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Database: UniProt
Entry: A0A2K1ZAN2_POPTR
LinkDB: A0A2K1ZAN2_POPTR
Original site: A0A2K1ZAN2_POPTR 
ID   A0A2K1ZAN2_POPTR        Unreviewed;       859 AA.
AC   A0A2K1ZAN2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=phosphatidylinositol-3,5-bisphosphate 3-phosphatase {ECO:0000256|ARBA:ARBA00012903};
DE            EC=3.1.3.95 {ECO:0000256|ARBA:ARBA00012903};
DE   AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase {ECO:0000256|ARBA:ARBA00032571};
DE   AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
GN   ORFNames=POPTR_008G026900 {ECO:0000313|EMBL:PNT22334.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT22334.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT22334.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC         bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC         ChEBI:CHEBI:57923; EC=3.1.3.95;
CC         Evidence={ECO:0000256|ARBA:ARBA00001669};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC         phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC         Evidence={ECO:0000256|ARBA:ARBA00001291};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR   EMBL; CM009297; PNT22334.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K1ZAN2; -.
DR   STRING; 3694.A0A2K1ZAN2; -.
DR   InParanoid; A0A2K1ZAN2; -.
DR   OMA; DYWRITN; -.
DR   OrthoDB; 5474662at2759; -.
DR   Proteomes; UP000006729; Chromosome 8.
DR   ExpressionAtlas; A0A2K1ZAN2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106018; F:phosphatidylinositol-3,5-bisphosphate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14507; PTP-MTM-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00568; GRAM; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006729}.
FT   DOMAIN          200..652
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        444
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         358..359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         444..450
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   859 AA;  94609 MW;  89055E0B172974A3 CRC64;
     MSAPRRSTSL RDSSSDSERM EGTGSWDDAL DWFKLEVQHP ASRSVSHHAN YKCLLEAERV
     LVEGRGVVLI NTDEAGTLIV TNFRLIFLSE GTENIIALGT IPLATIEKFS KMVVKNQSAP
     RHSEKTPSQR FLQVIGKDMR IVVFGFRSKT KQRRAIYDGL LRCTKPSRLW DLYAFSCGPF
     KFTNANPKVR LLNEYFRLLG KGLCRASMDM IDNGSYTMSN ELWRICNVNS NYIMCPSYPF
     ALIVPKSISD EEVIQASNFR SKGRLPVVSW CHPETGAVLA RSSQPLVGLM MNMRSNTDEK
     LVAELCSQLG DEKKRRRKLY IADARPRKNA LANVAMGGGS ESSSNYFQSE VVFFGIDNIH
     SMRESLSRLR DYLDAHGTTS SDGTLSLLRH GGWTWGGGNL SNMSASVSTL GDSGWLIHVQ
     SVLAGSAWIA ARVALESASV LVHCSDGWDR TSQLVALANL LLDPYYRTFT GFQALIEKDW
     LAFGHPFAER GGMPTVSGSS ERPPDLCRQS SVGSFPLPPM CQSSGSFAPP TPSSSHAQNQ
     QSPIFLQWID CVSQLLRMYP FAFEFSSAFL VDLLDCVLSC RFGNFFCNSE KERQQVGISE
     ACGCLWAYLA DLRSSEGRSH VHCNPFYSPL KHNGPLLPPA AALAPTLWPQ FHLRWACPSE
     AQAGELEAQC RIMSIKFSKL QKAKEGAEKK AKETAIVVES LSAELRNEKQ LSSSAMALAK
     RASKETAAIK RAIQSLGCKV HYASGGDTTV DIETSPVKNS QKSVFSPSTR ESVGIVQHED
     KSDLSVSISV AADDVVSNNP FGRVCDTLCP LRTRDGGCRW PDAGCAQLAS QFIGVKADYE
     ALDSLSIYEG YFKTMEGGK
//
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