MTMR8_DANRE
ID MTMR8_DANRE Reviewed; 632 AA.
AC Q6TEL0; Q7SZD1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Myotubularin-related protein 8;
DE AltName: Full=Myotubularin-related protein 6;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase {ECO:0000305};
DE EC=3.1.3.95 {ECO:0000250|UniProtKB:Q96EF0};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000305};
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:Q96EF0};
GN Name=mtmr8; Synonyms=mtmr6; ORFNames=si:dkey-286f3.1, zgc:56405;
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 MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC headgroup (By similarity). Has phosphatase activity towards
CC phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-
CC bisphosphate (By similarity). {ECO:0000250|UniProtKB:Q96EF0}.
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:Q96EF0};
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:Q96EF0};
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:Q96EF0}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; AY423041; AAQ98017.1; -; mRNA.
DR EMBL; CR812469; CAM15913.1; -; Genomic_DNA.
DR EMBL; BC053411; AAH53411.1; -; mRNA.
DR RefSeq; NP_956688.1; NM_200394.1.
DR AlphaFoldDB; Q6TEL0; -.
DR SMR; Q6TEL0; -.
DR STRING; 7955.ENSDARP00000007263; -.
DR PaxDb; Q6TEL0; -.
DR Ensembl; ENSDART00000002938; ENSDARP00000007263; ENSDARG00000008592.
DR Ensembl; ENSDART00000189357; ENSDARP00000146513; ENSDARG00000113186.
DR GeneID; 393365; -.
DR KEGG; dre:393365; -.
DR CTD; 55613; -.
DR ZFIN; ZDB-GENE-040426-1016; mtmr8.
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000162717; -.
DR HOGENOM; CLU_001839_3_2_1; -.
DR InParanoid; Q6TEL0; -.
DR OMA; CHKERED; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q6TEL0; -.
DR TreeFam; TF315197; -.
DR Reactome; R-DRE-1660499; Synthesis of PIPs at the plasma membrane.
DR PRO; PR:Q6TEL0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000008592; Expressed in mature ovarian follicle and 27 other tissues.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0004708; F:MAP kinase kinase activity; IMP:ZFIN.
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-phosphatase activity; IBA:GO_Central.
DR GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
DR GO; GO:0010507; P:negative regulation of autophagy; IBA:GO_Central.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:ZFIN.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030591; MTMR8.
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; PTHR10807; 1.
DR PANTHER; PTHR10807:SF36; PTHR10807:SF36; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lipid metabolism; Nucleus; Reference proteome.
FT CHAIN 1..632
FT /note="Myotubularin-related protein 8"
FT /id="PRO_0000330036"
FT DOMAIN 126..500
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 545..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 250..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 275..276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 338..344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT CONFLICT 48
FT /note="T -> A (in Ref. 3; AAH53411)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="F -> S (in Ref. 3; AAH53411)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="S -> A (in Ref. 3; AAH53411)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="A -> G (in Ref. 3; AAH53411)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="F -> S (in Ref. 3; AAH53411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 72503 MW; 523B584C69C45FE1 CRC64;
MEHIITPKVE NVKLLNRYTE KKSALGTLYL TATHLIYVEQ TSNTRKETWV LHHHILSVEK
LLLTASGCPL LIRCKTFQHL HLLFQKERDC QDVYQSLLRL FQPVKEEELY AFLYNPHQNE
EERRRGWELI SVVNDFNRMG LSNDYWEISH INKNFEMCST YPSILGLPKS ASVATVTGSA
KFRSRGRLPV LSYYHKDTKA AICRCSQPLS GLNSRCVEDE QMLQAISQAN PNSPFIYVVD
TRPKLNAMAN RAAGKGYENE DNYSNIRFQF QGIENIHVMR SSLQKLLEVC SMKSPSMSDY
LTGLENSGWL RHIKSVMDAG VFLAKAVCEE RASVLVHCSD GWDRTAQVCS LACLLLDPYY
RTIKGLMVLI EKEWISFGHK FSHRCGHLDS DPKEASPVFT QFLECVWQLS QQFPCVFEFN
EHYLIEIHDQ VYACQYGNFI GNCQKERLDM RLHEKTFSLW PHLLENQHQY RNPLYRRSLE
STVLRPSTLP LHFKFWCGMY NHYDRGMHPK QSVLDTLLTL TQRQVEGERT MTELQRQLAV
ADGVLPDPAG PINTHADQNN QSEKMPAPPV VQSNGSCAPL INGNVKEVGP GAENSNQEDR
EEPAANEHDL SSKDKPVFVE TEHSKEEVQE SS
