ID G1R9X4_NOMLE Unreviewed; 1163 AA.
AC G1R9X4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=MTMR4 {ECO:0000313|Ensembl:ENSNLEP00000010021.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000010021.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000010021.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000010021.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023732};
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:0000256|ARBA:ARBA00001291};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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; ADFV01070576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01070577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01070578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01070579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01070580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01070581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1R9X4; -.
DR STRING; 61853.ENSNLEP00000010021; -.
DR Ensembl; ENSNLET00000010511.2; ENSNLEP00000010021.2; ENSNLEG00000008197.2.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000158976; -.
DR HOGENOM; CLU_001839_2_2_1; -.
DR InParanoid; G1R9X4; -.
DR OMA; TRWLQHM; -.
DR TreeFam; TF315197; -.
DR Proteomes; UP000001073; Chromosome 14.
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:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IEA:UniProt.
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; IPR000387; Tyr_Pase_dom.
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; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 152..569
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 375..419
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1082..1142
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 800..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 406
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 319..322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 344..345
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 406..412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1163 AA; 130267 MW; 3BE5DE8BC31D5FF3 CRC64;
GEEGPPSLEY IQAKDLFPHK ELVKEEENLQ VPFTVLQGEG VEFLGRAADA LIAISNYRLH
IKFKDSVINV PLRMIDSVES RDMFQLHISC KDSQVVRCHF STFKQCQEWL SRLSRATARP
AKPEDLFAFA YHAWCLGLTE EDQHTHLCQP GEHIRCRQEA ELARMGFDLQ NVWRVSHINS
NYKLCPSYPQ KLLVPVWITD KELENVASFR SWKRIPVVVY RHLRNGAAIA RCSQPEISWW
GWRNADDEYL VTSIAKACAL DPGTRATGGS LSTGNNDTSE ACDADFDSSL TACSGVESTA
APQKLLILDA RSYTAAVANR AKGGGCECEE YYPNCEVVFM GMANIHAIRN SFQYLRAVCS
QMPDPSNWLS ALESTKWLQH LSVMLKAAVL VANTVDREGR PVLVHCSDGW DRTPQIVALA
KILLDPYYRT LEGFQVLVES DWLDFGHKFG DRCGHQENVE DQNEQCPVFL QWLDSVHQLL
KQFPCLFEFN EAFLVKLVQH TYSCLYGTFL ANNPCEREKR NIYKRTCSVW ALLRAGNKNF
HNFLYTPSSD MVLHPVCHVR ALHLWTAVYL PASSPCTLGE ENMDLYLSPV AQSQEFSGRS
LDRLPKTRSM DDLLSACDTS SPLTRTSSDP NLNNHCQEVR VGLEPWHSNP EGSEATFVDS
GVGGPQQTVG EVGLPPPLPS SQKDYLSNKP FKGHKSCSPS YKLLNTAVPW EMKSNTSDPE
IKRTSSRPFL HFSKVISNQC DGVCNFPESS QDSPTGMPQQ AQPDSMLGVP SKCVLDHSLS
TLCNPPSAAC QTPLDPSADF LNQDPSGSVA SISHQEQLSS VPDLTHGEED IGKRGNNRNG
QLLENPRFGK MPLELVRKPI SQSQISEFSF LGSNWDSFQG MVTSFPSGEA TPRRLLSYGC
CSKRPNSKQM RATGPCFGGQ WAQREGVKSP VCSSHSNGHC TGPGGKNRMW LSSHPKQVSS
TKPVPLTCPS PVPPLYLDDD GLPFPTDVIQ HRLRQIEAGY KQEVEQLRRQ VRELQMRLDI
RHCCAPPAEP PMDYEDDFTC LKESDGSDTE DFGSDHSEDC LSEASWEPVD KKETEVTRWV
PDHMASHCYN CDCEFWLAKR RHHCRNCGNV FCAGCCHLKL PIPDQQLYDP VLVCNSCYEH
IQVSRARELM SQQLKKPIAT ASS
//
