ID H3AES8_LATCH Unreviewed; 614 AA.
AC H3AES8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=MTMR7 {ECO:0000313|Ensembl:ENSLACP00000008149.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000008149.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000008149.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; AFYH01107694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01107695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01107696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01107697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01107698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01107699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01107700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01107701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01107702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01107703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AES8; -.
DR Ensembl; ENSLACT00000008215.1; ENSLACP00000008149.1; ENSLACG00000007217.1.
DR GeneTree; ENSGT00940000155777; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000007217; Expressed in chordate pharynx and 2 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd13344; PH-GRAM_MTMR7; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR036003; MTMR7_PH-GRAM.
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 InterPro; IPR000387; Tyr_Pase_dom.
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.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 126..457
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 262..306
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 567..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 474..504
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 567..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 293
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 230..231
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 293..299
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 614 AA; 70860 MW; 99D0DF3A0AA53C90 CRC64;
MDYIRTPKVE NVRLLDRISA RKAAVGTLYL TATHVIFVEN VSETRKETWV LHSQVCSIEK
QATTATGCPL LIRCKNFQVI QLILPQERDC HDVYLSLVRL SHPVKYEELY CFLFNPKLDK
EERKEGWNLI DLKAEYNRMG VLSSLWQIAH VNRDYRVCET YPTELYVPKS ATAPIIVGSS
KFRSRGRFPV LSYYYQDNNL NAIANRAAGK GYENEDNYSN IKFQFIGIEN IHVMRNSLQK
MLEVCELRSP SMSDFLWGLE NSGWLKHIKA ITDAGIFIAK AVAEEGASVL VHCSDGWDRT
AQVCSLASLL LDPYYRTIKG FMVLIEKDWV SFGHKFNHRY SHLDGDPKEV SPVIDQFIEC
VWQLMEQFPC AFEFNERFLI HIHNHIYSCQ FGNFICNNQK ESSELRIQER TFSLWAHLWK
NREDYINPLY RPDHSQTQGL LRPDTAPYNF KFWRSMYNRF EKVMHPRQSV NDFLMAVKEE
TQQLEEELEN LDEKLAKIEK LHLRSIKLKT KQRERNHHVG LSISNNALAN TPQDYSGSLG
MFPSRSPSQV VEDDASFILT KENLKVSDPD LSTNSDQESG VADLNCRSPS GGDFLPSEDS
GKDQDSDEAV FLAV
//
