ID A0A2D0T3H8_ICTPU Unreviewed; 1260 AA.
AC A0A2D0T3H8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=ptpro {ECO:0000313|RefSeq:XP_017349468.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017349468.1};
RN [1] {ECO:0000313|RefSeq:XP_017349468.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017349468.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_017349468.1; XM_017493979.3.
DR AlphaFoldDB; A0A2D0T3H8; -.
DR STRING; 7998.ENSIPUP00000007454; -.
DR GeneID; 108279665; -.
DR KEGG; ipu:108279665; -.
DR CTD; 5800; -.
DR OrthoDB; 5395787at2759; -.
DR Proteomes; UP000221080; Chromosome 19.
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; cd00063; FN3; 3.
DR CDD; cd14614; R-PTPc-O; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; IPR042996; PTPRO.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR47028; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE O; 1.
DR PANTHER; PTHR47028:SF1; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE O; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 4.
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; 3.
DR PROSITE; PS50853; FN3; 4.
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 Receptor {ECO:0000313|RefSeq:XP_017349468.1};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1260
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012316486"
FT TRANSMEM 864..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 924..945
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 370..465
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 475..571
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 572..674
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 769..859
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 982..1239
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1156..1230
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 240..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1260 AA; 141531 MW; D97A0CC8B9E1A14D CRC64;
MTSTLPHVLS LLLLLLLSIQ TAVSFEVTIQ DDDCIAMTLE PSDLRDNITA YAARISGEPR
THILPFQRTS DGQPAPAVLL YNTTYHGLCY TVGLVLANGS TWTKPVKTVT LLTKPLPLES
VQISDYQPAP ETGVVFELRS PERNSFSRVN ISYSEGRDQR FMLYKDFQKG KTVFKHWLPG
TCYSNITFRL ISEATVNKST LVKKSDVIHE PHRHRTVPNP PLNVSLKIVH LNEGGLPVTN
WRDKASPDAR LPRKAREVPL MEEQLETEAR DKPEDRRPDE ELQSVTQGPL ATAESLNSST
EAPFVNAVNA YTPTESVPAN TSDVSESRNS TASYWPTGGP SPAEGEYEFV NGVAPEYEDS
KELGSAMDLS PEPTDGSNRP PSIRLELRWL PPPPPATTDG FNVYVSRDGD PTETAVVDEN
THEFFTELSE AGTYRVLVTS VSSSGECEPR ESAPHRGFTF YLSPTGEWLE QPKERPQAVS
VKMLGKSTAS VSWAPSTQGH NGSLVSVVSL TCLKPSLSQR METTYCSEEN TTSDIIVNLT
PGAQYRVVVY HTNGPLISPP SEPVIIDIEP TGVRDLVVYP LSPTAVILSW QRPYNVAFRK
YVLQTFYFNS AMQTAQWTTY YEIAATASVI ASVRVTDLLP AWYYNFRVTM VTWGDPPLSC
CDGSTVSFVT APEAPHISSV DYSHGVLYVR WTYGDLFTDL SHSRMLHWQV LAEGKKGSRR
RFSTDVMRNV MKAALALPPG DIYNLTVTAC TERSRNTSIP HILKLDPAPP KSLYAVNATH
SAVTLLWTEE GVVDFYQVSC RQLGPITQLK AAEPQTAHSH VVTVNNLQAS TSYNCSVISY
SYSTPSEPTY ITISTLAQEM NPSIAAISAL AVLSVLLISL LVLFLLVLRK KHMQMTRECG
AETFVNFASF ERDGKLPYNW RRSLFAFLTL LPSCLWTDYL LAFYINPWSK TALKKRKLTS
PVQLDDFEAY IKDMGKDSAY KFSLQFEELK SVGLDLSHDA ADLPVNRPKN RYTNILPYDF
SRVKLISMHN DEGSDYINAN YIPGYKSPRE YIATQGPLPE TRNDFWKMVM QQNSRVIVML
TQCNERRRVK CDHYWPFTDE PVSYGEITVE MLSESDSPEW TVRNFRLSYA DEVQDVLHFN
YTSWPDHGVP TVNAIESILQ FVQLVRQQVN RTKGPVTVHC SAGVGRTGTF IALDRLMQHI
REHEYADILG MVSEMRSHRL SMVQTEEQYV FIHQCVLLMW KKKKQQSLTS DVIYENVTKS
//
