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Database: UniProt
Entry: A0A5J5BS59_9ASTE
LinkDB: A0A5J5BS59_9ASTE
Original site: A0A5J5BS59_9ASTE 
ID   A0A5J5BS59_9ASTE        Unreviewed;      1281 AA.
AC   A0A5J5BS59;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=F0562_020714 {ECO:0000313|EMBL:KAA8545835.1};
OS   Nyssa sinensis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Cornales; Nyssaceae; Nyssa.
OX   NCBI_TaxID=561372 {ECO:0000313|EMBL:KAA8545835.1, ECO:0000313|Proteomes:UP000325577};
RN   [1] {ECO:0000313|EMBL:KAA8545835.1, ECO:0000313|Proteomes:UP000325577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J267 {ECO:0000313|EMBL:KAA8545835.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAA8545835.1};
RA   Yang X., Kang M., Yang Y., Xiong H., Wang M., Zhang Z., Wang Z., Wu H.,
RA   Ma T., Liu J., Xi Z.;
RT   "A chromosome-level genome assembly of the Chinese tupelo Nyssa sinensis.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CM018033; KAA8545835.1; -; Genomic_DNA.
DR   Proteomes; UP000325577; Miscellaneous, Linkage group lg10.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0052866; F:phosphatidylinositol phosphate phosphatase activity; IEA:UniProt.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   CDD; cd14509; PTP_PTEN; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 2.10.25.160; Granulin; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR000118; Granulin.
DR   InterPro; IPR037277; Granulin_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   InterPro; IPR045101; PTP_PTEN.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR12305; PHOSPHATASE WITH HOMOLOGY TO TENSIN; 1.
DR   PANTHER; PTHR12305:SF96; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE AND PROTEIN-TYROSINE-PHOSPHATASE PTEN2A; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00396; Granulin; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00277; GRAN; 1.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57277; Granulin repeat; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325577};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   DOMAIN          608..787
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          701..761
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          794..921
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   DOMAIN          1017..1141
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          324..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          927..1052
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..343
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..984
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        985..1034
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1281 AA;  140755 MW;  A77D595028A38A6E CRC64;
     MSIISYDQKH GQAIPSRTEK EVKAIYESWL VRHGKAYNAI GEKEKRFEIF KDNLKFVDEH
     NAVNRTYKVG LNRFADLTNE EYRSMFLGGR MERKRRLGTR NDRYKFQARE KLPVAADWRE
     KGAVVPVKNQ GQCGSCWAFS TVAAVEAINK IVTGDLISLS EQELVDCDRS YNQGCNGGLM
     DYAFEFIINN GGIDSEEDYP YRGVDGMCDQ YRKNARVVTI DGYEDVPAND ENSLKKAVAN
     QPVSVAIEAG GRPFQLYQSG VFTGSCGTAL DHGVLAAGYG TENGVDYWIV RNSWGPEWGE
     NGYIRMQRNV DSTTGKCGIA IEPSYPIKTG PNPPKPSPSP PSPVKPPTVC DDYYSCPEGS
     TCCCVYEYGN FCFGWGCCPL ESATCCDDHY SCCPHEYPVC DLDQGACRMS KSNPLGVKAL
     KRGPAEPNWT HQHAGRKVGS TERKRTKKTT TTVPTDDVLA AAPPDRRCTH QLLLQAIATS
     YILAQDVQVS SVTDVGQDKS AHDSPSKLSA SGISSWAKSL KLPQSISGTQ DESPSGNAGK
     SSFSRFTSGI GLRLSPKSPQ SDDNSDGAST TAQSGFIGTL TKGLVDSSKS AVKAVQVKAR
     HVVSQNKRRY QEGGFDLDMT YITENIIAMG FPAGDMSSGF FGYVEGFYRN HMEEVIKFFE
     THHRGKYKVY NLCSERLYDA SLFEGKLASF PFDDHNCPPI QLIISFCQSA YSWLKEDIEN
     VVVVHCKAGM ARTGLMISSL LLYLKFFPTA EESIDYYNQK RCFDGKGLVL PSQIRYVKYF
     ERILTYFNGE NPPGRRCMLR GFRLHRCPYW IRPSITVSDH NGVCFSTKKH PRTKDLSTED
     FWFSAPKKGI MVFALPGEPG LTELVGDFKI HFHDRQGDFY CWLNTTMIEN RKILTTNDLD
     GFDKRKLPSP GFQVEVVLVD YEASVPTRPK TETPTNRSVE SSAASPASVD GGAVAANPTR
     ESGSDEKDDV FSDSEAEESG SSKSRQAKEA SGPGGTVSKT VTSAESSTNS EQIASLTRET
     EKVTLGSTGN TQIHSTSEKK KDVTGDAVSG LGVPKPVEEV SAFKAMAADA SVFTFGDDED
     YENGGTNPEF LEKMEFTLIE GLRELNVEVW NSNTFRKDDF IGSGKLQLQK VLSQGYDDTA
     CRLQTKSNRC AGEVKLILHY ANANNAANSS AWSAPPYVAV APPVPSAPPY VAVAPPVPPV
     SMYSAPPPPA YPASSPSPSY PPYSATYPPP APYPTPQAVY LLVQPNPPPS AFPLLTYQPP
     PQAWPHYAPG PYPPIYPPPP Y
//
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