MTMR9_CAEEL
ID MTMR9_CAEEL Reviewed; 569 AA.
AC Q965W9; Q6F3C7;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Myotubularin-related protein 9 {ECO:0000250|UniProtKB:Q96QG7};
DE AltName: Full=Inactive phosphatidylinositol 3-phosphatase 9 {ECO:0000305};
GN Name=mtm-9 {ECO:0000312|WormBase:Y39H10A.3a};
GN Synonyms=cup-10 {ECO:0000312|WormBase:Y39H10A.3a};
GN ORFNames=Y39H10A.3 {ECO:0000312|WormBase:Y39H10A.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAP79303.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH MTM-6,
RP AND SUBCELLULAR LOCATION.
RX PubMed=14565969; DOI=10.1091/mbc.e03-08-0605;
RA Dang H., Li Z., Skolnik E.Y., Fares H.;
RT "Disease-related myotubularins function in endocytic traffic in
RT Caenorhabditis elegans.";
RL Mol. Biol. Cell 15:189-196(2004).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=21076391; DOI=10.1038/emboj.2010.278;
RA Silhankova M., Port F., Harterink M., Basler K., Korswagen H.C.;
RT "Wnt signalling requires MTM-6 and MTM-9 myotubularin lipid-phosphatase
RT function in Wnt-producing cells.";
RL EMBO J. 29:4094-4105(2010).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=25479419; DOI=10.1371/journal.pone.0114501;
RA Ericson V.R., Spilker K.A., Tugizova M.S., Shen K.;
RT "MTM-6, a phosphoinositide phosphatase, is required to promote synapse
RT formation in Caenorhabditis elegans.";
RL PLoS ONE 9:E114501-E114501(2014).
CC -!- FUNCTION: May act as a regulatory subunit for mtm-6. In association
CC with phosphatase mtm-6, plays a role in endosome trafficking probably
CC by regulating phosphatidylinositol-3-phosphate levels
CC (PubMed:14565969). Regulates fluid phase endocytosis in coelomocytes
CC (PubMed:14565969). Regulates posterior migration of QL neuroblast
CC descendants and the anterior migration of QR neuroblast descendants and
CC HSN neurons during larval development probably by controlling Wnt
CC ligand secretion through the regulation of sorting receptor mig-14
CC trafficking (PubMed:21076391). Involved in the formation of correct
CC synapse number in DA9 motor neurons (PubMed:25479419).
CC {ECO:0000269|PubMed:14565969, ECO:0000269|PubMed:21076391,
CC ECO:0000269|PubMed:25479419}.
CC -!- SUBUNIT: Heterodimer with lipid phosphatase mtm-6.
CC {ECO:0000269|PubMed:14565969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14565969}. Membrane
CC {ECO:0000269|PubMed:14565969}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14565969}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y39H10A.3a};
CC IsoId=Q965W9-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y39H10A.3b};
CC IsoId=Q965W9-2; Sequence=VSP_058288;
CC -!- DEVELOPMENTAL STAGE: Expressed in the intestine and in head and tail
CC neurons including CAN neuron at L1 stage larva. Expressed in the
CC postdeirid neuron, in the developing vulva and in rectal epithelial
CC cells at L2 stage larva. Expressed in lateral hypodermal (seam) cells
CC and the hypodermal syncytium (hyp7) at L3 stage larva.
CC {ECO:0000269|PubMed:21076391}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the non-receptor class myotubularin
CC subfamily, lacks the conserved active site cysteine residue at position
CC 346 in the dsPTPase catalytic loop, suggesting that it has no
CC phosphatase activity. {ECO:0000305}.
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DR EMBL; AY313178; AAP79303.1; -; mRNA.
DR EMBL; BX284605; CCD73284.1; -; Genomic_DNA.
DR EMBL; BX284605; CCD73285.1; -; Genomic_DNA.
DR RefSeq; NP_504038.1; NM_071637.4. [Q965W9-1]
DR RefSeq; NP_872167.2; NM_182367.4. [Q965W9-2]
DR AlphaFoldDB; Q965W9; -.
DR SMR; Q965W9; -.
DR ComplexPortal; CPX-4024; MTM6-MTM9 myotubularin lipid phosphatase complex.
DR STRING; 6239.Y39H10A.3a; -.
DR EPD; Q965W9; -.
DR PaxDb; Q965W9; -.
DR PeptideAtlas; Q965W9; -.
DR EnsemblMetazoa; Y39H10A.3a.1; Y39H10A.3a.1; WBGene00003479. [Q965W9-1]
DR EnsemblMetazoa; Y39H10A.3b.1; Y39H10A.3b.1; WBGene00003479. [Q965W9-2]
DR GeneID; 178790; -.
DR KEGG; cel:CELE_Y39H10A.3; -.
DR UCSC; Y39H10A.3a; c. elegans.
DR CTD; 178790; -.
DR WormBase; Y39H10A.3a; CE26073; WBGene00003479; mtm-9. [Q965W9-1]
DR WormBase; Y39H10A.3b; CE36959; WBGene00003479; mtm-9. [Q965W9-2]
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000169600; -.
DR InParanoid; Q965W9; -.
DR OMA; RHENGAT; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q965W9; -.
DR BRENDA; 3.1.3.64; 1045.
DR Reactome; R-CEL-1660499; Synthesis of PIPs at the plasma membrane.
DR PRO; PR:Q965W9; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003479; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:1904144; C:phosphatidylinositol phosphate phosphatase complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0019902; F:phosphatase binding; IPI:WormBase.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IMP:WormBase.
DR GO; GO:0010507; P:negative regulation of autophagy; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0006907; P:pinocytosis; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0007416; P:synapse assembly; IC:ComplexPortal.
DR Gene3D; 2.30.29.30; -; 1.
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 PANTHER; PTHR10807; PTHR10807; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endocytosis; Membrane; Reference proteome.
FT CHAIN 1..569
FT /note="Myotubularin-related protein 9"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436177"
FT DOMAIN 134..513
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT VAR_SEQ 66..114
FT /note="CEPISKENPQRGGLLALKCKNFLLIIFEIGDLEICRATARTIESLSNIN ->
FT Y (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058288"
SQ SEQUENCE 569 AA; 64537 MW; CD7ABC14FA1A8D23 CRC64;
MELSELIEVT RVRDAFMRKG PRPAQVGDIC IFGHHLIFAP TTVGKEVPDN AEEFWLLHKA
VDRVLCEPIS KENPQRGGLL ALKCKNFLLI IFEIGDLEIC RATARTIESL SNINGFLHDY
AFFYNSPFTI LDDGWSAFDL EQEFARLMLS TDAFRISSVN ENFAICPTYP EKLIVPKGIG
DDYLKISATF REGGRFPVLS YFHKETKSPL VRCSQPLIGP TNRRCREDET ILNSMITVNR
GYIIDTRSKS SATAAKAKGG GAEPQGNYRQ WRYIQCPIPR QREIHDALTR MVDVCSERKV
TSDRWVSRVG QAGWLSSVAA SLEAAANVAQ CIYNERLEEV PVVIHGGDGL DSTLIASSLA
QILLDADART IRGFESVIER EWICGGHPFS LRNNHCAYAE GTVTGPFESP VFLVFLDAVH
QMIAQYPMSF EFDENFLIFL FEHAYASEFG SFLGNCEKEK KDNGIRKKTV SLWSHVHHPE
NMKQFVNVCY DPTPGVIWPS IAPQCIKIWD RLFFRWQRPD NSWSTPETET IQSLADHWKL
REKELIAKAS SLRRSVVELS RELRVLSPM
