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 27-MAR-2024, entry version 122. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSGALP00000027747; -. DR PaxDb; 9031-ENSGALP00000042583; -. DR Ensembl; ENSGALT00000044926; ENSGALP00000042583; ENSGALG00000017200. DR GeneID; 418992; -. DR KEGG; gga:418992; -. DR CTD; 8898; -. DR VEuPathDB; HostDB:geneid_418992; -. DR eggNOG; KOG4471; Eukaryota. DR HOGENOM; CLU_001839_4_1_1; -. DR InParanoid; Q5ZIV1; -. 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 cell types or tissues. DR ExpressionAtlas; Q5ZIV1; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IBA:GO_Central. 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:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB. DR CDD; cd13356; PH-GRAM_MTMR2_mammal-like; 1. DR CDD; cd14590; PTP-MTMR2; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; MYOTUBULARIN-RELATED; 1. DR PANTHER; PTHR10807:SF42; MYOTUBULARIN-RELATED PROTEIN 2; 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; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF50729; PH domain-like; 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 //