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Database: UniProt
Entry: A0A091DL89_FUKDA
LinkDB: A0A091DL89_FUKDA
Original site: A0A091DL89_FUKDA 
ID   A0A091DL89_FUKDA        Unreviewed;       552 AA.
AC   A0A091DL89;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=H920_15154 {ECO:0000313|EMBL:KFO23581.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO23581.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO23581.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO23581.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class 2 subfamily. {ECO:0000256|ARBA:ARBA00010750}.
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DR   EMBL; KN123762; KFO23581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091DL89; -.
DR   STRING; 885580.ENSFDAP00000000436; -.
DR   eggNOG; KOG0790; Eukaryota.
DR   Proteomes; UP000028990; 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; cd14605; PTPc-N11; 1.
DR   CDD; cd09931; SH2_C-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; PTHR46559; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11; 1.
DR   PANTHER; PTHR46559:SF1; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11; 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; 1.
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   Receptor {ECO:0000313|EMBL:KFO23581.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191}.
FT   DOMAIN          1..61
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          71..175
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          206..480
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          395..471
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          507..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        418
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000929-1"
FT   BINDING         384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
FT   BINDING         465
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
SQ   SEQUENCE   552 AA;  63505 MW;  FE1F296A98ED61C1 CRC64;
     MDNFRRNGAV THIKIQNTGD YYDLYGGEKF ATLAELVQYY MEHHGQLKEK NGDVIELKYP
     LNCADPTSER WFHGHLSGKE AEKLLTEKGK HGSFLVRESQ SHPGDFVLSV RTGDDKGESN
     DGKSKVTHVM IRCQELKYDV GGGERFDSLT DLVEHYKKNP MVETLGTVLQ LKQPLNTTRI
     NAAEIESRVR ELSKLAETTD KVKQGFWEEF ETLQQQECKL LYSRKEGQRQ ENKNKNRYKN
     ILPFDHTRVV LHDGDPNEPV SDYINANIIM PEFETKCNNS KPKKSYIATQ GCLQNTVNDF
     WRMVFQENSR VIVMTTKEVE RGKSKCVKYW PDEYALKEYG VMRVRNVKES AAHDYTLREL
     KLSKVGQGNT ERTVWQYHFR TWPDHGVPSD PGGVLDFLEE VHHKQESIMD AGPVVVHCSA
     GIGRTGTFIV IDILIDIIRE KGVDCDIDVP KTIQMVRSQR SGMVQTEAQY RFIYMAVQHY
     IETLQRRIEE EQKSKRKGHE YTNIKYSLAD QASGDQSPLP PCTPTPACAE MREDSARVYE
     NVGLMQQQKS FR
//
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