ID A0A401S0A2_CHIPU Unreviewed; 656 AA.
AC A0A401S0A2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=phosphatidylinositol-3-phosphatase {ECO:0000256|ARBA:ARBA00013038};
DE EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
GN ORFNames=chiPu_0002232 {ECO:0000313|EMBL:GCC23834.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC23834.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC23834.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC23834.1}.
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DR EMBL; BEZZ01000040; GCC23834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401S0A2; -.
DR STRING; 137246.A0A401S0A2; -.
DR OMA; GSDFMYV; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR CDD; cd13344; PH-GRAM_MTMR7; 1.
DR CDD; cd14583; PTP-MTMR7; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR036003; MTMR7_PH-GRAM.
DR InterPro; IPR030572; MTMR7_PTP.
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 PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF35; MYOTUBULARIN-RELATED PROTEIN 7; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF21098; PH-GRAM_MTMR6-like; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT DOMAIN 126..502
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 570..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 519..546
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 570..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 275..276
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 338..344
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 656 AA; 75336 MW; D0C8D9B47C6E18EC CRC64;
MEHIRTPKVE NVRMLDRVSS KKASVGSLYL TATHLIFVEN LSDSRKETWI LHSQICAVEK
QATTATGCPL LIRCKNFQVI QFIISQERDC HDIYISLIRL SRPVKYEELY CFSFNPKQEG
NERERGWNLT DLKAEYKRMG VPNNLWQVSH ANRDYGVCDT YPTELYVPKS VSTPVIVGSS
KFRSRGRFPV LCYFCQDNNA AICRSSQPLS GFSARCLEDE QMLQAIRKSN PGRDFLYVVD
TRPKLNAMAN RAAGKGYENE DNYSNIKFHF IGIENIHVMR NSLQKLLDVC ELRSPSMSDF
LWGLENSGWL KHIKAIMDAG IFIAKAVAEE AASVLVHCSD GWDRTAQVCS IAGLLLDPFY
RTLKGFMVLI EKDWVSFGHK FNHRYSHLDG DPREVSPVID QFFDCVWQLM EQFPCAFEFN
ERFLVHIHHH IYSCQFGNFI CNSNKESKEL RIQEKTQSLW PHLWKNGVDY KNPLYRQNHS
QTQGVLRPHT APSNFRFWRS MYNRFEKGMH PRQSVTEFLM AVKEETQQLE DELEILEEKL
GRLDQSQLRN RKVEIKLPHK LEISTSDQCL ANTPQDYTDN GKPFTSCSPS QADEDSETTI
LTHDMKHSDT DLSGNSDQES GVADLNCRSP SGGDFLSSDD NKNLSAYSEE LAFAVA
//
