ID MTMR2_DANRE Reviewed; 620 AA.
AC A0JMK5; B0R0X3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Myotubularin-related protein 2;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000250|UniProtKB:Q13614};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:Q13614};
GN Name=mtmr2; ORFNames=si:dkey-110k5.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC headgroup. Has phosphatase activity towards phosphatidylinositol 3-
CC phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity).
CC {ECO:0000250|UniProtKB:Q13614}.
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:0000250|UniProtKB:Q13614};
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:0000250|UniProtKB:Q13614};
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:0000250|UniProtKB:Q13614};
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:0000250|UniProtKB:Q13614};
CC -!- SUBUNIT: Homooligomer and heterooligomer.
CC {ECO:0000250|UniProtKB:Q13614}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13614}. Early
CC endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q13614}. Note=Partly associated with
CC membranes. {ECO:0000250|UniProtKB:Q13614}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; AL929305; CAQ13290.1; -; Genomic_DNA.
DR EMBL; BC125912; AAI25913.1; -; mRNA.
DR RefSeq; NP_571446.1; NM_131371.1.
DR AlphaFoldDB; A0JMK5; -.
DR SMR; A0JMK5; -.
DR STRING; 7955.ENSDARP00000007407; -.
DR PaxDb; 7955-ENSDARP00000007407; -.
DR PeptideAtlas; A0JMK5; -.
DR GeneID; 30644; -.
DR KEGG; dre:30644; -.
DR AGR; ZFIN:ZDB-GENE-990715-14; -.
DR CTD; 8898; -.
DR ZFIN; ZDB-GENE-990715-14; mtmr2.
DR eggNOG; KOG4471; Eukaryota.
DR HOGENOM; CLU_001839_4_1_1; -.
DR InParanoid; A0JMK5; -.
DR OMA; WRATKIN; -.
DR OrthoDB; 5474662at2759; -.
DR PhylomeDB; A0JMK5; -.
DR TreeFam; TF315197; -.
DR Reactome; R-DRE-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-DRE-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-DRE-1660517; Synthesis of PIPs at the late endosome membrane.
DR PRO; PR:A0JMK5; -.
DR Proteomes; UP000000437; Chromosome 5.
DR Bgee; ENSDARG00000004616; Expressed in pharyngeal gill and 26 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:ZFIN.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
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 InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF42; MYOTUBULARIN-RELATED PROTEIN 2; 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.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Endosome; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome.
FT CHAIN 1..620
FT /note="Myotubularin-related protein 2"
FT /id="PRO_0000356230"
FT DOMAIN 39..116
FT /note="GRAM"
FT DOMAIN 181..556
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 569..601
FT /evidence="ECO:0000255"
FT COMPBIAS 7..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 306..309
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 331..332
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 393..399
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 29
FT /note="V -> L (in Ref. 2; AAI25913)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 620 AA; 71109 MW; A67ADEE5D7B27C1F CRC64;
MEESASVDSV ESLCSSTTTR SDRSSGPKVS DTELRSKGRP IEKMYKDPSK GELPLLPVEL
VQESAKDVTY ICPFIGPIRG SLTVTNYRLF FRCTDREPVF GLDLPLGVLS RVEKIGAATG
RGDVSYGLAC KDMRNLRFVH KEPDDSLKKS VFEVLMKFAF PVSNNMSLFA FEYKQVFPEN
GWKVYDPLAE CKRQGLPNES WRISKLNDHY ELCDSYPATL VVPVTITDDE LRRVSSFRAK
GRIPVLSWIH PESQAAVVRS SQPMVGQNGR RCKEDEKLLQ AIMDANAQSH KLFIFDARPS
VNAAANKMKG GGFESEDAYQ NAELVFLDIH NIHVMRESLR KLKEVVYPNI EESHWLSNLE
STHWLEHIKL ILAGALRIAD KVESGKTSVV VHCSDGWDRT AQLTSLALIM LDSHYRTIRG
FQILVEKEWL SFGHRFQQRV GHGDKNHTDV DRSPIFLQFI DCVWQMTRQF PAAFEFNEYF
LITILDHLYS CLFGTFLCNS EQQRLKEEIP KRTVSLWSFV NSQLEEFVNP LYVHYSSHVL
FPTVGIRHLQ LWVSYYIRWN PRMRPQEPVH QRYKELLAKR AELQKRVEEL QREVSSRTAS
SSSERAGSPT RSITPVQTFV
//
