MTMR3_RAT
ID MTMR3_RAT Reviewed; 1194 AA.
AC Q5PQT2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Myotubularin-related protein 3;
DE EC=3.1.3.48;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000250|UniProtKB:Q13615};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:Q13615};
GN Name=Mtmr3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC headgroup. Has phosphatase activity towards phosphatidylinositol 3-
CC phosphate and phosphatidylinositol 3,5-bisphosphate. May also
CC dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues
CC (By similarity). {ECO:0000250|UniProtKB:Q13615}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q13615, ECO:0000255|PROSITE-
CC ProRule:PRU10044};
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:0000250|UniProtKB:Q13615};
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:0000250|UniProtKB:Q13615};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:45640, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:72835, ChEBI:CHEBI:78995;
CC Evidence={ECO:0000250|UniProtKB:Q13615};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78994,
CC ChEBI:CHEBI:84968; Evidence={ECO:0000250|UniProtKB:Q13615};
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:0000250|UniProtKB:Q13615};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13615}.
CC Membrane {ECO:0000250|UniProtKB:Q13615}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q13615}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; BC087045; AAH87045.1; -; mRNA.
DR RefSeq; NP_001012038.1; NM_001012038.1.
DR AlphaFoldDB; Q5PQT2; -.
DR SMR; Q5PQT2; -.
DR STRING; 10116.ENSRNOP00000054309; -.
DR iPTMnet; Q5PQT2; -.
DR PhosphoSitePlus; Q5PQT2; -.
DR jPOST; Q5PQT2; -.
DR PaxDb; Q5PQT2; -.
DR PRIDE; Q5PQT2; -.
DR Ensembl; ENSRNOT00000057501; ENSRNOP00000054309; ENSRNOG00000007120.
DR GeneID; 305482; -.
DR KEGG; rno:305482; -.
DR UCSC; RGD:1310972; rat.
DR CTD; 8897; -.
DR RGD; 1310972; Mtmr3.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000157272; -.
DR InParanoid; Q5PQT2; -.
DR PhylomeDB; Q5PQT2; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR PRO; PR:Q5PQT2; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000007120; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q5PQT2; baseline and differential.
DR Genevisible; Q5PQT2; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR GO; GO:1904562; P:phosphatidylinositol 5-phosphate metabolic process; ISO:RGD.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:RGD.
DR GO; GO:2000785; P:regulation of autophagosome assembly; ISO:RGD.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; ISO:RGD.
DR CDD; cd13341; PH-GRAM_MTMR3; 1.
DR CDD; cd14586; PTP-MTMR3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR046352; MTMR3_Pase_dom.
DR InterPro; IPR035888; MTMR3_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; IPR003595; Tyr_Pase_cat.
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 Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00404; PTPc_motif; 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; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Hydrolase; Lipid metabolism; Membrane;
KW Metal-binding; Phosphoprotein; Protein phosphatase; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..1194
FT /note="Myotubularin-related protein 3"
FT /id="PRO_0000304808"
FT DOMAIN 151..572
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT ZN_FING 1115..1175
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 583..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1025..1058
FT /evidence="ECO:0000255"
FT COMPBIAS 693..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 322..325
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 347..348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 409..415
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13615"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13615"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13615"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13615"
FT MOD_RES 725
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13615"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13615"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K296"
SQ SEQUENCE 1194 AA; 133500 MW; D0F4497AD70D5EE4 CRC64;
MRHSLECIQA NQIFPRKQLI REDENLQVPF LELHGESTEY VGRAEDAIIA LSNYRLHIKF
KESLVNVPLQ LIESVECRDI FQLHLTCKDC KVIRCQFPTF EQCQDWLKRL NNAIRPPGKI
EDLFSFAYHA WCMEVYASEK EQHGDLCRPG EHVTSRFKNE VERMGFDMNN AWRISNINEK
YKLCGSYPQE LIVPAWITDK ELESVAGFRS WKRIPAVIYR HQSNGAVIAR CGQPEVSWWG
WRNADDEHLV QSVAKACASD SQSSVGKVST RNSCRGFPNA GDLSDVEFDA SLSNASGTES
LALQPQKLLI LDARSYAAAV ANRAKGGGCE CPEYYPNCEV VFMGMANIHS IRRSFQSLRL
LCTQMPDPGN WLSALESTKW LHHLSVLLKS ALLVVHAVDR DQRPVLVHCS DGWDRTPQIV
ALAKLLLDPY YRTVEGFQVL VEMEWLDFGH KFADRCGHGE NSDDLNERCP VFLQWLDCVH
QLQRQFPCSF EFNEAFLVKL VQHTYSCLFG TFLCNNAKER GEKQTQERTC SVWSLLRAGN
KAFKNLLYSS QSEAVLYPVC HVRNLMLWSA VYLPCPSPST PTDDSCAPYP APGTSPDEPP
LSRLPKTRSF DNLTTTCDNM VPLASRRSSD PSLNEKWQEH GRSLELSSFA GSGEEVPAID
SLRRPSRLLG GAELSVAAGV AEGQMENILQ EATKEESGVE EPTHREHTEV PEVKEEAPLA
KESRTAAQGS GVLYQEPQLD DATLRSHLGP SLSSFSQGIP EHREVGHSVL SSSLPASLRG
EDSQEVPVEQ PQVENIAEDR ENVVPAVPVD VKIGLGTSES SPLLPSQVPF ETRGPHMNNS
VHMLLEDKVK SESGPQLHHR PCLASSGRFS GKDMLPIAPE PRSAERPQWD SVLHRTSSPG
NTLSLMMQAP CALPLDKCRQ RIVCNGALET ENKASEQPAG FDTLQKYPTP NGHCANGETG
RSKDSLSHQL SATSYSSAHS CSRNLHHKWL NSHSGRPSTT NSPEQPSRSH LDDDGMPVYT
DTIQQRLRQI ESGHQQEVET LKKQVQELKS RLESQYLTSS LRFNGDFGDE VTSIPDSESN
LDQNCLSRCS TEIFSEASWE QVDKQDTEMT RWLPDHLAAH CYACDSAFWL ASRKHHCRNC
GNVFCSSCCN QKVPVPSQQL FEPSRVCKSC YSSLHPTSSS IDLELDKPIA ATSN
