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Database: UniProt
Entry: A0A2G5UFV1_9PELO
LinkDB: A0A2G5UFV1_9PELO
Original site: A0A2G5UFV1_9PELO 
ID   A0A2G5UFV1_9PELO        Unreviewed;       898 AA.
AC   A0A2G5UFV1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
GN   Name=Cni-mtm-3 {ECO:0000313|EMBL:PIC38432.1};
GN   Synonyms=Cnig_chr_III.g10448 {ECO:0000313|EMBL:PIC38432.1};
GN   ORFNames=B9Z55_010448 {ECO:0000313|EMBL:PIC38432.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC38432.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PIC38432.1}.
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DR   EMBL; PDUG01000003; PIC38432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5UFV1; -.
DR   Proteomes; UP000230233; Chromosome iii.
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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00065; FYVE_like_SF; 1.
DR   CDD; cd14507; PTP-MTM-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR003595; Tyr_Pase_cat.
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:SF75; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          159..566
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   DOMAIN          748..813
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          581..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          663..690
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        399
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         337..338
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         399..405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   898 AA;  101674 MW;  F20F304A40AFBEAB CRC64;
     MSNDVLPETL HEANYQFGNP MPSVKEEDEN DFPLLPGECR VKVDGANDWP IIGGTIIVTN
     YRVVTIKISE DKKRVHIFPI SEIETMDMSN DNSIHLLMKG GRSTYLYCNN QKDAYFIHQL
     IMPALQRLNR SATVLYATRP QDWTSKNETA PLAAVNHFAW SFSEAVDELE RCGQLPSWLK
     RADSVAYEIT QVDFERLGMS EHFRISTVNS TFKVCPTYPE KVIVPKGISD EEIAISAPYR
     SIGRFPAVIW RCRKTRAVLL RSSQPQVGIL SWRNTTDERI IEEVVRTSRI EGEERKQFII
     MDARGYASAF ANRARSGGFE NTEYYQQAKL EFLGLPNIHA VRSSFTNIRT MLHAPVKENE
     LLLNSLQATG WLTNLSSLLV QATSCADHLA KGHSVLVHCS DGWDRTTQVT TLAKIMLDEH
     YRTVEGFEEL IRRDWIAFGH KLYDRQIGTY TTWSDSGERC PIFLQFLEAV RHLQREQPTA
     FQFSHAYLIK LAKHAYSGLF GTFLFNSHKE KRDAMTKWDA TLVEIWRYIG AHNEEFVNQS
     YDERYIGPLK TINVSIINLR VWHEVFADEG ERYTMIYSSK DERPSSGCAT PITSSSSGNL
     VKSKSSESIN SLNVDGSNHQ LANASTPATT EGGNLPLSTS FYQQQSIYQS NITGLESIDC
     DGLTKFEDEE QAMLRKKNKA REEAIRLRDR QIEELRRRAD IEKMLSPIRG DADDSDIDVA
     SLERASSDLS IMDPDRELPN FRPNTTWEAE APNCCLCKKE FNKMSVYQED RQHHCRNCGR
     VVCEECSKQR FAVVEEGQSV QKRVCDKCYE SMHEPEPRLN RTASLSEMSS FDSTSCGPTF
     PHASSPSSSS LNMLTSISSP TRPQPVPSSC KSSSNSISSP RPSPGEFSRH SSSQAVKG
//
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