MTMR1_HUMAN
ID MTMR1_HUMAN Reviewed; 665 AA.
AC Q13613; A0A024RC07; Q9UBX6; Q9UEM0; Q9UQD5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 4.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Myotubularin-related protein 1 {ECO:0000305};
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000269|PubMed:27018598};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000269|PubMed:11733541};
GN Name=MTMR1 {ECO:0000312|HGNC:HGNC:7449};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=9828128; DOI=10.1006/geno.1998.5560;
RA Kioschis P., Wiemann S., Heiss N.S., Francis F., Goetz C., Poustka A.,
RA Taudien S., Platzer M., Wiehe T., Beckmann G., Weber J., Nordsiek G.,
RA Rosenthal A.;
RT "Genomic organization of a 225-kb region in Xq28 containing the gene for X-
RT linked myotubular myopathy (MTM1) and a related gene (MTMR1).";
RL Genomics 54:256-266(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-665.
RC TISSUE=Brain;
RA Kioschis P., Wiemann S., Francis F., Goetz C., Poustka A., Taudien S.,
RA Platzer M., Wiehe T., Beckmann G., Weber J., Nordsiek G., Rosenthal A.;
RT "Ancient genomic duplication within the myotubular myopathy locus (MTM1) in
RT human Xq28.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 114-610.
RX PubMed=9736772; DOI=10.1093/hmg/7.11.1703;
RA Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N.,
RA Mandel J.-L.;
RT "Characterization of the myotubularin dual specificity phosphatase gene
RT family from yeast to human.";
RL Hum. Mol. Genet. 7:1703-1712(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 404-535.
RX PubMed=8640223; DOI=10.1038/ng0696-175;
RA Laporte J., Hu L.-J., Kretz C., Mandel J.-L., Kioschis P., Coy J.,
RA Klauck S.M., Poutska A., Dahl N.;
RT "A gene mutated in X-linked myotubular myopathy defines a new putative
RT tyrosine phosphatase family conserved in yeast.";
RL Nat. Genet. 13:175-182(1996).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11733541; DOI=10.1074/jbc.m111087200;
RA Kim S.A., Taylor G.S., Torgersen K.M., Dixon J.E.;
RT "Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated in
RT myotubular myopathy and type 4B Charcot-Marie-Tooth disease.";
RL J. Biol. Chem. 277:4526-4531(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13] {ECO:0007744|PDB:5C16}
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 95-665 OF MUTANT SER-438 IN
RP COMPLEX WITH PHOSPHATE IONS, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, DOMAIN,
RP MUTAGENESIS OF CYS-438; ASP-443; ARG-444 AND ARG-484, AND ACTIVE SITE.
RX PubMed=27018598; DOI=10.1371/journal.pone.0152611;
RA Bong S.M., Son K.B., Yang S.W., Park J.W., Cho J.W., Kim K.T., Kim H.,
RA Kim S.J., Kim Y.J., Lee B.I.;
RT "Crystal structure of human myotubularin-related protein 1 provides insight
RT into the structural basis of substrate specificity.";
RL PLoS ONE 11:E0152611-E0152611(2016).
CC -!- FUNCTION: Lipid phosphatase that has high specificity for
CC phosphatidylinositol 3-phosphate and has no activity with
CC phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-
CC bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate
CC (PubMed:11733541, PubMed:27018598). Activity with phosphatidylinositol
CC (3,5)-bisphosphate is controversial; it has been shown by
CC PubMed:27018598, while PubMed:11733541 find no activity with this
CC substrate. {ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:27018598}.
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:27018598};
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:11733541, ECO:0000269|PubMed:27018598};
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:0000269|PubMed:11733541};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27018598}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Z2C4};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z2C4}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q9Z2C4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Z2C4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13613-1; Sequence=Displayed;
CC Name=1A;
CC IsoId=Q13613-2; Sequence=VSP_005169, VSP_005170;
CC -!- DOMAIN: The C-terminal region is required for dimerization.
CC {ECO:0000269|PubMed:27018598}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; AF002223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471169; EAW99384.1; -; Genomic_DNA.
DR EMBL; CH471169; EAW99388.1; -; Genomic_DNA.
DR EMBL; AJ224979; CAA12271.1; -; mRNA.
DR EMBL; AF057354; AAD40368.1; -; mRNA.
DR EMBL; U58032; AAC79117.1; -; mRNA.
DR CCDS; CCDS14695.1; -. [Q13613-1]
DR RefSeq; NP_003819.1; NM_003828.3. [Q13613-1]
DR RefSeq; XP_006724918.1; XM_006724855.3. [Q13613-1]
DR PDB; 5C16; X-ray; 2.07 A; A/B/C/D=95-665.
DR PDBsum; 5C16; -.
DR AlphaFoldDB; Q13613; -.
DR SMR; Q13613; -.
DR BioGRID; 114306; 93.
DR IntAct; Q13613; 25.
DR MINT; Q13613; -.
DR STRING; 9606.ENSP00000359417; -.
DR SwissLipids; SLP:000001136; -.
DR DEPOD; MTMR1; -.
DR GlyGen; Q13613; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q13613; -.
DR PhosphoSitePlus; Q13613; -.
DR BioMuta; MTMR1; -.
DR DMDM; 33112667; -.
DR EPD; Q13613; -.
DR jPOST; Q13613; -.
DR MassIVE; Q13613; -.
DR MaxQB; Q13613; -.
DR PaxDb; Q13613; -.
DR PeptideAtlas; Q13613; -.
DR PRIDE; Q13613; -.
DR ProteomicsDB; 59598; -. [Q13613-1]
DR ProteomicsDB; 59599; -. [Q13613-2]
DR Antibodypedia; 442; 102 antibodies from 24 providers.
DR DNASU; 8776; -.
DR Ensembl; ENST00000370390.7; ENSP00000359417.3; ENSG00000063601.17. [Q13613-1]
DR Ensembl; ENST00000485376.5; ENSP00000434105.1; ENSG00000063601.17. [Q13613-2]
DR GeneID; 8776; -.
DR KEGG; hsa:8776; -.
DR UCSC; uc004fei.4; human. [Q13613-1]
DR CTD; 8776; -.
DR DisGeNET; 8776; -.
DR GeneCards; MTMR1; -.
DR HGNC; HGNC:7449; MTMR1.
DR HPA; ENSG00000063601; Low tissue specificity.
DR MIM; 300171; gene.
DR neXtProt; NX_Q13613; -.
DR OpenTargets; ENSG00000063601; -.
DR PharmGKB; PA31252; -.
DR VEuPathDB; HostDB:ENSG00000063601; -.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000153669; -.
DR InParanoid; Q13613; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q13613; -.
DR TreeFam; TF315197; -.
DR BRENDA; 3.1.3.95; 2681.
DR PathwayCommons; Q13613; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q13613; -.
DR BioGRID-ORCS; 8776; 11 hits in 709 CRISPR screens.
DR ChiTaRS; MTMR1; human.
DR GeneWiki; MTMR1; -.
DR GenomeRNAi; 8776; -.
DR Pharos; Q13613; Tbio.
DR PRO; PR:Q13613; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q13613; protein.
DR Bgee; ENSG00000063601; Expressed in secondary oocyte and 211 other tissues.
DR ExpressionAtlas; Q13613; baseline and differential.
DR Genevisible; Q13613; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; ISS: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:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR CDD; cd13358; PH-GRAM_MTMR1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR030587; MTMR1.
DR InterPro; IPR037857; MTMR1_PH-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; PTHR10807; 1.
DR PANTHER; PTHR10807:SF40; PTHR10807:SF40; 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; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Hydrolase; Lipid metabolism; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..665
FT /note="Myotubularin-related protein 1"
FT /id="PRO_0000094932"
FT DOMAIN 90..161
FT /note="GRAM"
FT DOMAIN 226..601
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..665
FT /note="Required for dimerization"
FT /evidence="ECO:0000269|PubMed:27018598"
FT REGION 642..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044,
FT ECO:0000305|PubMed:27018598"
FT BINDING 351..354
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27018598"
FT BINDING 376..377
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27018598"
FT BINDING 438..444
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27018598"
FT BINDING 484
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2C4"
FT VAR_SEQ 553..568
FT /note="DVYTKTISLWSYINSQ -> AWGAGTQRARGSLRSR (in isoform
FT 1A)"
FT /evidence="ECO:0000305"
FT /id="VSP_005169"
FT VAR_SEQ 569..665
FT /note="Missing (in isoform 1A)"
FT /evidence="ECO:0000305"
FT /id="VSP_005170"
FT MUTAGEN 438
FT /note="C->S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:27018598"
FT MUTAGEN 443
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:27018598"
FT MUTAGEN 444
FT /note="R->A: Abolishes enzyme activity with
FT phosphatidylinositol 3-phosphate. Reduces activity with
FT phosphatidylinositol (3,5)-bisphosphate."
FT /evidence="ECO:0000269|PubMed:27018598"
FT MUTAGEN 484
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:27018598"
FT CONFLICT 541
FT /note="F -> L (in Ref. 4; CAA12271)"
FT /evidence="ECO:0000305"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 122..138
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:5C16"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5C16"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:5C16"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 318..329
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:5C16"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 377..391
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 400..407
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 409..428
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 444..456
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 463..473
FT /evidence="ECO:0007829|PDB:5C16"
FT TURN 474..478
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 481..485
FT /evidence="ECO:0007829|PDB:5C16"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 500..514
FT /evidence="ECO:0007829|PDB:5C16"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 523..535
FT /evidence="ECO:0007829|PDB:5C16"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 546..551
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 561..567
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 568..572
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:5C16"
FT HELIX 598..601
FT /evidence="ECO:0007829|PDB:5C16"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:5C16"
SQ SEQUENCE 665 AA; 74678 MW; 12E766859F0DCA75 CRC64;
MDRPAAAAAA GCEGGGGPNP GPAGGRRPPR AAGGATAGSR QPSVETLDSP TGSHVEWCKQ
LIAATISSQI SGSVTSENVS RDYKALRDGN KLAQMEEAPL FPGESIKAIV KDVMYICPFM
GAVSGTLTVT DFKLYFKNVE RDPHFILDVP LGVISRVEKI GAQSHGDNSC GIEIVCKDMR
NLRLAYKQEE QSKLGIFENL NKHAFPLSNG QALFAFSYKE KFPINGWKVY DPVSEYKRQG
LPNESWKISK INSNYEFCDT YPAIIVVPTS VKDDDLSKVA AFRAKGRVPV LSWIHPESQA
TITRCSQPLV GPNDKRCKED EKYLQTIMDA NAQSHKLIIF DARQNSVADT NKTKGGGYES
ESAYPNAELV FLEIHNIHVM RESLRKLKEI VYPSIDEARW LSNVDGTHWL EYIRMLLAGA
VRIADKIESG KTSVVVHCSD GWDRTAQLTS LAMLMLDSYY RTIKGFETLV EKEWISFGHR
FALRVGHGND NHADADRSPI FLQFVDCVWQ MTRQFPSAFE FNELFLITIL DHLYSCLFGT
FLCNCEQQRF KEDVYTKTIS LWSYINSQLD EFSNPFFVNY ENHVLYPVAS LSHLELWVNY
YVRWNPRMRP QMPIHQNLKE LLAVRAELQK RVEGLQREVA TRAVSSSSER GSSPSHSATS
VHTSV
