ID A0A3M0JB89_HIRRU Unreviewed; 1098 AA.
AC A0A3M0JB89;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Myotubularin {ECO:0000256|ARBA:ARBA00016293};
DE EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
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=DUI87_25277 {ECO:0000313|EMBL:RMB98371.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB98371.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMB98371.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMB98371.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMB98371.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78994,
CC ChEBI:CHEBI:84968; Evidence={ECO:0000256|ARBA:ARBA00023672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934;
CC Evidence={ECO:0000256|ARBA:ARBA00023732};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911,
CC ChEBI:CHEBI:85342; Evidence={ECO:0000256|ARBA:ARBA00023712};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell
CC projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Cell
CC projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm,
CC myofibril, sarcomere {ECO:0000256|ARBA:ARBA00004204}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}. Late endosome
CC {ECO:0000256|ARBA:ARBA00004603}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMB98371.1}.
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DR EMBL; QRBI01000153; RMB98371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0JB89; -.
DR STRING; 333673.A0A3M0JB89; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR CDD; cd13355; PH-GRAM_MTM1; 1.
DR CDD; cd13358; PH-GRAM_MTMR1; 1.
DR CDD; cd14591; PTP-MTM1; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR037857; MTMR1_PH-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 InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR10807:SF69; MYOTUBULARIN; 1.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR Pfam; PF02893; GRAM; 2.
DR Pfam; PF06602; Myotub-related; 3.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221}.
FT DOMAIN 163..538
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 344..406
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 690..1034
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 871..933
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 313..314
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 375..381
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1098 AA; 126293 MW; 43B0C3F2FA426652 CRC64;
MASSSTPKYN SNSLENSLSK RTLKDGTNWE QNEEIPRLPG ETRVTDKDVI YMCPFNGPVK
GRVYITNYRL YLRSVENDPV VILNVPLGVI SRIEKMGGAS SRGENSYGLD ITCKDMRNLR
FALKQEGHSR RDIFEVLTKY AFPQSHNLPF FAFVNEEKFP ENGWMVYNPM SEYRRQGLPN
ERWRVTFINE HYGLCDTYPS LLVVPYNATD DDLKKVAAFR SRNRIPVLSW IHPETQAVIM
RCSQPLVGMS GKRNKDDERY LDIIREANGQ ISKLTIYDAR PNVNAVANKA TGGGYEGEDA
YPNAELFFLD IHNIHVMRES LKKLKDIVYP NVEESHWLSS LESTHWLEHI KLVLTGAIQV
ADKVSSGRSS VLVHCSDGWD RTAQLTSLAM LMLDSYYRTV EGFEVLVQKE WISFGHKFAS
RIGHGDKNHA DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE QFLITILDHL YSCRFGTFLY
NSEFLREKEK VTEKTLSLWS LINSEKSKYT NPFYSKELNR ALYPVASMRH LELWVNYYIR
WNPRIRQQAL RDGNKLAQME EAPLFPGESI KVIAKDVMYI CPFMGAVSGT LTVTDFRMFI
KSVERDPPFV VDVPLGVISR VEKIGVQSHG DNSCGIEIVC KDMRNLRLAY KQEEQNRLEI
FENLVTRAFP VSNGLPLFAF SYKEKFAVNG WKVYDPMAEY KRQGLPNESW KISKINSTYE
LCDTYPAVLV VPTSVKDDDL SKVAAFRAKG RVPVLSWIHP ESQATITRCS QPSVGPNDKR
CKEDEKYLQT IMDANAQSHK LIIFDARQNS VADTNKAKGG GYESESAYPN AELVFLEIHN
IHVMRESLRK LKEIVYPTID ETRWLSNVDS THWLEYIRML LAGAVRIADK IESGKTSVVV
HCSDGWDRTA QLTALAMLML DSYYRTIKGF EVLVEKEWIS FGHRFAMFPA AFEFNELFLI
TILDHLYSCL FGTFLCNCEK ERLKEEVSTK TVSLWSYINS QLEEFTNPFY VNYENHVLYP
VASLNHLELW VNYYIRWNPR MRPQVPIHQN LKELLAIRTE LQKKVEDLQR EAATRSISSS
SDRGSSPSHS ATPVHTSV
//
