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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//