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Database: UniProt
Entry: A0A2Y9LSK1_DELLE
LinkDB: A0A2Y9LSK1_DELLE
Original site: A0A2Y9LSK1_DELLE 
ID   A0A2Y9LSK1_DELLE        Unreviewed;       784 AA.
AC   A0A2Y9LSK1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPN12 {ECO:0000313|RefSeq:XP_022410067.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022410067.1};
RN   [1] {ECO:0000313|RefSeq:XP_022410067.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022410067.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class 4 subfamily. {ECO:0000256|ARBA:ARBA00034734}.
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DR   RefSeq; XP_022410067.1; XM_022554359.1.
DR   AlphaFoldDB; A0A2Y9LSK1; -.
DR   STRING; 9749.A0A2Y9LSK1; -.
DR   KEGG; dle:111164609; -.
DR   InParanoid; A0A2Y9LSK1; -.
DR   OrthoDB; 5489271at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14604; PTPc-N12; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR012266; PTN12.
DR   InterPro; IPR047170; PTN12/18/22.
DR   InterPro; IPR047251; PTN12_cat.
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; PTHR45983; TYROSINE PHOSPHATSE N18, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR45983:SF3; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 12; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000932; Tyr-Ptase_nr12; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT   DOMAIN          28..293
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          207..284
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          323..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..371
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..677
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  88329 MW;  10BDE84D793BECAD CRC64;
     MEQVEILRKF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT ATGEKEENVK
     KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP KAYVATQGPL ANTVIDFWRM
     IWEYNVVIIV MACREFEMGR KKCERYWPLY GEDPITFAPF KISCEAEQAR TDYFIRTLLL
     EFQNESRRLY QFHYVNWPDH DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA
     ICAIDYTWNL LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL
     YEIHGAQKIA DGVNEINTEN MVSSIDPDKQ DSPPPKPPRT RSCLVEGDAK EEILQPPEPH
     PVPPILTPSP PSAFPTVTTV WQDNDRYHPK PVLHVVSSEQ HSTDLNRNYN KSTELTGKNE
     STVEQIDKKL ERNLSFEIKK VPLQEGPKSF EGNTLLNRGH AIKIKSASAS PCTIDKVFKS
     QELNSRDLKI DGISQNSCVD CNATQSNKAP VILPEESQKN SDTPPRPDRL PLDEKGHAPW
     SFHGPENTLP MPDSSEGKSS DTHCQTMKTG SSTPSPTTQL ATHDLTDHHN SSPLFRAPLS
     FTNPLHSDDS DSDERNSDGA VTKNKTSIST ASATVSAAAN TESISTRKVL SMSIARHDIA
     GTIHSGAEKD VDVSEDSPPP LPERTPESFV LASEHNTPVR SEWSELQNQE QCEQRKPEGL
     ITSGSETCDH PARGIHTETC TECPTTFSNK KDQISESPTE ATEIGFGNRC GKPKGPRDPP
     SEWT
//
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