ID A0A2U3Y387_LEPWE Unreviewed; 621 AA.
AC A0A2U3Y387;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=MTMR6 {ECO:0000313|RefSeq:XP_006738185.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006738185.1};
RN [1] {ECO:0000313|RefSeq:XP_006738185.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006738185.1};
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}.
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 RefSeq; XP_006738185.1; XM_006738122.2.
DR AlphaFoldDB; A0A2U3Y387; -.
DR STRING; 9713.A0A2U3Y387; -.
DR GeneID; 102750058; -.
DR KEGG; lww:102750058; -.
DR CTD; 9107; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000245341; Unplaced.
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; cd13343; PH-GRAM_MTMR6; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR035998; MTMR6_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 PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF34; MYOTUBULARIN-RELATED PROTEIN 6; 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:UP000245341}.
FT DOMAIN 124..499
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT COILED 516..543
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 336
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 273..274
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 336..342
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 621 AA; 72088 MW; 6CB169E3D18282D1 CRC64;
MEHIRTTKVE QVKLLDRFST SNKSLTGTLY LTATHLLFID SHQKETWILH HHIALVEKLA
LTTSGCPLVI QCKNFRIVHF IVPRERDCHD IYNSLLQLSK QAKYEDLYAF SYNPKQNDSE
RLQGWQLIDL AEEYKRMGVP NSNWQLSDAN REYKICETYP RELYVPRIAS KPIIVGSSKF
RSKGRFPVLS YYHQNKEAAI CRCSQPLSGF SARCLEDEHL LQAISKANPV NRYMYVMDTR
PKLNAMANRA AGKGYENEDN YSNIRFQFVG IENIHVMRSS LQKLLEVNGT KGLSVSDFYS
GLESSGWLRH IKAVMDAAIF LAKAIMVENA SVLVHCSDGW DRTSQVCSLG SLLLDSYYRT
IKGFMVLIEK DWISFGHKFS ERCGHLDGDP KEVSPVFTQF LECVWHLTEQ FPQDFEFNEA
FLLQIHEHIH SCQFGNFLGN CQKEREELKL KEKTYSLWPF LLDDQKKYLN PLYSSKSPKF
AVLEPNTVSF SFKFWRNMYH QFDRTLHPRQ SVFNIIMNMN EQNKRLEKDI KDLESKIKQR
KNKQTDEILT KELLHSVHPE SPTLKTSLCF KEQTLLPVNH ALRTIEGSNP ADNRYSEYAE
EFSKSEPGVV NLEYGVARMT C
//
