ID MTMR6_MOUSE Reviewed; 617 AA.
AC Q8VE11;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 29-MAY-2013, entry version 86.
DE RecName: Full=Myotubularin-related protein 6;
DE EC=3.1.3.-;
GN Name=Mtmr6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mast cell;
RX PubMed=17947660;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC headgroup. Acts as a negative regulator of KCNN4/KCa3.1 channel
CC activity in CD4+ T-cells possibly by decreasing intracellular
CC levels of phosphatidylinositol 3 phosphatase. Negatively regulates
CC proliferation of reactivated CD4+ T-cells (By similarity).
CC -!- SUBUNIT: Interacts with KCNN4, MTMR7, MTMR8 and MTMR9 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus envelope (By similarity).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class myotubularin subfamily.
CC -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
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DR EMBL; AK076218; BAC36259.1; -; mRNA.
DR EMBL; AK154859; BAE32884.1; -; mRNA.
DR EMBL; CH466535; EDL36118.1; -; Genomic_DNA.
DR EMBL; BC020019; AAH20019.1; -; mRNA.
DR IPI; IPI00123689; -.
DR RefSeq; NP_659092.1; NM_144843.4.
DR UniGene; Mm.247007; -.
DR ProteinModelPortal; Q8VE11; -.
DR SMR; Q8VE11; 4-505.
DR STRING; 10090.ENSMUSP00000022563; -.
DR PhosphoSite; Q8VE11; -.
DR PaxDb; Q8VE11; -.
DR PRIDE; Q8VE11; -.
DR DNASU; 219135; -.
DR Ensembl; ENSMUST00000022563; ENSMUSP00000022563; ENSMUSG00000021987.
DR GeneID; 219135; -.
DR KEGG; mmu:219135; -.
DR UCSC; uc007ufa.2; mouse.
DR CTD; 9107; -.
DR MGI; MGI:2145637; Mtmr6.
DR eggNOG; NOG322789; -.
DR GeneTree; ENSGT00700000104053; -.
DR HOGENOM; HOG000210599; -.
DR HOVERGEN; HBG000220; -.
DR InParanoid; Q8VE11; -.
DR KO; K01112; -.
DR OMA; VFNIIMN; -.
DR OrthoDB; EOG49P9Z0; -.
DR ChiTaRS; MTMR6; mouse.
DR NextBio; 376593; -.
DR Bgee; Q8VE11; -.
DR Genevestigator; Q8VE11; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Compara.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:Compara.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010569; Myotub-related.
DR InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR Pfam; PF06602; Myotub-related; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Hydrolase; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 617 Myotubularin-related protein 6.
FT /FTId=PRO_0000367041.
FT DOMAIN 124 499 Myotubularin phosphatase.
FT REGION 248 251 Substrate binding (By similarity).
FT REGION 273 274 Substrate binding (By similarity).
FT REGION 336 342 Substrate binding (By similarity).
FT ACT_SITE 336 336 Phosphocysteine intermediate (By
FT similarity).
FT BINDING 382 382 Substrate (By similarity).
FT MOD_RES 108 108 Phosphotyrosine.
FT MOD_RES 557 557 Phosphoserine (By similarity).
FT MOD_RES 585 585 Phosphoserine (By similarity).
SQ SEQUENCE 617 AA; 70933 MW; EE699C578602A013 CRC64;
MEHIRTTKVE QVKLLDRFST NNKSLTGTLY LTATHLLFID AQQKETWILH HHIASVEKLA
LTTSGCPLVI QCKNFRIVHF IVPRERDCHD IYNSLLQLSK QAKYEDLYAF SYNPKQNDTE
RRNGWQLIDL AAEYERMGVP NANWQLSDAN REYKVCETYP RELYVPRTAS RPVIVGSSNF
RSKGRLPVLS YCRQGTEAAI CRCSQPLSGF SARCLEDEHL LQAISKANPG NRYMYVVDTR
PKLNAIANRA AGKGYENEDN YSNIRFQFVG IENIHVMRSS LQKLLEVNGS KGLSVNDFYS
GLESSGWLRH IKAVLDAAIF LAKAIVVENA SVLVHCSDGW DRTSQVCSLG SLLLDSYYRT
MKGFMVLIEK DWISFGHKFS ERCGHLDGDP REVSPVFTQF LECVWHLTQQ FPQAFEFNEA
FLLQIHEHIH SCQFGNFLGN CQKEREELRL KEKTYSLWPF LLDDKKKYLN PLYSSKSQRL
TVLEPNTASF NFKFWRNMYH QFDRTLHPRQ SVLSIIMNMN EQSKQLEEDI KDLEAKIKQC
KNGILTKELL HAVHPESPAL KTSLCLKEPS LLPVKDTLRA IEGSSPADNR YCDYAEEFSK
SEPTVVSLEY GVARMTC
//
