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   24-JAN-2024, entry version 128.
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.ENSRNOP00000074555; -.
DR   iPTMnet; Q5PQT2; -.
DR   PhosphoSitePlus; Q5PQT2; -.
DR   jPOST; Q5PQT2; -.
DR   PaxDb; 10116-ENSRNOP00000054309; -.
DR   Ensembl; ENSRNOT00000057501.3; ENSRNOP00000054309.2; ENSRNOG00000007120.8.
DR   GeneID; 305482; -.
DR   KEGG; rno:305482; -.
DR   UCSC; RGD:1310972; rat.
DR   AGR; RGD:1310972; -.
DR   CTD; 8897; -.
DR   RGD; 1310972; Mtmr3.
DR   eggNOG; KOG4471; Eukaryota.
DR   GeneTree; ENSGT00940000157272; -.
DR   InParanoid; Q5PQT2; -.
DR   OrthoDB; 5474662at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q5PQT2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; 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-phosphate 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: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; cd15732; FYVE_MTMR3; 1.
DR   CDD; cd13341; PH-GRAM_MTMR3; 1.
DR   CDD; cd14586; PTP-MTMR3; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR035888; MTMR3_PH-GRAM.
DR   InterPro; IPR046352; MTMR3_PTP.
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; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF66; MYOTUBULARIN-RELATED PROTEIN 3; 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; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   Genevisible; Q5PQT2; RN.
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
//