ID L5KI40_PTEAL Unreviewed; 595 AA.
AC L5KI40;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000929};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000929};
GN ORFNames=PAL_GLEAN10015575 {ECO:0000313|EMBL:ELK10411.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK10411.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 ECO:0000256|PIRNR:PIRNR000929};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000929}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 2 subfamily. {ECO:0000256|ARBA:ARBA00010750,
CC ECO:0000256|PIRNR:PIRNR000929}.
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DR EMBL; KB030754; ELK10411.1; -; Genomic_DNA.
DR RefSeq; XP_006914717.1; XM_006914655.1.
DR RefSeq; XP_006914718.1; XM_006914656.1.
DR AlphaFoldDB; L5KI40; -.
DR STRING; 9402.L5KI40; -.
DR GeneID; 102895931; -.
DR KEGG; pale:102895931; -.
DR CTD; 5777; -.
DR eggNOG; KOG0790; Eukaryota.
DR InParanoid; L5KI40; -.
DR OrthoDB; 2911650at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14606; PTPc-N6; 1.
DR CDD; cd09931; SH2_C-SH2_SHP_like; 1.
DR CDD; cd10340; SH2_N-SH2_SHP_like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
DR PANTHER; PTHR46257; TYROSINE-PROTEIN PHOSPHATASE CORKSCREW; 1.
DR PANTHER; PTHR46257:SF4; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 6; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS50001; SH2; 2.
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|PIRNR:PIRNR000929};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000929};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR000929};
KW Receptor {ECO:0000313|EMBL:ELK10411.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 4..100
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 110..213
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 244..515
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 430..506
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 531..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 453
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-1"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
FT BINDING 500
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
SQ SEQUENCE 595 AA; 67691 MW; B0887A316864FB54 CRC64;
MVRWFHRDLS GLDAETLLKG RGVHGSFLAR PSRKNQGDFS LSVRVGDQVT HIRIQNSGDF
YDLYGGEKFA TLTELVEYYT QQQGVLQDRD GTIIHLKYPL NCSDPTNERW YHGHMSGGQA
ETLLQAKGEP WTFLVRESLS QPGDFVLSVL SDQPKAGPGS PLRVTHIKVM CEGERYTLGG
SETFDSLTDL VEYFKKTGIE EASGAFVYLR QPYYATRVNA ADIENRVLEL NKKQESEDTA
KAGFWEEFES LQKQEVKNLH QRLEGQRPEN KCKNRYKNIL PFDHSRVILQ GRDSNVPGSD
YINANYVTNQ LLGPDENAKT YIASQGCLEA TVNDFWQMTW QENTRVIVMT TREVEKGRNK
CVPYWPEVGT QRVYGPYTVT NCGEYDTAEY KLRTLQVSPL DNGNLVREIW HYQYLSWPDH
GVPSEPGGVL SFLDQINQRQ ESLPHPGPII VHCSAGIGRT GTIIVIDMLM ESISTKGLDC
DIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEVMQSQK GQESEYGNIT
YPPAMKNAHA QASRTSSKHK EDVYENLHSK NKREEKVKKQ RSADKDKSKG SLKRK
//
