ID   PHLC_TRYBB              Reviewed;         358 AA.
AC   P09194; Q7KA50;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Variant-surface-glycoprotein phospholipase C;
DE            Short=VSG lipase;
DE            EC=4.6.1.14;
DE   AltName: Full=Glycosylphosphatidylinositol-specific phospholipase C;
DE            Short=GPI-PLC;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2523022; DOI=10.1016/0166-6851(89)90091-1;
RA   Carrington M., Buelow R., Reinke H., Overath P.;
RT   "Sequence and expression of the glycosyl-phosphatidylinositol-specific
RT   phospholipase C of Trypanosoma brucei.";
RL   Mol. Biochem. Parasitol. 33:289-296(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ILTAT 1.3;
RX   PubMed=3194399; DOI=10.1073/pnas.85.23.8914;
RA   Hereld D., Hart G.W., Englund P.T.;
RT   "cDNA encoding the glycosyl-phosphatidylinositol-specific phospholipase C
RT   of Trypanosoma brucei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:8914-8918(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=STIB 367H / ILTAR1;
RX   PubMed=9719514; DOI=10.1016/s0166-6851(98)00056-5;
RA   Redpath M.B., Carnall N., Webb H., Courel M., Amorim A., Guther M.L.S.,
RA   Cardoso de Almeida M.L., Carrington M.;
RT   "Conservation of genetic linkage between heat shock protein 100 and
RT   glycosylphosphatidylinositol-specific phospholipase C in Trypanosoma brucei
RT   and Trypanosoma cruzi.";
RL   Mol. Biochem. Parasitol. 94:113-121(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11377739; DOI=10.1016/s0166-6851(01)00268-7;
RA   Maier A.G., Webb H., Ding M., Bremser M., Carrington M., Clayton C.;
RT   "The coatomer of Trypanosoma brucei.";
RL   Mol. Biochem. Parasitol. 115:55-61(2001).
CC   -!- FUNCTION: By hydrolysis of the attached glycolipid, releases soluble
CC       variant surface glycoprotein containing phosphoinositol from the cell
CC       wall of T.brucei after cell lysis. It also cleaves similar membrane
CC       anchors on some mammalian proteins. VSG lipase may play a role in
CC       processes such as parasite differentiation or antigenic variation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-
CC         myo-inositol = 6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic
CC         phosphate + a 1,2-diacyl-sn-glycerol; Xref=Rhea:RHEA:14333,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:57997, ChEBI:CHEBI:58891; EC=4.6.1.14;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- PTM: The N-terminus is blocked.
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DR   EMBL; X13292; CAA31654.1; -; mRNA.
DR   EMBL; J04124; AAA30230.1; -; mRNA.
DR   EMBL; AJ000080; CAA03907.1; -; Genomic_DNA.
DR   EMBL; AJ250726; CAB60085.1; -; Genomic_DNA.
DR   PIR; A31254; A31254.
DR   PIR; S03389; S03389.
DR   AlphaFoldDB; P09194; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:GeneDB.
DR   GO; GO:0047396; F:glycosylphosphatidylinositol diacylglycerol-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004629; F:phospholipase C activity; TAS:GeneDB.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IMP:GeneDB.
DR   GO; GO:0006507; P:GPI anchor release; TAS:GeneDB.
DR   GO; GO:0006629; P:lipid metabolic process; IMP:GeneDB.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SUPFAM; SSF51695; SSF51695; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Membrane.
FT   CHAIN           1..358
FT                   /note="Variant-surface-glycoprotein phospholipase C"
FT                   /id="PRO_0000088483"
FT   DOMAIN          25..198
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   CONFLICT        102
FT                   /note="I -> V (in Ref. 2; AAA30230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="S -> R (in Ref. 2; AAA30230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="T -> N (in Ref. 2; AAA30230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="G -> S (in Ref. 2; AAA30230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="K -> Q (in Ref. 2; AAA30230)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   358 AA;  40663 MW;  237E7D738D540C60 CRC64;
     MFGGVKWSPQ SWMSDTRSSI EKKCIGQVYM VGAHNAGTHG IQMFSPFGLD APEKLRSLPP
     YVTFLLRFLT VGVSSRWGRC QNLSIRQLLD HGVRYLDLRM NISPDQENKI YTTHFHISVP
     LQEVLKDVKD FLTTPASANE FVILDFLHFY GFNESHTMKR FVEELQALEE FYIPTTVSLT
     TPLCNLWQST RRIFLVVRPY VEYPYARLRS VALKSIWVNQ MELNDLLDRL EELMTRDLED
     VSIGGVPSKM YVTQAIGTPR NNDFAVAACC GACPGSHPDL YSAAKHKNPH LLKWFYDLNV
     NGVMRGERVT IRRGNNTHGN ILLLDFVQEG TCTVKGVDKP MNAVALCVHL NTNQTARS