PLIP_DICDI
ID PLIP_DICDI Reviewed; 232 AA.
AC Q86IG3; Q559B2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phospholipid-inositol phosphatase {ECO:0000303|PubMed:12878591};
DE Short=PLIP {ECO:0000303|PubMed:12878591};
DE EC=3.1.3.- {ECO:0000269|PubMed:12878591};
DE AltName: Full=5-Phosphatidylinositol phosphatase {ECO:0000303|PubMed:12878591};
GN Name=plip {ECO:0000303|PubMed:12878591};
GN ORFNames=DDB0185057 {ECO:0000312|EMBL:EAL71055.1};
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:AAQ24381.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX3 {ECO:0000312|EMBL:AAQ24381.1};
RX PubMed=12878591; DOI=10.1074/jbc.m306318200;
RA Merlot S., Meili R., Pagliarini D.J., Maehama T., Dixon J.E., Firtel R.A.;
RT "A PTEN-related 5-phosphatidylinositol phosphatase localized in the
RT Golgi.";
RL J. Biol. Chem. 278:39866-39873(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP MISCELLANEOUS.
RX PubMed=25180230; DOI=10.15252/embj.201488677;
RA Clark J., Kay R.R., Kielkowska A., Niewczas I., Fets L., Oxley D.,
RA Stephens L.R., Hawkins P.T.;
RT "Dictyostelium uses ether-linked inositol phospholipids for intracellular
RT signalling.";
RL EMBO J. 33:2188-2200(2014).
CC -!- FUNCTION: Exhibits phosphatidylinositol-phosphate phosphatase activity.
CC Has a preference for phosphatidylinositol 5-phosphate (1,2-diacyl-sn-
CC glycero-3-phospho-(1D-myo-inositol-5-phosphate)) in vitro
CC (PubMed:12878591). May be involved in membrane trafficking by
CC dephosphorylating phosphatidylinositides (PubMed:12878591).
CC {ECO:0000269|PubMed:12878591, ECO:0000303|PubMed:12878591}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:41147, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57795, ChEBI:CHEBI:57880;
CC Evidence={ECO:0000269|PubMed:12878591};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41148;
CC Evidence={ECO:0000269|PubMed:12878591};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42308, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78911;
CC Evidence={ECO:0000269|PubMed:12878591};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42309;
CC Evidence={ECO:0000269|PubMed:12878591};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-2-acyl-sn-glycero-3-phospho-(1'-myo-inositol-5'-
CC phosphate) + H2O = 1-O-alkyl-2-acyl-sn-glycero-3-phospho-1D-myo-
CC inositol + phosphate; Xref=Rhea:RHEA:67744, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65218, ChEBI:CHEBI:173076;
CC Evidence={ECO:0000305|PubMed:12878591};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67745;
CC Evidence={ECO:0000305|PubMed:12878591};
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:12878591}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12878591}.
CC -!- DISRUPTION PHENOTYPE: Mutants fail to aggregate to form a multicellular
CC organism under conditions of low cell density.
CC {ECO:0000269|PubMed:12878591}.
CC -!- MISCELLANEOUS: Dictyostelium phosphatidylinositol phosphates (PIPs) are
CC unusual, with the lipid chain joined to the sn-1-position of the
CC glycerol backbone by an ether, rather than ester linkage. The
CC composition of the inositol phospholipids in Dictyostelium is
CC strikingly biased, over 95% of the PI, PIP and PIP2 pools contain the
CC C34:1e structure, with an ether-linked C16:0 chain (palmityl or
CC hexadecyl) in the sn-1 position and an ester-linked C18:1 chain (11-
CC octadecenoyl) in the sn-2 position. {ECO:0000269|PubMed:25180230}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AAFI01000022; EAL71055.1; -; Genomic_DNA.
DR EMBL; AY347275; AAQ24381.1; -; mRNA.
DR RefSeq; XP_644904.1; XM_639812.1.
DR AlphaFoldDB; Q86IG3; -.
DR SMR; Q86IG3; -.
DR STRING; 44689.DDB0185057; -.
DR SwissLipids; SLP:000000845; -.
DR PaxDb; Q86IG3; -.
DR GeneID; 8618583; -.
DR KEGG; ddi:DDB_G0272835; -.
DR dictyBase; DDB_G0272835; plip.
DR eggNOG; KOG1719; Eukaryota.
DR HOGENOM; CLU_047330_2_0_1; -.
DR InParanoid; Q86IG3; -.
DR OMA; TENATRC; -.
DR PhylomeDB; Q86IG3; -.
DR PRO; PR:Q86IG3; -.
DR GO; GO:0000139; C:Golgi membrane; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:dictyBase.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:dictyBase.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR CDD; cd14524; PTPMT1; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR044596; PTPMT1-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Hydrolase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Protein phosphatase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..232
FT /note="Phospholipid-inositol phosphatase"
FT /id="PRO_0000453675"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 77..222
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 166
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 232 AA; 26622 MW; 47981B715790FF69 CRC64;
MNENEGIIIE NINNDSGSTY LMNILGILIP IKIVVTIYLF SKARLPVGFA RYFGRLYHFM
TNPIRLGLQI AGLRGPFISQ LDDNVYLGAM PMGSDVTLLF YKYKINSIVN LCDEYQGPTQ
HYTQYGMQQL YVPVVDHFEP DVEIIEKSIQ FILKQIELGN RVYIHCKAGR GRSGAIAICW
IAYSRRVSLE VAQKILLEKR KIVRKQLYKQ KNVNQYYSSY CLNSNINSTT SI
