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Database: UniProt
Entry: A0A026W202_OOCBI
LinkDB: A0A026W202_OOCBI
Original site: A0A026W202_OOCBI 
ID   A0A026W202_OOCBI        Unreviewed;       448 AA.
AC   A0A026W202;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN {ECO:0000313|EMBL:EZA50068.1};
GN   ORFNames=X777_11733 {ECO:0000313|EMBL:EZA50068.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA50068.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA50068.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
CC   -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC       {ECO:0000256|ARBA:ARBA00007881}.
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DR   EMBL; KK107487; EZA50068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026W202; -.
DR   STRING; 2015173.A0A026W202; -.
DR   EnsemblMetazoa; XM_011347452.3; XP_011345754.1; LOC105284147.
DR   OMA; TXFLDSK; -.
DR   Proteomes; UP000053097; Unassembled WGS sequence.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProt.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14509; PTP_PTEN; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR045101; PTP_PTEN.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR12305; PHOSPHATASE WITH HOMOLOGY TO TENSIN; 1.
DR   PANTHER; PTHR12305:SF81; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE AND DUAL-SPECIFICITY PROTEIN PHOSPHATASE PTEN; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SMART; SM01301; PTPlike_phytase; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT   DOMAIN          23..194
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          111..168
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          199..375
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   REGION          383..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  50610 MW;  7BDB2690F91C7972 CRC64;
     MANTISNMKM TNPIKGLVSK RRKRFTEDGF DLDLTYITDN LIAMGFPAEK LEGVYRNHID
     DVVKLLESKH KDHYKIYNLC SERSYDCKKF KQRVATYAFD DHNPPKLEQI KPFCEDVHSW
     LSQHKDNVAV VHCKAGKGRT GVMVCCYLLH SKQFPTATEA LNYYGTKRTH DRKGVTIPSQ
     RRYVDYYATL VQDGLNYQPV TLILREIQLD PVPIFNGGQG SLHFVISESN KQVFSDVYEV
     RKGTSSISIP LHNVALKGDI RVDFFNRPKM KLKEKMFHFW FNTFFVREKT NSEYDNGELP
     VERSARALSC DGTAMELPMV TSHVKPRTGS LASLGPMPPT LVLRIDKSGL DDAHKDKHHK
     LYSPDFKVSL FMHCMSGSIS PAVPATTNRS GDGVQLGMGG QETPSESSEA DSSECDTTGD
     EDGWESVDLD QRVGRYRLLS DGAMIDLL
//
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