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Database: UniProt
Entry: A0A2R2MNG0_LINUN
LinkDB: A0A2R2MNG0_LINUN
Original site: A0A2R2MNG0_LINUN 
ID   A0A2R2MNG0_LINUN        Unreviewed;       849 AA.
AC   A0A2R2MNG0;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=LOC106162742 {ECO:0000313|RefSeq:XP_023931750.1};
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_023931750.1};
RN   [1] {ECO:0000313|RefSeq:XP_023931750.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_023931750.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR   RefSeq; XP_023931750.1; XM_024075982.1.
DR   AlphaFoldDB; A0A2R2MNG0; -.
DR   EnsemblMetazoa; XM_024075982.1; XP_023931750.1; LOC106162742.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd14541; PTPc-N3_4; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014847; FA.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR041783; PTPN3/4_FERM_C.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR45706:SF4; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01195; FA; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50106; PDZ; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT   DOMAIN          1..249
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          431..517
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          579..835
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          752..826
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          320..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  97655 MW;  100E160C3753B01A CRC64;
     MCVHYCLHIL YLLFQFYFNF PLFLFPPVSV GPPYYFQFGV KFYVSDPSKL SEEYTRYHFF
     LQLKKDILEG KLVCPPTTAA LLASYAVQSE LGDYNPEEHT DGYLSEFRFI PNQTENFERE
     VSELHKQHKG QMPADAEYNY LDVVKRLDMY GVDVHLARDQ SNMDIQLGVA SAGLVVFQNS
     VKINTFSWAK IVKISFKRKQ FFIQLRREIG TNNNDNIDNL IGFYMTSYRS CKNLWKSCVE
     HHTFFRLHKP NPPIKKKLLS LGSKFRYSGR TEFQTLEDGK RRARIERTFS RSPSKRYARR
     TVGGTTRDVI MDEKNVLDGY RNAPVNNGPV NNHVKQSRSM NSTINLTRNY DGYGRSPRSS
     FQDYRRKSNT QWSDNQSEPD EGGFVPPVPA KMQDYYLDEN TSMSQQSFEL PDYHEFVPNG
     NGFVDGQGLV VIRMRPDDQG RFGFNVKSVN CRGRDPARPH QGGADQGMPI IVSRVAPGSP
     ADLCIPRLNE GDQVLQINRR DVSTHSHEQV VMFIRATREN HSGELELIVR PNVYVGDDPV
     EEPEFQYIPD THHISTTTHG DVLAESLLLL QEGIESGAAV AQFEQLYRKK PGMTMNAARL
     PENIPKNRYR DISPYDQTRV VIKNGPDYIN ANFVNMEIPG SGIVNRYIAA QGPLPNTVVD
     YWEMIWEQQS TLVVMLTTKM ERGRVKCHQY WPNLYETEDL GALQLTCLKE QETPSFAFRE
     FLLVNMDTNE ERHIVQMQYI AWPDHGVPDD SSDFLDFVIR VRQNRVGMVE PTVVHCSAGI
     GRTGVLITME TAMCLIEANQ PVYPLDIVRQ MRDQRAMLIQ TASQYRFVCE AILRVYSEGI
     VKPLDDYQR
//
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