNSRPYSKH FATLEAAPGK VHFFRAKEIR PSEITLLWAL
     PDFDQNGILL GFTVSFKKKN TKTFDKFEFP ADVTVGTIHN LTPGKTYIFM IEAKTKIGKG
     PAVMLEETMP IWPPPTPNNQ IFPTDVAHTT TTIRIRFRKS YFSSAHGAVV AYTIIVVEDD
     DKDSSGLELP TWYDVQTFAK WPAYQVNEPY NPFTNTTVEE FVIGTGGCVE TSRYCNGPLK
     PGSQYKVKIR AFTARDKFTD TVYSQVISTE RDNTSIIVAA VLVPLMLLIG AILIIVLLRR
     RRKTPFAKKT SKRNIAGKED SLSIPESIID TSRPSKLKEF PEHFRLMSAD SDFRFSEEYE
     ELKMVGRDLP RTAADIPVNR PKNRFTNILP YDHSRVKLLP TDDEEGSDYI NANYVSGYNS
     PREFIVTQGP LHSTRDDFWR MVWEQNCRAL VMLTRCIEKG REKCDHYWPY DTQPTTYGDI
     QVTILNESQY ADWTISEFKV CRGDHSRVVR HFHFTTWPDF GVPDPPQSLI RFVRTFRERI
     PSDQKPIVAH CSAGVGRSGT FIALDRILQH IQIHDYVDIF GIVYEMRKER VWMVQTEQQY
     ICIHQCLLCV MEGRENENPP RAEAHENEGY EDDEGIAESG M
//
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