ID A0A016VNA3_9BILA Unreviewed; 1316 AA.
AC A0A016VNA3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
GN Name=Acey_s0007.g3253 {ECO:0000313|EMBL:EYC28492.1};
GN Synonyms=Acey-plc-3 {ECO:0000313|EMBL:EYC28492.1};
GN ORFNames=Y032_0007g3253 {ECO:0000313|EMBL:EYC28492.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC28492.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000256|RuleBase:RU361133};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC28492.1}.
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 EMBL; JARK01001343; EYC28492.1; -; Genomic_DNA.
DR STRING; 53326.A0A016VNA3; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR035024; PLC-gamma_N-SH2.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10336:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 555..654
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 665..754
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 780..838
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 930..1040
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1037..1168
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 27..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1316 AA; 149411 MW; F721C95BAE414595 CRC64;
MSNLTFTTQS WGLKGLFVAG EQRASNGPPE MVVGGPARKT TVSSGPSPGT LRGYNKHQEM
DFAKIYLAMQ KGHKVCKINV LKKWDPAYKL LTLNMDTRQL FLAKLEQAAV RSKPTLLDLR
HVREVQTLDY KLSAIQIGDK WKKDREIQNF DPLKILVISY GTQFTLKEWT LLFESAEACR
LWNVGVHNLM LDTRDRFSSS HCARVERFIA KHFYSLVTPG SEFVARKHMK PFVQTSLQYK
VSSRQLQEVT EDQMNLLQFS KATRNFIHSQ PLFMSRFAEL SQDAETVTFD DFMRFLENMQ
RDDMVSNRTR VVDFLRRYLT GDQLRSESSL DSYAQALLMG CRCIELDCWD GQRKPNSQEF
QDIVIYHGYT MTSKLLLRDV LYVIKHYAFI TSVYPVILSI EDNCSVPAQR LLAQEIKEIL
GDDLLTQPIN PSETELPSPA ALKKKIILKH KKLPIENEDL ATFVSASTDE FQDTDILARE
CIKKGMLSLM DSVRHEWSSH VFILFPDRLC YLLDSCDDSA MKDDSVSMMG DDDREEDTLS
EFGVRPEEQH ITEEWFHGHC GRDEARNRIL EHKDKGNGLF MVRDSNLFLG DFSLTILHEG
NVHHVRIKTR IVDKEKKYYF MDNKVCDTLY ELVSYYTRHY LTTPTFKMAL TTPCPQPQPH
LGQPWFSETA DKEKAEALLS QVPEDGAFLL RYSSSDKNVF VLSIRVDGEI WHYRLKRDGR
IFVVNQTVFE NLNQIVEYYR SREFVRGISL RIPVNENDMS AIPAHLEIAR GSYQELSQLE
EKVLARALRP YRGTGEDDLS FPANAIITVL RKEEALWTGR YGSSVGWFPA SYVQEILPEK
TTTSGVASNY NTIELAGTVI ERVTDGEKQH VIKISHSAQQ WSGQQWLLAA RSVEEADDWQ
NQLWDLTRSV NNKISVLRTK EKSARIAAEL SNLVVYCQAV PFDPAHVNGG SFYEMCSFVE
NKLDRLLEKG LISFNVRQLS RVYPHGSRIT SANYNPVPMW NASCHMVALN YQTGDKPMQL
NQGKFMGNGR CGYVLKPEYM LEEGFDPSRP ESVTTSCPVR LTVQVIAGRH LSRRDKHKGI
CSPFVEVEVI GLPCDEAIFK TRTIASNGLN PTWNQTAVFD VTCPEVALLR FHVEDGDFVG
PKTDPFIGQA VFPLDCIRCG FRSVPLLNQF SEELELSSLL VDVQMIALAD SSLVRSAHTI
LQSSRMAPVF RSKDRKLRSF DSVASSASLA SPSVPREITP RPVVSSGLSS SVDSQSPSAT
SIATRKFSAF QSQDSVDSAD SMSPSSNGTI SSEKDKKRGK WGFPGFRFRS KDKDHG
//
