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Database: UniProt
Entry: A0A484D369_PERFV
LinkDB: A0A484D369_PERFV
Original site: A0A484D369_PERFV 
ID   A0A484D369_PERFV        Unreviewed;      3598 AA.
AC   A0A484D369;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=EPR50_G00089430 {ECO:0000313|EMBL:TDH09692.1};
OS   Perca flavescens (American yellow perch) (Morone flavescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX   NCBI_TaxID=8167 {ECO:0000313|EMBL:TDH09692.1, ECO:0000313|Proteomes:UP000295070};
RN   [1] {ECO:0000313|EMBL:TDH09692.1, ECO:0000313|Proteomes:UP000295070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YP-PL-M2 {ECO:0000313|EMBL:TDH09692.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:TDH09692.1};
RA   Feron R., Morvezen R., Bestin A., Haffray P., Klopp C., Zahm M., Cabau C.,
RA   Roques C., Donnadieu C., Bouchez O., Christie M., Larson W., Guiguen Y.;
RT   "A chromosome-scale genome assembly of the yellow perch, Perca
RT   flavescens.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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};
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:TDH09692.1}.
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DR   EMBL; SCKG01000008; TDH09692.1; -; Genomic_DNA.
DR   STRING; 8167.A0A484D369; -.
DR   OrthoDB; 2873210at2759; -.
DR   Proteomes; UP000295070; Chromosome 8.
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   CDD; cd00037; CLECT; 1.
DR   CDD; cd00063; FN3; 18.
DR   CDD; cd14616; R-PTPc-Q; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 23.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
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; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 14.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00060; FN3; 27.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 16.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS50853; FN3; 21.
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000295070};
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..3598
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019786319"
FT   TRANSMEM        3191..3210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          106..206
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          210..331
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          462..565
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          764..851
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          938..1026
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1111..1204
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1205..1299
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1447..1535
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1538..1637
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1707..1811
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1812..1907
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1912..2001
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2006..2095
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2100..2187
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2192..2293
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2298..2400
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2405..2493
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2497..2590
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2594..2685
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2686..2806
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2811..2905
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2910..3008
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3303..3558
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          3476..3549
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          381..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1629..1667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1715..1737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..404
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3598 AA;  394580 MW;  158C32F59FD46459 CRC64;
     MGGTERLWLL ASLCQVVLLT CEQHLNPVEV EVVFQSFPSI KDADTYTVTC RTASNQLVYV
     EPFKHSACSP DCKMSLRLVE DPGGYNITLR ASRNDATLEA KTFHFIPASP SSLHVYSTTT
     TALLTWRLHR QQSLSTLSLY NTQTQSVTHI FNVNSSEANS WYTVKGLQPG TRFKAKVVVT
     TFLKHLNMTL EQSLSSGMET AQCPPDWLAD GRSCYTVRRT GLTWSDAQHR CRGLAAGSHL
     ADLKTLEDLL FISSHLRSHN NLLLLWTGLN DQQEEGKPLW SDGSVYNLTN TMMSLLPANQ
     TDCFALQRNA TGPGYFLTPF FCNIPLPFIC HCQTPTAPAS LSFDLVQVTE QHVELHWSDL
     SPLNSLNLSS FEIFLQYQEE TNGESGQGEE DSGRKSEDKK RTQSQSSITK IVRVPIFLSS
     RGVTVAGLSP GSIYTFTLQA SHPAGFAWSL GQTRTAYTRP LPPQNITVGS VSVSQISVHW
     MMMDAQFRVG WTFVVRYVDM SSRQERIVGM TNNSRLSETG GLQSYTAVIG GLESYREYRV
     EVYTVTQHGI ESCGQAPVTV LTAVRAPRGL EVLSTTGNLT VCWTSSPDDP SDGYYITSHP
     LINPTPTSLW INQSSPGAHW VNESVCVNLG TFTPGQTYEV GVVSLRGKDR SKRTSVIHTT
     DPMPVQVAVS LSVGTNSAQL YIQQPQLGLI DGVKVCVCPG MCDSLCEGLC GNTCDWYSLP
     AGVHIITISN LSPGSDHQLR VYSTSREKIG PPYYTHPVRT NQAPPIRVRE GVVTDSSIEL
     LWDPAQGQAL SYEVICLNCD HSHMVQKVFS QSATFSSLTP CRFYHFAVRT EKESFTDSSP
     VTINITAAPS PVKVSLVNKT TSSIHICWSM LGGVTSGLIL SIKNRTSSQE LIISPQEARS
     YSFEGLAYGS QYTIEVISTC RERRSKPAAM ILHTLPEVPQ EVALSEQVVT SVFVTWRPPP
     GQVEGYKLVF GLRSVDRKSW IEVLVRGARY EIRDLIPGSD YGVSIQSVLG SDTSQAVHRE
     FSTRPAGLCG LHLDNMNSSS VSVSWDSAFG GFDFHKVTVA NTSVTNTLTV AKEERVAVVT
     GLVAGCSYNV SAERVRGVTA GSAAFLTVTT VPVRVHGVRV VNVSARAFSL RWEQAAGCVD
     HYQVNLLPNQ GKVTVHPAHD GYIQADVVNV SPRTQYSVTV TAASSSNISP GVSRMINTNE
     SVPGPPLNLE GEAVGSNGIL LSWTMPRYTS NIDGYVIRYK EVCPYPDPTF TQVTKYLDVP
     ETLLTEFTSG STYHIQVAAI APAGIGAFSK SLYIKTSESP PGLVTNLTAF AQNHTFVVVT
     WFLPHRINGL ITKFAVKAKH ARTGQTVRIL EVNAEDIMTG ALPHCNDAAD ILSRATLSPL
     GITASSSPIT LSAVPPAASW SVPISVGVDQ LRPYTAYLFE VSAFTSDGEG QIASTMVRMP
     ESAPEDPPQN FFILNMTSRS ISVSWSSPRI ITGKFTYVLY LYGPTGYLFE NSTGDTRFAL
     SGLTPYTRYT VAVRAKAAGE VGPAAEDVII TPAEAPSAVQ DLMAEAEDSV SIRVSWRMPA
     QPNGPITQYK LQVLVAEILL QDITLTAEMN TTGLHKDKTL PPDVRNYPGR RKRTAELSLI
     TSPPTFTAAI SDRTLPTGAT ASSLTHSGQR SADPITNTNA QSTAHSMVTE KSSTSYISAS
     YSTSIQSSAV SGTSAFSLTS VPPATLPPWL TRQSHAGDMT SDSSPLALTP GQLRSSTHDA
     SVTGHFLTRS ATATGTTGVT VREEVMNVLS EELSYLVSDL NPFTEYTFRV TASTTVGEGP
     ATNITEKTRE QVPSSVLEVS YQNISSTSIL VSWIPPLNPN GRITHYTVYG LKLHSNQALK
     WVTNATSILI TDLDKYTGYK LRVAASTAVG ESSLSEEDDI FVVTLEDEPD SPPVNLTVVD
     TSPSTTTLAW SAPEQANGMI QRYEVLYENE SFSALMNTSS NTITLKNLKP FSNYTVSVRA
     YTRYGHGNQT SDALYLLSGE DVPGSPPYGV TYESLSPSEV NVTWQPPLLP NGVITHYSLE
     LWNSSHYLNL TSPTNNIHIT HLRKYARYRV MVQAHTRVGA GNYSSEPLNI TTLEDAPDTP
     PQFLHAKKLS DYEVELSWQP PLEANSDILY YIVRVWNETT ELWQNVTGTS VVINVDSESR
     YNASVSSWNR LGDGGVLIYI SFNTINAEPF DPPRNVTFTN VTTSSVNLLW HPPAEPNGII
     VHYTIYYSYD NTVAEQRVPI SDLGAPASPD SALSYTLTRL IGGTNYTLWM TSSTAQGDGG
     VQSEPLTLFL PEDVPSDSVQ NLTAQIFSST AIIVSWDPPM EPNGRPTYLL TLQEAGTPPD
     VSNQGAPAVN KTISRNTTDN VFLFTRLKKY FPYVLTVTPA TGAGAAYNHT STMYLRTDDD
     IPSSAPLLVS TRNLSSSSIV IVWQRPLEAN GEITEYTLTV FGPGGSSTSH TPSTSFTLTN
     LLPYTAYNLT VTAATRKGSG PYLLLQLHTD EGGPMSPPRN LTIYNHTAVS VLLSWEPPLE
     PNGVVIQYGF RIRDLITHTV THRNSSGPST TEYLSGFRPH SSYEISVYTY TRVGHGNQFS
     SPVTFTTNES VADAVGNLSC SGVSWDSIQL FWELPANPNG QIIFYEILLK VDSQSYTHQA
     HLPEYTVTGL SPDQEYTLTV AAVNSAGSGD SLNCTASTLS ESAPAAPRFL TISQVTPNNV
     TLQWAPPLSI PGLLKEYHVI AQLLSTVCEP NTLTTAQPSP EDELTSDCVD SNVTVSVNAS
     DGIEKNHSVT FQSLAKYRYY RFKVAAVTNA GVGEYTHWNY ARTLAGNPDD PPRDLKVTPT
     SKGLHIAWDA PAVLSGPTSY LVQVDGPGLN ISTVRAPGEL TTVVVTNLTA FTRYLVTITA
     FIGPLKHAAS QGKAIGPIEF QTLEEEPKDP PKNVVVSVMQ EEVNRVKVTF FPPEEPNGNI
     TAYFVYVYEK EQLIKNISLN ITQRDQDMLT AVIEGLKGGH SYSIQISARN GAGRSPPSPH
     VQITTGIKAP AKPTQRPQAV LGHGGVAMVT HRSITIHMPA CFYSDDNGPI TKIQVIVAES
     GVKDMQNLTN WKNAFFDRPA PYLTDKGFPN PSCDLGDGAL PTDTRVRGGR SVSRGGGPLV
     RKNHTTYVIG ENDDCVKENN TDNFCNGPLK PKTVYVFRFR ATNINGQYTD SEYSEHVRTA
     VDGLLTRDEQ IILGVLLSFF LAVLLIIIIC GSVKIHQRKK EGGTYSPREA EIIETKCKLD
     QLIAVADLEL KQEKLNRYSS FFFRRKEIYV IQLLSYRKSL KPVNKKSFLQ HVEDLCANDN
     SKFQEEFAEL PKLLQDLATT DADLPWNKSK NRFPNIKPYN NNRVKLLSEP GSAGSDYINA
     SFVSGYLCPN EFIATQGPLP GTVADFWRMI WETGTHTIAM LTQCYEKGRI RCHKYWPEDN
     KPMSVFSDIL ISKVSEEVLP DWTVRTLKVE KHGHYILVRH FNYTSWPEHG VPESCSTLIK
     FVKAVRAHRH DNTTIVVHCS AGVGRTGVFI ALDHLIQHIR DHDFVDIYGL VAELRSERMC
     MVQNLAQYIF LHQSTLELLN NKGNSQSIWF VSYSALEKMD SLEAMEGDVE LEWEETTM
//
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