ID   A0A455APE6_PHYMC        Unreviewed;       692 AA.
AC   A0A455APE6;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   Name=MTMR8 {ECO:0000313|RefSeq:XP_028338452.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028338452.1};
RN   [1] {ECO:0000313|RefSeq:XP_028338452.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028338452.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_028338452.1; XM_028482651.1.
DR   AlphaFoldDB; A0A455APE6; -.
DR   STRING; 9755.ENSPCTP00005008382; -.
DR   Ensembl; ENSPCTT00005009232; ENSPCTP00005008382; ENSPCTG00005005857.
DR   KEGG; pcad:102992691; -.
DR   InParanoid; A0A455APE6; -.
DR   OrthoDB; 5474662at2759; -.
DR   Proteomes; UP000248484; Chromosome 21.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016241; P:regulation of macroautophagy; IEA:Ensembl.
DR   CDD; cd14584; PTP-MTMR8; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR030591; MTMR8_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:SF36; MYOTUBULARIN-RELATED PROTEIN 8; 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   Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT   DOMAIN          126..500
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
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   692 AA;  77713 MW;  65F53FC49CDE5A49 CRC64;
     MDHITVPKVE NVKLLDRYVG KKPANGSLYL TATHLIYVEA SGAARKETWI ALHHIATVEK
     LSITSLGCPL ILHCKNFRVA HFVLESDVVC HEVYISLLKL SQPALHEDLY AFSYNPKSSK
     EMRENGWKLI DPISDFGRMG LPNRYWTITD ANRNYEICST YPPEIVVPKS VTLGTVAGSS
     KFRSKERVPV LSYLYKENNA AICRCSQPLS GFYTRCIDDE LLLEAISQTN PGSQFMYVVD
     TRPKLNAMAN RAAGKGYENE DNYANIRFRF MGIENIHVMR NSLQKLLEVC ELKTPTMSEF
     LSGLESSGWL RHIKAIMDAG IFIAKAVKVE KTNVLVHCSD GWDRTAQVCS VASILLDPFY
     RTFKGLMILI EKEWISMGHK FSQRCGHLDG DSKEVSPIFT QFLDCIWQLM EQFPCAFEFN
     ENFLLEIHDH VFSCQFGNFL GNCQKDREDL RIYEKTHSVW PFLVQRKPDF RNPLYKGFTV
     YGVLNPSTVP YNIQFWCGMY NRFDKGLQPK QSMLESLLEI KKQRSMLEAD VHKLEKKVKA
     HDEPPEEVCT CSQLGRLLSQ HLGTPLTNPL GFMGIDGDLN TLMENGTLSR EGGLRVQMDQ
     VKNQCADLHP DYYGTMGNLR AINISGDVGF SGDTGISGVS GISGNTGTSE AMGFYEDISI
     SGAMSFSGTT GISEDTGLSK AITKGAGFSK QQ
//