Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-5693-00965
Entry Name
UniProt Accession
Theoretical PI
5.8
Molecular Weight
82017.16
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Phosphoinositide phospholipase C
Protein Synonyms/Alias
3.1.4.11;
Gene Name
plc1
Gene Synonyms/Alias
Created Date
01-MAY-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGLCTSKCN
[1]
N-Myristoylation
Organism
Trypanosoma cruzi
NCBI Taxa ID
5693
Reference
[1] Furuya T, Kashuba C, Docampo R, Moreno SN. A novelphosphatidylinositol-phospholipase C of Trypanosoma cruzi that is lipid modified and activated during trypomastigote to amastigote differentiation. J Biol Chem.2000 Mar 3;275(9):6428-38.[PMID:10692446]
Functional Description
Sequence Annotation
Protein Length
725 AA.
Protein Sequence
(Canonical)
MGLCTSKCNV EDKMCRYAPA AERLVDDFFA QDNEFLGDAG AFFACMWGAS RDILLCSGDE  60
ATAFLRRACF SNPKSEEALN LYLSSSNFGR ALWDLNRAKF MMIWMKYDAD NSGDISLREL  120
GKLVKGLNFP ADLSKQLIAA VKAAGGIVNY AFLEKEYFLL TRLKELEYVF TGVAGPVRET  180
ITRDEFKSFL RNYQGEELNG ERVKEILDYV CCMKTGEVYF TNFLKFLEDN RFCSIVDEEK  240
VSKVYQDMNQ PICNYFINSS HNTYLTGDQL TSNSSADMYR KALLDGCRCV ELDCWDGFAG  300
EPIVYHGHTR TSKISFLSCI KVIKEYAFKA SEYPVILSIE VHTSSAQADR MAEIMCDTFG  360
DMLFQSPWAP AEPTTFLFSP ENLKRKILVK SKRVATSSAI SDAEITENEE EEENDEEEET  420
EGEEKELTTS GPNPLYRQFK EEKKKEEKKK EKKKKIKVAL EKLSRVVSIE SAGFKGTSDM  480
SYLEKRQPYQ CTSFVESKAK KIAVSNAMEF KLINQHCLSR IYPAGSRVGS SNYNPQLFWN  540
CGCQIVALNW QSTHTYAWRL NKGFFSDNGN CGYVLKPESV RSSAASRNGS QVRSLNLEII  600
SGFCLPKPKR SNKGEIVDPF ITCFIEGPDG NSDRKTSGTI RNNGFHPVWR GKGLGTEFSW  660
DVKDWDLSTL VVQVYDEDKK TRDDFLAECI LPLRVLKAGI RQIPLHDING NSIFGSFLTC  720
SLTFS                                                              725
FASTA
(Canonical)
>LipidDB-5693-00965|Q9TZN8
MGLCTSKCNVEDKMCRYAPAAERLVDDFFAQDNEFLGDAGAFFACMWGASRDILLCSGDE
ATAFLRRACFSNPKSEEALNLYLSSSNFGRALWDLNRAKFMMIWMKYDADNSGDISLREL
GKLVKGLNFPADLSKQLIAAVKAAGGIVNYAFLEKEYFLLTRLKELEYVFTGVAGPVRET
ITRDEFKSFLRNYQGEELNGERVKEILDYVCCMKTGEVYFTNFLKFLEDNRFCSIVDEEK
VSKVYQDMNQPICNYFINSSHNTYLTGDQLTSNSSADMYRKALLDGCRCVELDCWDGFAG
EPIVYHGHTRTSKISFLSCIKVIKEYAFKASEYPVILSIEVHTSSAQADRMAEIMCDTFG
DMLFQSPWAPAEPTTFLFSPENLKRKILVKSKRVATSSAISDAEITENEEEEENDEEEET
EGEEKELTTSGPNPLYRQFKEEKKKEEKKKEKKKKIKVALEKLSRVVSIESAGFKGTSDM
SYLEKRQPYQCTSFVESKAKKIAVSNAMEFKLINQHCLSRIYPAGSRVGSSNYNPQLFWN
CGCQIVALNWQSTHTYAWRLNKGFFSDNGNCGYVLKPESVRSSAASRNGSQVRSLNLEII
SGFCLPKPKRSNKGEIVDPFITCFIEGPDGNSDRKTSGTIRNNGFHPVWRGKGLGTEFSW
DVKDWDLSTLVVQVYDEDKKTRDDFLAECILPLRVLKAGIRQIPLHDINGNSIFGSFLTC
SLTFS
Gene Ontology
GO:0005509; F:calcium ion binding; IEA:InterPro
GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC
GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW
GO:0035556; P:intracellular signal transduction; IEA:InterPro
GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW
Interpro
InterPro; IPR000008; C2_dom
InterPro; IPR011992; EF-hand-dom_pair
InterPro; IPR018247; EF_Hand_1_Ca_BS
InterPro; IPR002048; EF_hand_dom
InterPro; IPR001192; PI-PLC_fam
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl
InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom
InterPro; IPR001711; PLipase_C_Pinositol-sp_Y
Pfam
Pfam; PF00168; C2;
Pfam; PF00388; PI-PLC-X;
Pfam; PF00387; PI-PLC-Y;
SMART
SMART; SM00239; C2;
SMART; SM00148; PLCXc;
SMART; SM00149; PLCYc;
PROSITE
PROSITE; PS50004; C2;
PROSITE; PS00018; EF_HAND_1;
PROSITE; PS50222; EF_HAND_2;
PROSITE; PS50007; PIPLC_X_DOMAIN;
PROSITE; PS50008; PIPLC_Y_DOMAIN;
PRINTS
PRINTS; PR00390; PHPHLIPASEC;