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Database: UniProt
Entry: A0A1S3J8F9_LINUN
LinkDB: A0A1S3J8F9_LINUN
Original site: A0A1S3J8F9_LINUN 
ID   A0A1S3J8F9_LINUN        Unreviewed;      1181 AA.
AC   A0A1S3J8F9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=LOC106170987 {ECO:0000313|RefSeq:XP_013406516.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013406516.1};
RN   [1] {ECO:0000313|RefSeq:XP_013406516.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013406516.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class 4 subfamily. {ECO:0000256|ARBA:ARBA00034734}.
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DR   RefSeq; XP_013406516.1; XM_013551062.1.
DR   AlphaFoldDB; A0A1S3J8F9; -.
DR   EnsemblMetazoa; XM_013551062.1; XP_013406516.1; LOC106170987.
DR   GeneID; 106170987; -.
DR   OrthoDB; 5489271at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR047170; PTN12/18/22.
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; PTHR45983; TYROSINE PHOSPHATSE N18, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR45983:SF2; TYROSINE PHOSPHATSE N18, PUTATIVE-RELATED; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT   DOMAIN          28..291
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          205..282
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          396..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..969
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          983..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1158..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1054..1068
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1181 AA;  131183 MW;  27E81C71039C0952 CRC64;
     MSIREILEDF VRHTDSLDEK DDDGRDGFER DFAELKQRSL EYKNTYSSSA GQKLYNGVKN
     RYKDILPFEY TRVPLQPLPG LTGSDYINAN YVKGVSGHNT YIAAQAPLPT SVIDFWRMIW
     ENEVKVVLMA CNLREAGKTK CEKYWPELDR EVQFGDLLIT LTKEDHQSPD YTLRELEVRK
     ANICKVVYQL HYTAWPDHGV PDHYDYILDL VAEAREKQQQ ETLPIVVHCS AGCGRTGTII
     AIDYCWSLLK KGKLTKDFNL FNVIDEMRRQ RPSAVQTPDQ YWFVFMAVRE LFERHLRIIE
     RHSYENVQVG EGSTYEKEDS YDPYENVDVF ESTASINQED DYAIPEPAHG VVQAAASPFK
     GPSKPPQAAP ARIHPAEIAI EKTVAKLASK QADFLVPDSS GHVPRHPPEK GLGPSREERR
     EEYVNVDIPK STMAETGKPL LKTVVKRDPL PVQGQTEVQK RDEYVNVDLP KRTSIKEMDP
     MPAAKATVAR KPSNESRNLQ VADGVDQSSS YTIQGGTHVN AKVKSFEKTQ SSVDASSTRK
     SSADTMQKGH QAVQDSSLLK GQNVTVIAVK GENQEGRIFD RKDPVSPVMP YAIGNVHLKE
     NAHYEAVWPV QKEQNLPTQE AAHIQISSKE DDARSQSVSE LRQKLGSDLV LGSEQGKKSS
     TSEDHHKLNP LQKLKNKISG EGNLKSADHK KKKSFDEDKD HSGKDQHSKP HHEEKGGPLE
     HLKSAFQLGC GSCVSVDPAY AAVMQSQNAP LEKPPPHGVT PASDGFMKEL KAAQGGLRTA
     EPENRASTNV NQQQHGVINK THPIPLPSGV RKSQPMAQPQ AVPYAVSNVQ LRNSTHETVT
     GSHASSSDDI QPYASSSEFG LKGKTVQRGH NSDFEDEAAA PYSVTSEMGL FGRKKQENSF
     PSKSSATPPV AHEYADPFLD SQSTVSESSG EYAEPYSTTR ELFGKRSSQN DARPPALIPK
     IEETKEPNSL EYSYSFEHCK QMPLSSPKGF FDNSSVGGPN PKAPPRKKRS SQDGSPQGEG
     QTYEPVLLKS SERDVNPPGS RENRPTEVKQ PFQRPRAVSE DDDKPPPIPT KSEGAFLDVS
     QDVSEKPEES GPESGGKPKT TNVLEKLMSK VPMKSNKGRE PSLPSAGVST PAVFIPFKTD
     SDEALFCPPS HHPFFKKVEF PHRNERKPQG PRPMVGAWKL P
//
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