PHLC_TRYCR
ID PHLC_TRYCR Reviewed; 380 AA.
AC O15886;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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 (By
CC similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
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DR EMBL; AJ000079; CAA03904.1; -; Genomic_DNA.
DR AlphaFoldDB; O15886; -.
DR PRIDE; O15886; -.
DR VEuPathDB; TriTrypDB:BCY84_05557; -.
DR VEuPathDB; TriTrypDB:C3747_94g187; -.
DR VEuPathDB; TriTrypDB:C4B63_9g417; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_9648; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0101930; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM05365; -.
DR VEuPathDB; TriTrypDB:TcCLB.506821.30; -.
DR VEuPathDB; TriTrypDB:TcCLB.508765.30; -.
DR VEuPathDB; TriTrypDB:TCDM_08177; -.
DR VEuPathDB; TriTrypDB:TcG_07569; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_000264; -.
DR VEuPathDB; TriTrypDB:TcYC6_0077870; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047396; F:glycosylphosphatidylinositol diacylglycerol-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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 SMART; SM00148; PLCXc; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE 3: Inferred from homology;
KW Lyase; Membrane.
FT CHAIN 1..380
FT /note="Variant-surface-glycoprotein phospholipase C"
FT /id="PRO_0000088484"
FT DOMAIN 31..205
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
SQ SEQUENCE 380 AA; 42737 MW; 273CD402B52068C5 CRC64;
MLPESDDFTN TAWHPQSWMH DLRSFIGEMA ITQVCFVGSH DAASYGVSKD SPFGADAPGF
LLGDSVFASL LRFLFRGICA SWSRCQWMSV RAQLNHGVRY LDMRVATNPE DASRLYTLHH
QISVPLADVL EDVKAFLNDP LSADEFIVLD FQHLYLTDDS DGKGKFFREL DRLSDRFIPV
DVPLTTPLEF LWRASSRRRI FLVVGSGEDE SPYPAARIRS KCMVSRWVNE NSLRKLLEAL
DNLLLDDLKY PQTGVPSKLY VTQAVFTPRY SDIFLGIFPK ISRRVVSSIY DVATRVNPSL
LEWFYSLNAR GLLDGMKVMI PSGINTHGNI FMLDCVELGS CQIMDGTTET NAVGMCVYLN
ILRASRLFED SSAAPSLNEG
