ID A0A1U8L1X8_GOSHI Unreviewed; 846 AA.
AC A0A1U8L1X8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Name=LOC107922039 {ECO:0000313|RefSeq:XP_016707353.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016707353.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016707353.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016707353.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_016707353.1; XM_016851864.1.
DR AlphaFoldDB; A0A1U8L1X8; -.
DR STRING; 3635.A0A1U8L1X8; -.
DR PaxDb; 3635-A0A1U8L1X8; -.
DR GeneID; 107922039; -.
DR KEGG; ghi:107922039; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000189702; Chromosome 25.
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:UP000189702}.
FT DOMAIN 200..644
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT ACT_SITE 440
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 354..355
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 440..446
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 846 AA; 93849 MW; C0115A6D1FFB825F CRC64;
MAASRPSRSV SARDISIGCE RLDGAGSWDT LEWTKIEPVT RSVSHANFEF LLEAERVLDE
GHGVVLVNTD EAGTLFVTNF RLLFLSDGTR NIVPLGTIPL ATIEKFNKMV VKIQSTSRNA
NKSSSRRLLQ IIGKDMRIIV FCFRPRTKQR RAIFDALSRC TKPERIWDLY AFTCGPSKFC
NLSPKVRLLN EYFRLLGKGF HHASMRMIED GSFTMSNDSW RISDINFNYS LCQSYPFALL
VPKSVSDDEI IQASNFRARS RVPAVSWCNP ETGAVLARSS QPLVGIMNTR STADEKLVAA
LCAQLSDEKD SRRKLYIADA RPRKNALANG AMGGGSESSS NYFQSEIVFF GIDNIHAMRE
SFARFRDYLD THGAASSDGM SSFLRHGGWT WGGGNLSSMS ASVSTLGDSG WLIHVQSVLA
GSAWIAARVA LESAAVLVHC SDGWDRTSQL VSLANLMLDP YYRTFTGFQA LVEKDWLAFG
HPFSDRVGMP SISGSSFELS RNASSTGSFS SSPLRQSSGS SQASNSSHAQ NNYSPIFLQW
VDCVSQLLRI YPFAFEFSSN FLVDFLDCVL SCRFGNFLCN SEKERQICGV DESCGCLWAY
LADMRSSEGR SHAHYNLFYD TLKHNGPLLP PAAALAPTLW PQFHLRWACP FESQAGELEA
ECRNMAIKFS ELQKAKEVAE MKAKEYLAAM EILNVDLQNE KQVSSSAINL AKRASKENAA
IQRAVQSLGC RVNFTNSSDS TVDVESSLME TSQRFSLPRR ESEYTMEHND RSDLSVSITV
VADDVVPSSS PLGQVCETLC PLRTQGRGCQ WPDAACAQLG SQFVGLKANF DAFDRLSIYD
RYFKSE
//
