ID MTMR4_XENLA Reviewed; 1078 AA. AC Q7ZXF1; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Myotubularin-related protein 4; DE EC=3.1.3.48; GN Name=mtmr4; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; BC045024; AAH45024.1; -; mRNA. DR RefSeq; NP_001080273.1; NM_001086804.1. DR AlphaFoldDB; Q7ZXF1; -. DR SMR; Q7ZXF1; -. DR GeneID; 379965; -. DR KEGG; xla:379965; -. DR AGR; Xenbase:XB-GENE-986319; -. DR CTD; 379965; -. DR Xenbase; XB-GENE-986319; mtmr4.L. DR OrthoDB; 5474662at2759; -. DR Proteomes; UP000186698; Chromosome 2L. DR Bgee; 379965; Expressed in spleen and 19 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR CDD; cd15733; FYVE_MTMR4; 1. DR CDD; cd13342; PH-GRAM_MTMR4; 1. DR CDD; cd14587; PTP-MTMR4; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR046978; MTMR4_FYVE. DR InterPro; IPR035997; MTMR4_PH-GRAM. DR InterPro; IPR030590; MTMR4_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; 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:SF64; MYOTUBULARIN-RELATED PROTEIN 4; 1. DR Pfam; PF01363; FYVE; 1. DR Pfam; PF06602; Myotub-related; 1. DR SMART; SM00064; FYVE; 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. PE 2: Evidence at transcript level; KW Coiled coil; Cytoplasm; Hydrolase; Membrane; Metal-binding; KW Protein phosphatase; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1..1078 FT /note="Myotubularin-related protein 4" FT /id="PRO_0000304811" FT DOMAIN 154..571 FT /note="Myotubularin phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669" FT ZN_FING 997..1057 FT /note="FYVE-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT REGION 267..290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 629..694 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 960..982 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 904..935 FT /evidence="ECO:0000255" FT COMPBIAS 268..290 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 629..660 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 667..683 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 408 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044" FT BINDING 321..324 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 346..347 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 408..414 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 454 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 1003 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1006 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1019 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1022 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1027 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1030 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1049 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1052 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" SQ SEQUENCE 1078 AA; 122251 MW; D036A01723DB8045 CRC64; MGDEPPSLEY IQAKDLFPPR ELVKEEEKLQ VPFPVLPGEG VEYLGSANDA VIAISNYRLH IKFKDSVVNV PLRMIEAVES RDMFQLQIIC KDSKVVRCHF STFKQCQEWL KRLSRATLRP AKQEDLFAFA YHAWCQGVCT DEEEPLIHLC RPGDHVKSRF QIELKRMGFD LQNAWRVSEI NNNYKLCQSY PQKLLVPVWI TDKELENVAT FRSWKRIPVV VYRHTRTGAV IARCSQPEIS WWGWRNADDE YLVTSIAKAC ALNPAVRMPN GNPSNKGNND GSDNSDTDFD SSLTACPVEG GGVPQKLLIV DARSYTAAVA NRAKGGGCEC EEYYPNCEVA FMGMANIHSI RNSFQYLRAV CNQVPDPGNW LSALESTKWL QHLSAMLKAA TVVASAVDRE ERPVLVHCSD GWDRTPQIVS LAKILLDPYY RTLEGFQVLV ETDWLDYGHK FADRCGHQEN REDQNEQCPV FLQWLDCIHQ LLFQFPCHFE FNHAFLVKLV QHTYSCLYGT FLANNLCERE MRNIYKRTCS VWSLLRTGNK IFHNLLYMPG SDLVLHPVCH VRALQLWTAV YLPATSPCTP MDDRMEMYLT PASQGPQFHA RSLVRLPKTR SMDNLLTACD SGGLLTRTSS DPNLNNHQGN LESCSSSKEG NETEICDIQQ QALSIEPKEE DGNDSKSTDH ENEDSGSATN QNNNEQNALN NILSIAKPDS IQCKRDRFKS VLEKSSVIPV PSNEGTITDD NSHSNGTSEH LPVPALVTNG SVQNKSCVDV SKAMKLSTEL SRTDKKPVFQ TQRDEFSFCT SNWDSLPGMM RSVPICEVGL RRPLSYDCST RSQHSRNGRH TMKLTGNLPA SFHCSGPFTK RCRCVMACHT KQVQGSRFLP LACPSPAPLI YQDDDGLPIP SDVVQQRLRQ MEASYKQEVD LLRRQVWELQ LQLEIRQYCA PPSEPEADYE DDFTCVKESD GSDMDDLYSD KSEDRLSEAS WEPVDKKETE VTRWVPDHMA SHCFNCDCEF WLAKRRHHCR NCGNVFCAAC CHLKLPIPDQ QLYDPVLVCN TCYDHIQVSR ARELMSQQLK KPLTAASS //