ID A7RVM7_NEMVE Unreviewed; 610 AA.
AC A7RVM7;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase {ECO:0000256|ARBA:ARBA00032571};
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-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
GN ORFNames=NEMVEDRAFT_v1g241000 {ECO:0000313|EMBL:EDO44480.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO44480.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO44480.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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=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; DS469544; EDO44480.1; -; Genomic_DNA.
DR RefSeq; XP_001636543.1; XM_001636493.1.
DR AlphaFoldDB; A7RVM7; -.
DR STRING; 45351.A7RVM7; -.
DR EnsemblMetazoa; EDO44480; EDO44480; NEMVEDRAFT_v1g241000.
DR KEGG; nve:5516409; -.
DR eggNOG; KOG4471; Eukaryota.
DR HOGENOM; CLU_001839_4_1_1; -.
DR InParanoid; A7RVM7; -.
DR OMA; WRATKIN; -.
DR OrthoDB; 5474662at2759; -.
DR PhylomeDB; A7RVM7; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR CDD; cd13357; PH-GRAM_MTMR2_insect-like; 1.
DR CDD; cd14535; PTP-MTM1-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 InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF130; PHOSPHATIDYLINOSITOL-3,5-BISPHOSPHATE 3-PHOSPHATASE; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00404; PTPc_motif; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT DOMAIN 166..541
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 591..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 558..585
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 377
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 290..293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 315..316
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 377..383
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 610 AA; 70923 MW; 4CD665D41D0EA29B CRC64;
MDGPKRQHSH NSKAEGGLGT VIEDGNVKAE LSANQGELAL CKGEKPQATA KDVTYLCPFT
GPVRGFLYIT NYKLFFKADD DIPFTVEVPL GTIYRVEKIG GTTSRGENAY GLEIYCKDFR
NLRFAHKQEN HSRRLIYERI MHYAFPASNG KPYFAYSFKD EFEYNGWDVY DAEKEFERLG
LPTDCWYVTR INEKYELSDT YPAVVGVPSS VSDEDIKKVA VFRSRNRLPV LCWLHPTNNA
SITRASQPNR GLLARNKDDE KYFQAILEAN PQCHKLLIFD ARPRINAVAN QAKGGGYETE
ENYQNTEVIF LDIANIHVMR ESLRKLKDIC FPNIDDTHWL TNLENTKWLD HIKMIMAGAV
RIADAVDRCR TSVVVHCSDG WDRTPQLTAL AMLLMDPYYR TIIGFEVLIE KEWLSFGHKF
NQRYGHGDKN HADDQRSPVF LQFIDCVWQV TRQFPCAFEF NETFLITILD HLYSCMFGTF
LYNSESQREK EDVKTRTTSL WSYINTSMME FKNPLYAPYL HQHVLFPVPS LRRLELWTRY
YIRWNPRMQA QESEEQRNRD LFFLCEQLRQ KCEELQQEID QRMTVEVPST PDAVSLHSTN
SNSQWATAQL
//
