MYTM2_ARATH
ID MYTM2_ARATH Reviewed; 833 AA.
AC F4JWB3; Q0WP53; Q9LZ70;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Phosphatidylinositol-3-phosphatase myotubularin-2;
DE Short=AtMTM2;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000269|PubMed:22324391};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000269|PubMed:22324391};
GN Name=MTM2; OrderedLocusNames=At5g04540; ORFNames=T32M21.150;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
RX PubMed=12068129; DOI=10.1104/pp.004002;
RA Kerk D., Bulgrien J., Smith D.W., Barsam B., Veretnik S., Gribskov M.;
RT "The complement of protein phosphatase catalytic subunits encoded in the
RT genome of Arabidopsis.";
RL Plant Physiol. 129:908-925(2002).
RN [5]
RP GENE FAMILY.
RX PubMed=18201690; DOI=10.1016/j.ydbio.2007.11.031;
RA Jiang S.Y., Ramamoorthy R., Ramachandran S.;
RT "Comparative transcriptional profiling and evolutionary analysis of the
RT GRAM domain family in eukaryotes.";
RL Dev. Biol. 314:418-432(2008).
RN [6]
RP NOMENCLATURE.
RX PubMed=19901554; DOI=10.4161/psb.4.11.10103;
RA Ding Y., Lapko H., Ndamukong I., Xia Y., Al-Abdallat A., Lalithambika S.,
RA Sadder M., Saleh A., Fromm M., Riethoven J.-J., Lu G., Avramova Z.;
RT "The Arabidopsis chromatin modifier ATX1, the myotubularin-like AtMTM and
RT the response to drought.";
RL Plant Signal. Behav. 4:1049-1058(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LEU-250, SUBCELLULAR
RP LOCATION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=22324391; DOI=10.1111/j.1365-313x.2012.04936.x;
RA Ding Y., Ndamukong I., Zhao Y., Xia Y., Riethoven J.-J., Jones D.R.,
RA Divecha N., Avramova Z.;
RT "Divergent functions of the myotubularin (MTM) homologs AtMTM1 and AtMTM2
RT in Arabidopsis thaliana: evolution of the plant MTM family.";
RL Plant J. 70:866-878(2012).
CC -!- FUNCTION: Phosphatase with phosphoinositide 3'-phosphatase activity
CC that can use phosphatidylinositol-3-phosphate (PtdIns3P) and
CC phosphatidylinositol-3,5-diphosphate (PtdIns3,5P(2)) as substrates and
CC produces phosphatidylinositol-5-phosphate (PtdIns5P); participates in
CC pathway(s) that transfer gene regulatory signals to the nucleus.
CC {ECO:0000269|PubMed:22324391}.
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:0000269|PubMed:22324391};
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:0000269|PubMed:22324391};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=216.5 uM for PtdIns3P {ECO:0000269|PubMed:22324391};
CC KM=158.2 uM for PtdIns3,5P(2) {ECO:0000269|PubMed:22324391};
CC Vmax=15.4 pmol/min/mg enzyme with PtdIns3P as substrate
CC {ECO:0000269|PubMed:22324391};
CC Vmax=28.4 pmol/min/mg enzyme with PtdIns3,5P(2) as substrate
CC {ECO:0000269|PubMed:22324391};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22324391}.
CC Note=Highly concentrated at the peripheral lobes of the epidermal
CC cells.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers and roots, and, to a
CC lower extent, in siliques and leaves. {ECO:0000269|PubMed:22324391}.
CC -!- DEVELOPMENTAL STAGE: Expressed in young seedlings, especially at the
CC tip of the growing shoot meristems. Later observed in roots and in
CC aerial parts. Weakly expressed in leaves with local higher levels in
CC the trichomes and in cotyledon veins. Present at low levels in flowers
CC with higher accumulation in cells at organ-stem junctions. Restricted
CC to the developing peduncle. {ECO:0000269|PubMed:22324391}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in both normal and
CC dehydration conditions. {ECO:0000269|PubMed:22324391}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB85561.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162875; CAB85561.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90758.1; -; Genomic_DNA.
DR EMBL; AK229229; BAF01096.1; -; mRNA.
DR PIR; T48451; T48451.
DR RefSeq; NP_196074.2; NM_120536.5.
DR AlphaFoldDB; F4JWB3; -.
DR SMR; F4JWB3; -.
DR STRING; 3702.AT5G04540.1; -.
DR iPTMnet; F4JWB3; -.
DR PaxDb; F4JWB3; -.
DR PRIDE; F4JWB3; -.
DR ProteomicsDB; 248920; -.
DR EnsemblPlants; AT5G04540.1; AT5G04540.1; AT5G04540.
DR GeneID; 830333; -.
DR Gramene; AT5G04540.1; AT5G04540.1; AT5G04540.
DR KEGG; ath:AT5G04540; -.
DR Araport; AT5G04540; -.
DR TAIR; locus:2184402; AT5G04540.
DR eggNOG; KOG4471; Eukaryota.
DR HOGENOM; CLU_017601_0_0_1; -.
DR InParanoid; F4JWB3; -.
DR OMA; DYWRITN; -.
DR OrthoDB; 824298at2759; -.
DR PRO; PR:F4JWB3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JWB3; baseline and differential.
DR Genevisible; F4JWB3; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 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; PTHR10807; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00568; GRAM; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Hydrolase; Lipid metabolism; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..833
FT /note="Phosphatidylinositol-3-phosphatase myotubularin-2"
FT /id="PRO_0000425084"
FT DOMAIN 42..109
FT /note="GRAM"
FT DOMAIN 181..647
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 503..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 660..717
FT /evidence="ECO:0000255"
FT COMPBIAS 755..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 440
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 329..332
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 354..355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 440..446
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 250
FT /note="L->W: Modified subcellular location at granular
FT particles."
FT /evidence="ECO:0000269|PubMed:22324391"
FT CONFLICT 250
FT /note="L -> F (in Ref. 3; BAF01096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 833 AA; 92588 MW; B3046D15022DC7BF CRC64;
MTALRPLSGR SRSLRCSSEK MEGTGSWDVL EWTKLDSASW SGSYSNLDCL LESERIIFEA
CGVILINTDE AGTLLLSNFR ILFLSEGTRK LVPLGTIPFV AIEKFNKLAP KVQSNKYHNN
ENAPTRLLQV TGKDMRIVVY GFRPGTKQRH TVVDTLLRCN KPERVWDLYA FTCGPSQFGN
TNPKERLLNE YFRLLGKSSQ RASMNMIEDG SFTLSNDLWR ITNLNSNYDL CQSYPFALMV
PKSISDEELL QTSTFRARCR LPVISWCHPG SGAVIARSSQ PLVGLMMNMR SNSDEKLVAS
FCTQLAGHKG ARRKLYIVDA RPRKNALANG AKGGGSESSS NYLQSEIVFL GIDNIHAMRE
SFSRLRDYLD MHGTTSSDGT SSFLRHGGWT WGGGNLSSMS ASVSVLGDSG WLSHIQSILA
GVAWIAARVA MESASVLVHC SDGWDRTTQL VSLACLLLDP YYRTFSGFQA LVEKDWLSFG
HPFSDRVGMP NVSESGNFEL PIQSSSARSF PSSPVRQSPG SAAAQSSSSS YGLNNYSPIF
LQWLDCISQL MRMYPSAFEF SPTFLVDFID CLLSCRFGNF LCNSEKERQQ CGISETCGCI
WAYLADLRSS SGTSHVHCNP FYDPSRYDGP LLPPAAALAP TLWPQFHLRW ACPVEPNVTE
TEDQCRAMTV KYSEMKKEKE EAERKVDELS SAMESLNEEL LNERDISRAA RESAKRATKE
RAVISRAVQS LGCKVKFTRN GDCTVEVEDG PQKCSHSIPQ KQSEDNTTDV SESISSVTEQ
NVCEAVCPLR TREGTCRWPD AGCARIGNQF LGLKTNFEAF DNLCVYDSYF TAE
