MTMRE_MOUSE
ID MTMRE_MOUSE Reviewed; 648 AA.
AC Q8VEL2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Myotubularin-related protein 14;
DE EC=3.1.3.-;
DE AltName: Full=mJumpy;
GN Name=Mtmr14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=17008356; DOI=10.1093/hmg/ddl250;
RA Tosch V., Rohde H.M., Tronchere H., Zanoteli E., Monroy N., Kretz C.,
RA Dondaine N., Payrastre B., Mandel J.-L., Laporte J.;
RT "A novel PtdIns3P and PtdIns(3,5)P2 phosphatase with an inactivating
RT variant in centronuclear myopathy.";
RL Hum. Mol. Genet. 15:3098-3106(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Lipid phosphatase which efficiently dephosphorylates
CC phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2; inactive
CC toward PtdIns4P, PtdIns(3,4)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P3.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Found in reticular structures and
CC plasma membrane ruffles. Concentrated near the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: In C2C12 cell line, increased expression during
CC myotube formation and differentiation in culture.
CC {ECO:0000269|PubMed:17008356}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18294.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC018294; AAH18294.1; ALT_INIT; mRNA.
DR CCDS; CCDS20412.2; -.
DR RefSeq; NP_081125.2; NM_026849.2.
DR RefSeq; XP_006506888.1; XM_006506825.1.
DR AlphaFoldDB; Q8VEL2; -.
DR BioGRID; 220681; 1.
DR STRING; 10090.ENSMUSP00000108771; -.
DR GlyGen; Q8VEL2; 3 sites.
DR iPTMnet; Q8VEL2; -.
DR PhosphoSitePlus; Q8VEL2; -.
DR EPD; Q8VEL2; -.
DR MaxQB; Q8VEL2; -.
DR PaxDb; Q8VEL2; -.
DR PeptideAtlas; Q8VEL2; -.
DR PRIDE; Q8VEL2; -.
DR ProteomicsDB; 286082; -.
DR Antibodypedia; 25426; 269 antibodies from 26 providers.
DR DNASU; 97287; -.
DR Ensembl; ENSMUST00000113146; ENSMUSP00000108771; ENSMUSG00000030269.
DR GeneID; 97287; -.
DR KEGG; mmu:97287; -.
DR UCSC; uc009dex.2; mouse.
DR CTD; 64419; -.
DR MGI; MGI:1916075; Mtmr14.
DR VEuPathDB; HostDB:ENSMUSG00000030269; -.
DR eggNOG; ENOG502QQ9R; Eukaryota.
DR GeneTree; ENSGT00390000018852; -.
DR HOGENOM; CLU_016325_2_0_1; -.
DR InParanoid; Q8VEL2; -.
DR OMA; QIVYLEY; -.
DR OrthoDB; 775284at2759; -.
DR PhylomeDB; Q8VEL2; -.
DR TreeFam; TF324044; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR BioGRID-ORCS; 97287; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Mtmr14; mouse.
DR PRO; PR:Q8VEL2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VEL2; protein.
DR Bgee; ENSMUSG00000030269; Expressed in animal zygote and 250 other tissues.
DR ExpressionAtlas; Q8VEL2; baseline and differential.
DR Genevisible; Q8VEL2; MM.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISO:MGI.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd13213; PH-GRAM_MTMR14; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR039802; MTMR14.
DR InterPro; IPR039803; MTMR14_PH-GRAM.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR PANTHER; PTHR13524; PTHR13524; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Glycoprotein; Hydrolase; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..648
FT /note="Myotubularin-related protein 14"
FT /id="PRO_0000260215"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 329
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCE2"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCE2"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCE2"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCE2"
FT MOD_RES 636
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCE2"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 648 AA; 72443 MW; E1927FE8F32BB38D CRC64;
MAGARAAAAA SAGSTASSGS PPPQEPGLWE LLEEFSRTQY RAKDSGGKSG SKVERIEKRC
LELFGRDYCF SVIPNVNGDI CGHYPRHIVF LEYESSEKEK DTFQSTVQVN KLQDLIHRSK
MARCRGRFVC PVILFKGKHI CRSATLAGWG ELYGRSGYNY LFSGGADDTW ASTEDVTEED
FVLRSGDTHL FDKVRGYDIK LLQYLSVKYI CDLMVENKKV KFGMNVTSSE KVDKAQRYAN
FTLLSIPYPG CEFFKEYKDR DYMAEGLIFN WKQDYVDAPL NIPNFLTQSL NIDWSQYQSW
DLVQQTQNYL KLLLFIMNRD DDSGLLVHCI SGWDRTPLFI SLLRLSLWAD GLIHTSLKPA
EILYLTVAYD WFLFGHMLVD RLSKGEEIFF FCFNFLKHIT SEEFCLKTQR RKSLPTRDAG
FTVEDICMLR HKDRGSTTSL GSDFSLVLEH SPGAVGSFSY ETVELAPAGA PTQAAWRKSH
SSSPQSMLWS RPQPSEERLP SHHGLTEAKS SSSSSSNHSD NFFRMGSSPL EVPKPRSVDH
PLPGSSLSTD FGSWQLVSGC GSIQDRPVLH TDSSLPFSFQ DELPNSCLLT ALSDRETRLQ
EVRSAFLAAY SSTVGLRAAT PSPSGAIGGL LEQFARGVGL RGTSTSTL
