MTMR4_XENLA
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 03-AUG-2022, entry version 97.
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}.
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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 CTD; 379965; -.
DR Xenbase; XB-GENE-986319; mtmr4.L.
DR OrthoDB; 824298at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 379965; Expressed in spleen and 19 other 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:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:InterPro.
DR CDD; cd13342; PH-GRAM_MTMR4; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR030590; MTMR4.
DR InterPro; IPR035997; MTMR4_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; 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; 2.
DR PANTHER; PTHR10807:SF64; PTHR10807:SF64; 2.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 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 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
