MTMR2_CHICK
ID MTMR2_CHICK Reviewed; 571 AA.
AC Q5ZIV1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Myotubularin-related protein 2;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000250|UniProtKB:Q13614};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:Q13614};
GN Name=MTMR2; ORFNames=RCJMB04_23g22;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q13614}.
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:Q13614};
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:Q13614};
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:Q13614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911,
CC ChEBI:CHEBI:85342; Evidence={ECO:0000250|UniProtKB:Q13614};
CC -!- SUBUNIT: Homooligomer and heterooligomer.
CC {ECO:0000250|UniProtKB:Q13614}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13614}. Early
CC endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q13614}. Note=Partly associated with
CC membranes. {ECO:0000250|UniProtKB:Q13614}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; AJ720683; CAG32342.1; -; mRNA.
DR RefSeq; NP_001034363.1; NM_001039274.1.
DR RefSeq; XP_015135444.1; XM_015279958.1.
DR RefSeq; XP_015135452.1; XM_015279966.1.
DR RefSeq; XP_015135459.1; XM_015279973.1.
DR AlphaFoldDB; Q5ZIV1; -.
DR SMR; Q5ZIV1; -.
DR STRING; 9031.ENSGALP00000042583; -.
DR PaxDb; Q5ZIV1; -.
DR PRIDE; Q5ZIV1; -.
DR Ensembl; ENSGALT00000027800; ENSGALP00000027747; ENSGALG00000017200.
DR Ensembl; ENSGALT00000044926; ENSGALP00000042583; ENSGALG00000017200.
DR Ensembl; ENSGALT00000102271; ENSGALP00000066323; ENSGALG00000017200.
DR GeneID; 418992; -.
DR KEGG; gga:418992; -.
DR CTD; 8898; -.
DR VEuPathDB; HostDB:geneid_418992; -.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000153669; -.
DR HOGENOM; CLU_001839_4_1_1; -.
DR InParanoid; Q5ZIV1; -.
DR OMA; ESYAICD; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q5ZIV1; -.
DR TreeFam; TF315197; -.
DR Reactome; R-GGA-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-GGA-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-GGA-1660517; Synthesis of PIPs at the late endosome membrane.
DR PRO; PR:Q5ZIV1; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000017200; Expressed in brain and 14 other tissues.
DR ExpressionAtlas; Q5ZIV1; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
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:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Endosome; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome.
FT CHAIN 1..571
FT /note="Myotubularin-related protein 2"
FT /id="PRO_0000356229"
FT DOMAIN 1..67
FT /note="GRAM"
FT DOMAIN 133..508
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 544..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 521..553
FT /evidence="ECO:0000255"
FT COMPBIAS 546..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 345
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 258..261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283..284
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345..351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 571 AA; 65968 MW; 6C984994DCB04B27 CRC64;
MEEPPLLPGE TIKDMAKDVT YICPFTGAIR GTLTVTNYRL YFKSMERDPP FVLDASLGVI
NRVEKIGGAS SRGENSYGLE IVCKDIRNLR FAHKPEGRTR RSIFENLMKY AFPVSNNLPL
FAFEYKEVFP ENGWKVYDPI WEYRRQGIPN ESWRLSKINE HYELCDTYPA ILAVPVNIPD
EELKRVASFR SRGRIPVLSW IHPESQATIT RCSQPMVGVS GKRSKEDEKY LQAIMDSNAQ
SHKIFIFDAR PSVNAVANKA KGGGYESEDA YQNAELVFLD IHNIHVMRES LRKLKEIVYP
NIEETHWLSN LESTHWLEHI KLILAGALRI ADKVESGKTS VVVHCSDGWD RTAQLTSLSL
LMLDGYYRTI RGFEVLVEKE WLSFGHRFQL RVGHGDKNHA DADRSPVFLQ FIDCVWQMTR
QFPTAFEFNE YFLITILDHL YSCLFGTFLC SSEQQRVKES LPKKTVSLWS YINSQLEDFT
NPLYVSYSNH VLYPVASMRH LELWVGYYIR WNPRMKPQEP VHNRYKELLA KRAELQKKVE
ELQREITNRS TSSSERAGSP AQCVTPVQTV V
