ID A0A2R9BYZ9_PANPA Unreviewed; 1138 AA.
AC A0A2R9BYZ9;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSPPAP00000033715.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000033715.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000033715.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000033715.1}
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}.
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DR EMBL; AJFE02058898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02058899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02058900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9BYZ9; -.
DR Ensembl; ENSPPAT00000056592.1; ENSPPAP00000033715.1; ENSPPAG00000039667.1.
DR GeneTree; ENSGT00940000158976; -.
DR Proteomes; UP000240080; Chromosome 17.
DR Bgee; ENSPPAG00000039667; Expressed in cerebellum and 6 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: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:UP000240080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 153..594
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 376..420
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1057..1117
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 588..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 320..323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 345..346
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 407..413
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1138 AA; 126570 MW; DBB57B105FCC8396 CRC64;
MGEEGPPSLE YIQAKDLFPP KELVKEEENL QVPFTVLQGE GVEFLGRAAD ALIAISNYRL
HIKFKDSVIN VPLRMIDSVE SRDMFQLHIS CKDSKVVRCH FSTFKQCQEW LSRLSRATAR
PAKPEDLFAF AYHAWCLGLT EEDQHTHLCQ PGEHIRCRQE AELARMGFDL QNVWRVSHIN
SNYKLCPSYP QKLLVPVWIT DKELENVASF RSWKRIPVVV YRHLRNGAAI ARCSQPEISW
WGWRNADDEY LVTSIAKACA LDPGTRATGG SLGTGNNDTS EACDADFDSS LTACSGVEST
AAPQKLLILD ARSYTAAVAN RAKGGGCECE EYYPNCEVVF MGMANIHAIR NSFQYLRAVC
SQMPDPSNWL SALESTKWLQ HLSVMLKAAV LVANTVDREG RPVLVHCSDG WDRTPQIVAL
AKILLDPYYR TLEGFQVLVE SDWLDFGHKF GDRCGHQENV EDQNEQCPVF LQWLDSVHQL
LKQFPCLFEF NEAFLVLHPV CHVRALHLWT AVYLPASSPC TLGEENMDLY LSPVAQSQEF
SGRSLDRLPK TRSMDDLLSA CDTSSPLTRT SSDPNLNNHC QEVRVGLEPW HSNPEGSETS
FVDSGVGGPQ QTVGEVGLPP PLPSSQKDYL SNKPFKSHKS CSPSYKQLNT AVPREMKSNT
SDPEIKVLEE TKGPAPDPSA QDELGRTLDG IGEPPEHCPE TEAVSALSKV ISNKCDGVCN
FPESSQNSPT GTPQQAQPDS MLGVPSKCVL DHSLSTVCNP PSAACQTPLD PSADFLNQDP
SGSVASISHQ EQLSSVPDLT HGEEDTGKRG NNRNGQLLEN PRFGKMPLEL VRKPISQSQI
SEFSFLGSNW DSFQGMVTSF PSGEATPRRL LSYGCCSKRP NSKQMRATGP CFGGQWAQRE
GVKSPVCSSH SNGHCTGPGG KNQMWLSGHP KQVSSTKPVP LTCPSPVPPL YLDDDGLPFP
TDVIQHRLRQ IEAGYKQEVE QLRRQVRELQ MRLDIRHCCA PPAEPPMDYE DDFTCLKESD
GSDTEDFGSD HSEDCLSEAS WEPVDKKETE VTRWVPDHMA SHCYNCDCEF WLAKRRHHCR
NCGNVFCAGC CHLKLPIPDQ QLYDPVLVCN SCYEHIQVSR ARELMSQQLK KPIATASS
//
