ID A0A182N156_9DIPT Unreviewed; 1074 AA.
AC A0A182N156;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR001364-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR001364-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR001364-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000256|ARBA:ARBA00007315}.
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DR AlphaFoldDB; A0A182N156; -.
DR STRING; 7168.A0A182N156; -.
DR EnsemblMetazoa; ADIR001364-RA; ADIR001364-PA; ADIR001364.
DR VEuPathDB; VectorBase:ADIR001364; -.
DR OrthoDB; 9871at2759; -.
DR Proteomes; UP000075884; Unassembled WGS sequence.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF27; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 229..387
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 311..373
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..45
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 116480 MW; 546E780AD5DEFBAB CRC64;
MSLPSRPDAY ATSQEEEEEE ELEEVDEEDE EEEERELEQD LEEDGPKCDF DPGLRRGTMM
GMVSVVQDRL YLAVIRTLNP PSSTDRVYYF NVDEELTYES FYHDHGPLNL AKVARYCKRV
NELLRKQERP IIHYTSPNPK SILNAAFLMG CYAIIYQGHT GSSVMRVMSA VLRHTRGLKY
CDASQIELRY LSLRDCLNGV MKAHRHNLFN LADFDNVEYE YYERVENGDM NWIVPGKLLA
FCGPQRETRY SRGVIANGPD VYFDYFQRHN VTTIVRLNLK VYDARSFTDE GFVHYDLYFP
DGSSPNDAVL QQFLDICEQS AGAVAVHCKA GLGRTGTLIA AYLVKHYGMT AQEAIGWLRV
CRPGSVIGQQ QTWLRQKQAA LQQDGVNYRR SGRPAVPTRH PYGIYSREEA ARLLTMQQQE
HRADRDDADH GDGASVVVVA PADAGGAPPP VEDDGHGAAA TLQGISQQVD TMRLSDDEDG
HARIATANQY NNNTLHFKTT RYGRNSAYVR THRSSSSAAA ARRSGSVGDD GGSSGGCAAT
SAGSRIPPYQ AGRTSALCPA AHGAAAGSPA APAYRRRLSS GIMPTLSTQG DQLNLIKATR
RRRNTIVATE RFRTYQTAPR KTIHPRVLLE ESSDLFPLGL DEPDNDLDTS SGYMTDGLNP
SNLSLQTDEE METRPAPETT PTPEAMERKD YPGDEVLTMT PPAAPLSPRS LRTTPTAEAA
VGNGIEEREY RHHLQQEYSI LEGDAATDEP NFAPPGLHRT DTATPDDSEF PADGVFHESD
PFPEPDFSTA SKVSDSSSED LRGSPPTIAR SDPEDGATNP TEPLIETKVV PDLSSKDLRG
SPPTNVRNPK PRRSAPDANT GGSTESKIPI YTSSVAAAAN SPFTVRGTSA TPLPPSTPAA
PTPLPQVLVC DVNGNNRPPA AAATVPVPRV VTRQMLRKQL LPDATRKRGE NSENRAKRGD
INSNVIEHAD ETKRYKRTRS GNIHDCPKSK EKVRKLGLSG LAKGAAASRA AAAAAAAAAA
AAAATTMPKA KVVGEARAKQ RAADGGGGGV GVGGGVGGVG IATKTKGTAS RGKR
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