MTMR4_MOUSE
ID MTMR4_MOUSE Reviewed; 1190 AA.
AC Q91XS1; Q5ND06; Q5ND08;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Myotubularin-related protein 4;
DE EC=3.1.3.48;
GN Name=Mtmr4;
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 [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Bone marrow;
RA Gorski K.S., Shin T., Otuji M., Suyi T., Pardoll D., Tsuchiya H.;
RT "Isolation of a FYVE zinc finger containing phosphatase expressed in mouse
RT bone marrow derived dendritic cells.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Amnion;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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: Dephosphorylates proteins phosphorylated on Ser, Thr, and Tyr
CC residues and low molecular weight phosphatase substrate para-
CC nitrophenylphosphate. Phosphorylates phosphatidylinositol 3,4,5-
CC trisphosphate (PIP3) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Localized to
CC perinuclear region. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91XS1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91XS1-2; Sequence=VSP_028126;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; AF262986; AAK58180.1; -; mRNA.
DR EMBL; AK146641; BAE27324.1; -; mRNA.
DR EMBL; AL596086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25214.1; -. [Q91XS1-1]
DR CCDS; CCDS88215.1; -. [Q91XS1-2]
DR RefSeq; NP_573478.1; NM_133215.1. [Q91XS1-1]
DR RefSeq; XP_006532447.1; XM_006532384.3. [Q91XS1-1]
DR RefSeq; XP_006532448.1; XM_006532385.3. [Q91XS1-1]
DR RefSeq; XP_011247082.1; XM_011248780.2. [Q91XS1-1]
DR AlphaFoldDB; Q91XS1; -.
DR SMR; Q91XS1; -.
DR BioGRID; 228413; 3.
DR STRING; 10090.ENSMUSP00000099468; -.
DR iPTMnet; Q91XS1; -.
DR PhosphoSitePlus; Q91XS1; -.
DR EPD; Q91XS1; -.
DR MaxQB; Q91XS1; -.
DR PaxDb; Q91XS1; -.
DR PRIDE; Q91XS1; -.
DR ProteomicsDB; 286077; -. [Q91XS1-1]
DR ProteomicsDB; 286078; -. [Q91XS1-2]
DR Antibodypedia; 30984; 190 antibodies from 26 providers.
DR DNASU; 170749; -.
DR Ensembl; ENSMUST00000092802; ENSMUSP00000090478; ENSMUSG00000018401. [Q91XS1-2]
DR Ensembl; ENSMUST00000103179; ENSMUSP00000099468; ENSMUSG00000018401. [Q91XS1-1]
DR Ensembl; ENSMUST00000119628; ENSMUSP00000112902; ENSMUSG00000018401. [Q91XS1-1]
DR GeneID; 170749; -.
DR KEGG; mmu:170749; -.
DR UCSC; uc007ktz.1; mouse. [Q91XS1-1]
DR UCSC; uc007kua.1; mouse. [Q91XS1-2]
DR CTD; 9110; -.
DR MGI; MGI:2180699; Mtmr4.
DR VEuPathDB; HostDB:ENSMUSG00000018401; -.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000158976; -.
DR HOGENOM; CLU_001839_2_2_1; -.
DR InParanoid; Q91XS1; -.
DR OMA; TRWLQHM; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q91XS1; -.
DR TreeFam; TF315197; -.
DR Reactome; R-MMU-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-MMU-1660517; Synthesis of PIPs at the late endosome membrane.
DR Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
DR BioGRID-ORCS; 170749; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Mtmr4; mouse.
DR PRO; PR:Q91XS1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91XS1; protein.
DR Bgee; ENSMUSG00000018401; Expressed in urogenital fold and 237 other tissues.
DR ExpressionAtlas; Q91XS1; baseline and differential.
DR Genevisible; Q91XS1; MM.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:InterPro.
DR CDD; cd13342; PH-GRAM_MTMR4; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR030590; MTMR4.
DR InterPro; IPR035997; MTMR4_PH-GRAM.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR PANTHER; PTHR10807:SF64; PTHR10807:SF64; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Hydrolase; Membrane;
KW Metal-binding; Phosphoprotein; Protein phosphatase; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..1190
FT /note="Myotubularin-related protein 4"
FT /id="PRO_0000304810"
FT DOMAIN 153..570
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT ZN_FING 1109..1169
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 616..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1020..1052
FT /evidence="ECO:0000255"
FT COMPBIAS 616..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 320..323
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345..346
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 407..413
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYA4"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYA4"
FT VAR_SEQ 497..553
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_028126"
SQ SEQUENCE 1190 AA; 132885 MW; 37E6741227E9DBFF CRC64;
MGEEGPPSLE YIQAKDLFPP KELVKEEENL QVPFTVLQGE GVEFLGRATD ALIAISNYRL
HIKFKDSVIN VPLRMIDSVE SRDMFQLHIA CKDSKVVRCH FSTFKQCQEW LSRLSRATAR
PAKPEDLFAF AYHAWCLGLT EEDQHTHLCQ PGEHIRCRQE AELARMGFDL QNVWRVSHIN
SNYKLCPSYP QKLLVPVWIT DKELENVASF RSWKRIPVVV YRHLRNGAAI ARCSQPEISW
WGWRNADDEY LVTSIAKACA LDPGTRASGG SLSTGTNDAS EACDTDFDSS LTACSGVEST
AAPQKLLILD ARSYTAAVAN RAKGGGCECE EYYPNCEVLF MGMANIHAIR NSFQYLRAVC
SQMPDPSNWL SALESTKWLQ HLSVMLKAAV LVANTVDREG RPVLVHCSDG WDRTPQIVAL
AKILLDPYYR TLEGFQVLVE SDWLDFGHKF GDRCGHQENA EDQNEQCPVF LQWLDSVHQL
LKQFPCLFEF NEAFLVKLVQ HTYSCLYGTF LANNPCEREK RNIYKRTCSV WALLRAGNKN
FHNFLYTPGS DVVLHPVCHV RALHLWTAVY LPASSPCTLG EENMDLYLSP VAQSQEFSGR
SLDRLPKTRS MDDLLSACDT SSPLTRTSSD PNLNNHSQEV RGSLEPWHSS PEGAETVIDS
GVGSPQLTVG EMGLPPPLPS SQKEYLSNKP FKGHKSCSLS YKLLNTSVSW EMKSNTSDIK
VLEETEALAP DPSAQEEQGR TSDGLGKPPE QFLEKEAVSS LCSVSSKCGG ACDFPEPPQD
PLTGTPQQPH LDSMQISPSR CTPDHSQGSL CNPPSVASQT PEPNTDLLSQ DPPGSTASIS
HQEQPSSVPD LIYKKEDAGK RGSKNGQLLE NPRFGKMPLE LARKPISQSQ ISEFSFLGSN
WDSFQGMMTS FPSGETTPRR LLAYGCCSKR PSNKHIRAAG PCLGGQWAQR EGMKSPVCSS
HSNGHCTGPG GKNNRMWFSS HPKQVSSTKP SLLSCPSPVP PLYLDDDGLP FPTDVIQHRL
RQIEAGYRQE VEQLRRQVRE LQMRLDIRHC CAPPAEPPMD YEDDFTCLKE SDGSDTEDFG
SDHSEDCLSE ASWEPVDKKE TEVTRWVPDH MASHCFNCDC EFWLAKRRHH CRNCGNVFCA
GCCHLKLPIP DQQLYDPVLV CNSCYEHIQV SRARELMSQH LKKPIATASS
