ID W5MTY9_LEPOC Unreviewed; 1136 AA.
AC W5MTY9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Dual specificity phosphatase 27, atypical {ECO:0000313|Ensembl:ENSLOCP00000011848.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011848.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011848.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01003522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MTY9; -.
DR Ensembl; ENSLOCT00000011869.1; ENSLOCP00000011848.1; ENSLOCG00000009695.1.
DR GeneTree; ENSGT00940000159723; -.
DR HOGENOM; CLU_009343_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG17.
DR Bgee; ENSLOCG00000009695; Expressed in muscle tissue and 5 other cell types or tissues.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14576; DSP_iDUSP27; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45682; AGAP008228-PA; 1.
DR PANTHER; PTHR45682:SF4; SERINE_THREONINE_TYROSINE-INTERACTING-LIKE PROTEIN 2; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01908; ADSPHPHTASE.
DR PRINTS; PR01909; ADSPHPHTASEA.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 136..284
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 205..264
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 128191 MW; 214BF5E38CCE0E10 CRC64;
AVAMASRGDP AGEQVVPEEE DAVSVRSVQA RYLRSPSPSR FSIMSDADTE SIFMEPIHLS
PAVAAKQIIN EELKPKELKV EPGVPETMME SAEQLLVEDL YNRVKDMMDD SSPFDTPCVL
DIQRALTQDR LEAPTNPVDE VWPNIFIAEK AVAVNKSRLK RLGITHILNT AHGTGVYTGP
DFYTGMNIQY MGIEVDDFPE MDISQHFRPA AEFLDEALLT HRGKVLVDSM MGVSRSAVLV
AAYMMIFHHM TIMEALMTLR KKRPIYPNES FLRQLRELNE TLLEERGGVI QAKTHSVMAE
EEESGSVMGA KAHSIFVEEE DKMSTMSSVL TAAAKSSVVS KRPTLIDEDE EDRLYEEWRK
KQGLPPSEKP NPKEVKIPRL PEEKEDEDVD GMIREWQRRN EQYQSEDWWR AQLMSEDEQS
LLGGSSFSAN GCDDLESVNS VDIRALKERL AASGAGRFRS DSVSTEDSAA DIWTKRLREI
EEEAAARYGD KGRGATENGT GEKEIDEESL FSETSSLYNF CKKNKEKLTP LERWRIKRIQ
FGWNKKDAEA EKAEGGSVQG EEEETKVASG EVNLTAYQNW KLKHQKKLGT ENKDEIVELS
KGEDTASIKK KQRRAEILER SRQTLEESQS MCGWDTESSM SGSIPLSAIW PTMSARSISD
DTTSMLSMQS NRSSFSQSRN LQGLPPAPIT PLPNIQVGND DAISLASIQN WIANVVTETI
IQKQNELLMQ GGLPPSRSPS VMSSGARPGA VGKYMDDDKV SLLSMQSGVS YASSSSRQRE
LPSTDSHSVL SCSSLSNIKP EGHSSKDKIT RTSKPLYSLF ADDVDLKKLD TKDKEMKSEM
RGKMSAYEKE KIAADNKRST LFRRKKAKDD KEDEDDTMRA SGNYSYTKFD RSDRSDTVPN
ITGQLSRSVT ESADKTSSID KWLNDIKTPS RYQQKSYGGE SSEAKFPRSS YTKEDNIETS
YSKSSRGWKE FSDRSLSSLD EVYKSSSRFS SKEPSTASDL HSSDRFGVHS YDDHRRNSTE
LYDFRRSATT EEATSNIATQ KHRSQVTYSS EDDDSEDNHG LEYGAKRRFT QSFSKSEENN
RETKRSDSDD EEAPLNTWYR IKSKPKEDEE LDDDEVITAW RRQQESKSRT QRRREI
//
