ID   MTMR_DICDI              Reviewed;        1324 AA.
AC   Q54GQ1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Myotubularin-related protein DDB_G0290005;
DE            EC=3.1.3.-;
GN   ORFNames=DDB_G0290005;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC       headgroup. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000150; EAL62448.2; -; Genomic_DNA.
DR   RefSeq; XP_635951.2; XM_630859.2.
DR   AlphaFoldDB; Q54GQ1; -.
DR   SMR; Q54GQ1; -.
DR   STRING; 44689.DDB0266510; -.
DR   PaxDb; Q54GQ1; -.
DR   EnsemblProtists; EAL62448; EAL62448; DDB_G0290005.
DR   GeneID; 8627433; -.
DR   KEGG; ddi:DDB_G0290005; -.
DR   dictyBase; DDB_G0290005; mtm4.
DR   eggNOG; KOG4471; Eukaryota.
DR   HOGENOM; CLU_259628_0_0_1; -.
DR   InParanoid; Q54GQ1; -.
DR   OMA; KFMTRNG; -.
DR   Reactome; R-DDI-1483248; Synthesis of PIPs at the ER membrane.
DR   Reactome; R-DDI-1632852; Macroautophagy.
DR   Reactome; R-DDI-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-DDI-1660516; Synthesis of PIPs at the early endosome membrane.
DR   Reactome; R-DDI-1660517; Synthesis of PIPs at the late endosome membrane.
DR   Reactome; R-DDI-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:Q54GQ1; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   PANTHER; PTHR10807; PTHR10807; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..1324
FT                   /note="Myotubularin-related protein DDB_G0290005"
FT                   /id="PRO_0000346929"
FT   DOMAIN          349..807
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT   REGION          140..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..1043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1066..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1232..1296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1020..1195
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        141..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..883
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..991
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1043
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        575
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         514..515
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         575..581
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         621
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1324 AA;  149677 MW;  EF1703F7C309F8D1 CRC64;
     MFSNKNTDNV ENDNNNALGS VIARINSQNI ITKNKAPVIS EDFETQDFDY PSFDDETPNY
     DRPQPTMVEN FTLLPGEFVL MITKNVVNLS LTTTTHRIGT LYQTNYQMFF IDDSTRQLVS
     TIANGQLLQI KKLKGHVTVK YHDNTTPNNN NNNNNNNNNN NNNTNNNNNN NINKSNNSST
     DQLNSFSLEK QPSQNENLNN NNNNNNNNNN GNNNINNNNL MNSLTQPSTS SRSRLLKSNS
     TPINLNESST STNSPTLSST TTTTTTTSST NGNCSTNTWY SNGVSEKALI LEIRCKDFMI
     TRYCLPFNEK GNEAFELMNK LICNNYQDSN QLFSMSYSPF KGVISPIDGW LFYDPIEEYT
     RQGLIGNSNG SDEWRLTKMN SKYELCSTYP QHFIIPFSIS DYLLNKSSSH RNKNRFPVVT
     WRHKQTHATL SRSSQQTGKS RCEEDELLIQ AIRKSKTILP NNNNQQQQPQ QQQQTLYIID
     IKSTSSSPTS SSSSHCEDIS HYSQCQIESE CLSNIHELRE SQLKLFKVIR NWNEKKGWSE
     IQSTGWLDQL SKLLMVTKKI LTHLHLEGFS CLIHCIDGWD RTCQLSSLVQ LCADPYYRTI
     KGFIVLISKE WLSFGHKFMT RNGQSISSTS TTTTNSSSNG QLTSSSSNTS ISSNATTTTT
     TTTSSKQTSP VFLQFIDVVW QLTKQFPTSF EFSDSFLSVI LHHLNSNLFG TFLYDSEKER
     QQNNLPTETQ SLWTLLLSAQ KNSSLLNPLF NQQLSNETSS TTNLTATTSI PLTNSTTLDQ
     QLQFKNNNDD GVLFPNPKGV QLWSDYFLKW RNPPKASRKS NTLIAHSLGV SYVNGDLIAF
     QKKKRSRRSK DGASGSSSGS SGSSSKHHHH HHHHHHHHHH RKSTDEKDSK EKSSKSSRSR
     TSSSSKRKSL STSSNSITQP DIKINETITT TTTTPTNTTT LTNTSTTPRN TTTLTNASTT
     PTTTTTTTTT TTPTKDETIN ESVQVNNDKL KSPSGDDIKQ EQDEMNQFTS QHPNNQMESS
     SEINQQNEQS QLEQQQEQQQ QQEQQLQHEQ QQIEQQQLQK QQQQQEQQEQ QELEQQEQPN
     ETITYSMESD SQSSISQNQN QLQQQQQQQT LLDPIDESSL LATTTTTTSS TAITSASKLE
     KELRKQEKEK RKLEKEKKQK ERAERKLEKE KKRDQKEREQ KEKELLEQQK PKADITVVLQ
     SPSKKKAMSL TMPVRGTKSR ISIFSSPLVP TLHPNLSDQN SQTNSSGDNS GNVNNSPNLT
     STPISNLSNN NNNNNNSNEN SNNNNNNNNN NNDNTSFSKR IFKTLRGTKT FNREPTPTVG
     TALN