ID A0A1S3WJS7_ERIEU Unreviewed; 1172 AA.
AC A0A1S3WJS7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=MTMR3 {ECO:0000313|RefSeq:XP_016046394.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016046394.1};
RN [1] {ECO:0000313|RefSeq:XP_016046394.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 ---------------------------------------------------------------------------
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_016046394.1; XM_016190908.1.
DR AlphaFoldDB; A0A1S3WJS7; -.
DR CTD; 8897; -.
DR eggNOG; KOG4471; Eukaryota.
DR InParanoid; A0A1S3WJS7; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000079721; Unplaced.
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; cd15732; FYVE_MTMR3; 1.
DR CDD; cd13341; PH-GRAM_MTMR3; 1.
DR CDD; cd14586; PTP-MTMR3; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035888; MTMR3_PH-GRAM.
DR InterPro; IPR046352; MTMR3_PTP.
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:SF66; MYOTUBULARIN-RELATED PROTEIN 3; 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 SUPFAM; SSF50729; PH domain-like; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 155..576
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1093..1153
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1009..1036
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 697..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 326..329
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 351..352
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 413..419
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1172 AA; 129042 MW; 79E37E8756582C07 CRC64;
MDEESPHNLE CIQANRIFPR KQLVREDETL QVPFLELHGE STEYVGRAED AVIALSNYRL
HIKFKESLVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ FSTFEQCQEW LKRLNSAIRP
PTRIEDLFSF AYHAWCLEVY ASEKEQHGDL CRPGEHVSSR FKNEVERMGF DMNNAWRISN
INEKYRLCGS YPQELIVPAW ITDKELESVA GFRSWKRLPA VVYRHQSNGA VIARCGQPEV
SWWGWRNADD EHLVQSVAKA CACDSQSSGS KPPTRSSTRD FANTGDLSDA EFDSSLSNAS
GTESLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA NIHSIRRSFQ
SLRLLCTQMP DPGNWLSALE GTKWLHHLSV LLKSALLAVH AVDRDQRPVL VHCSDGWDRT
PQIVALAKLL LDPYYRTIEG FQVLVETEWL DFGHKFADRC GHGESAGDLS ERCPVFLQWL
DCVHQLQRQF PCSFAFNEAF LVKLVQHTYS CLFGTFLCNN AKERGERHTR ERTCSVWSLL
RAGNKAFGNL LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPSTPVDESC APYPAPATAP
DDPPLSRLPK TRSFDNLPVV CDNTVPLASR RCSDPSLNEK WQEQRRSLEL SSLACAGEEP
PGADGLGRPA RLPGSAELSV AAGVTEGQME NILQEATKEE SGLEEPAHGR GSEVRVPERR
EETQSEQERW GETPEGSAIA SHREPGPDTA VPRSLPSPGL ALALASQGLP EQQGGLGRHS
ASPQEPCRGE GGRAVPEEPP GDGGEALLPA LLDAKADCGA SAPSSLPPSQ APAETRGPST
GSPVGTLAEN KGEPEGEPRD HHRPSLVSSG RFGGRDRLPE VTEPKPLERS PAERPQAGCV
VHRTPPGGGH GPTPAPCAVP SSGCKEGPVC NGIPEMENKV SEKPPAPGET VGSKDTLGHQ
LPATSCGSVP GHARSAQHKW RPSAACSHLD DDGMPVYTDT IQQRLRQIES GHQQEVETLK
KQVQELRSRL ESQYLASSLR FNGDFGDEVT SVPDSESSVD QNCLSRCSTE LFSEASWEQV
DKQDTEMTRW LPDHLAAHCY ACDSAFWLAS RKHHCRNCGN VFCSSCCNQK VPVPSQQLFE
PSRVCKSCYS SLRPTSSSID LELDKPIAAT SN
//
